Monitoring base excision repair in Chlamydomonas reinhardtii cell extracts
•Base excision repair can be detected in cells extracts of Chlamydomonas reinhardtii.•An uracil DNA glycosylase belonging to Family-1 initiates BER of uracil.•Abasic sites may be processed both by AP lyases and AP endonucleases.•Full repair occurs by both single-nucleotide insertion and long-patch D...
Saved in:
| Published in: | DNA repair Vol. 65; pp. 34 - 41 |
|---|---|
| Main Authors: | , , , , , |
| Format: | Journal Article |
| Language: | English |
| Published: |
Netherlands
Elsevier B.V
01-05-2018
|
| Subjects: | |
| Online Access: | Get full text |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| Abstract | •Base excision repair can be detected in cells extracts of Chlamydomonas reinhardtii.•An uracil DNA glycosylase belonging to Family-1 initiates BER of uracil.•Abasic sites may be processed both by AP lyases and AP endonucleases.•Full repair occurs by both single-nucleotide insertion and long-patch DNA synthesis.
Base excision repair (BER) is a major defense pathway against spontaneous DNA damage. This multistep process is initiated by DNA glycosylases that recognise and excise the damaged base, and proceeds by the concerted action of additional proteins that perform incision of the abasic site, gap filling and ligation. BER has been extensively studied in bacteria, yeasts and animals. Although knowledge of this pathway in land plants is increasing, there are no reports detecting BER in algae. We describe here an experimental in vitro system allowing the specific analysis of BER in the model alga Chlamydomonas reinhardtii. We show that C. reinhardtii cell-free extracts contain the enzymatic machinery required to perform BER of ubiquitous DNA lesions, such as uracil and abasic sites. Our results also reveal that repair can occur by both single-nucleotide insertion and long-patch DNA synthesis. The experimental system described here should prove useful in the biochemical and genetic dissection of BER in algae, and may contribute to provide a broader picture of the evolution and biological relevance of DNA repair pathways in photosynthetic eukaryotes. |
|---|---|
| AbstractList | •Base excision repair can be detected in cells extracts of Chlamydomonas reinhardtii.•An uracil DNA glycosylase belonging to Family-1 initiates BER of uracil.•Abasic sites may be processed both by AP lyases and AP endonucleases.•Full repair occurs by both single-nucleotide insertion and long-patch DNA synthesis.
Base excision repair (BER) is a major defense pathway against spontaneous DNA damage. This multistep process is initiated by DNA glycosylases that recognise and excise the damaged base, and proceeds by the concerted action of additional proteins that perform incision of the abasic site, gap filling and ligation. BER has been extensively studied in bacteria, yeasts and animals. Although knowledge of this pathway in land plants is increasing, there are no reports detecting BER in algae. We describe here an experimental in vitro system allowing the specific analysis of BER in the model alga Chlamydomonas reinhardtii. We show that C. reinhardtii cell-free extracts contain the enzymatic machinery required to perform BER of ubiquitous DNA lesions, such as uracil and abasic sites. Our results also reveal that repair can occur by both single-nucleotide insertion and long-patch DNA synthesis. The experimental system described here should prove useful in the biochemical and genetic dissection of BER in algae, and may contribute to provide a broader picture of the evolution and biological relevance of DNA repair pathways in photosynthetic eukaryotes. Base excision repair (BER) is a major defense pathway against spontaneous DNA damage. This multistep process is initiated by DNA glycosylases that recognise and excise the damaged base, and proceeds by the concerted action of additional proteins that perform incision of the abasic site, gap filling and ligation. BER has been extensively studied in bacteria, yeasts and animals. Although knowledge of this pathway in land plants is increasing, there are no reports detecting BER in algae. We describe here an experimental in vitro system allowing the specific analysis of BER in the model alga Chlamydomonas reinhardtii. We show that C. reinhardtii cell-free extracts contain the enzymatic machinery required to perform BER of ubiquitous DNA lesions, such as uracil and abasic sites. Our results also reveal that repair can occur by both single-nucleotide insertion and long-patch DNA synthesis. The experimental system described here should prove useful in the biochemical and genetic dissection of BER in algae, and may contribute to provide a broader picture of the evolution and biological relevance of DNA repair pathways in photosynthetic eukaryotes. |
| Author | Vázquez‐Grande, Vanessa M. Romero-Valenzuela, Álvaro C. Morales-Ruiz, Teresa Ariza, Rafael R. Roldán-Arjona, Teresa Córdoba‐Cañero, Dolores |
| Author_xml | – sequence: 1 givenname: Teresa surname: Morales-Ruiz fullname: Morales-Ruiz, Teresa organization: Instituto Maimónides de Investigación Biomédica de Córdoba (IMIBIC), Spain – sequence: 2 givenname: Álvaro C. surname: Romero-Valenzuela fullname: Romero-Valenzuela, Álvaro C. organization: Departamento de Genética, Facultad de Ciencias, Universidad de Córdoba, Spain – sequence: 3 givenname: Vanessa M. surname: Vázquez‐Grande fullname: Vázquez‐Grande, Vanessa M. organization: Departamento de Genética, Facultad de Ciencias, Universidad de Córdoba, Spain – sequence: 4 givenname: Teresa surname: Roldán-Arjona fullname: Roldán-Arjona, Teresa organization: Instituto Maimónides de Investigación Biomédica de Córdoba (IMIBIC), Spain – sequence: 5 givenname: Rafael R. orcidid: 0000-0002-0338-7306 surname: Ariza fullname: Ariza, Rafael R. organization: Instituto Maimónides de Investigación Biomédica de Córdoba (IMIBIC), Spain – sequence: 6 givenname: Dolores surname: Córdoba‐Cañero fullname: Córdoba‐Cañero, Dolores email: b72cocad@uco.es organization: Instituto Maimónides de Investigación Biomédica de Córdoba (IMIBIC), Spain |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/29547780$$D View this record in MEDLINE/PubMed |
| BookMark | eNp9kMtOwzAQRS0E4lH4A4SyZNNgO_EjGyRU8RSIDawtxx5TV41d7BTB3-OqwJLVjEb33pk5R2g3xAAInRJcE0z4xaK2QSdY1RQTWWNaY0J20CFhXE6FZHz3r-ftATrKeYExYYLzfXRAO9YKIfEheniKwY8x-fBW9TpDBZ_GZx9DVaK1T5UP1Wy-1MOXjUMMOpe5D3Od7Oh9ZWC5LI4xaTPmY7Tn9DLDyU-doNeb65fZ3fTx-fZ-dvU4Na1ox6lrLBdMGKuFIUZyjHlnHAhwutfMSEEd5bZvZNNg11vHjBUdJ1JgRyhtumaCzre5qxTf15BHNfi8uUQHiOusCo-2Y5gSVqTtVmpSzDmBU6vkB52-FMFqQ1Et1JbixiUVpqpQLLaznw3rfgD7Z_rFVgSXWwGUPz88JJWNh2DA-gRmVDb6_zd8Ayv9h9o |
| CitedBy_id | crossref_primary_10_1007_s11103_023_01407_8 crossref_primary_10_3389_fpls_2019_01055 crossref_primary_10_3390_ijms241914746 crossref_primary_10_1016_j_jphotochemrev_2019_100322 crossref_primary_10_1111_1462_2920_14788 |
| Cites_doi | 10.1093/nar/18.17.5069 10.1126/science.1143609 10.1371/journal.pone.0004297 10.1074/jbc.275.6.4460 10.1021/bi9910878 10.1074/jbc.M411864200 10.1016/j.dnarep.2013.02.001 10.1128/MCB.12.4.1605 10.1074/jbc.M112.427617 10.1111/tpj.12588 10.1093/nar/22.22.4673 10.1093/nar/gki780 10.1021/bi962281m 10.1111/j.1365-313X.2009.03994.x 10.1093/mutage/gel020 10.1016/j.biochi.2008.07.005 10.1038/sj.onc.1205996 10.1111/j.1432-1033.2004.04214.x 10.1128/MCB.13.2.1051 10.1038/45843 10.1016/j.molcel.2011.11.034 10.1038/383735a0 10.1371/journal.pone.0109160 10.1016/S0960-9822(99)80087-6 10.1073/pnas.94.24.12863 10.1016/S0021-9258(19)85067-6 10.1093/nar/gkm372 10.1074/jbc.274.34.24176 10.1093/emboj/16.11.3341 10.1073/pnas.71.9.3649 10.1016/0167-4781(84)90021-6 10.1093/nar/30.10.2124 10.1016/j.molcel.2004.06.003 10.1074/jbc.M109.067173 10.1093/nar/gkh851 10.1074/jbc.274.47.33696 10.1007/978-1-61779-998-3_18 10.1111/j.1574-6976.2009.00188.x 10.1016/j.dnarep.2008.07.012 10.1111/j.1365-313X.2011.04720.x 10.1074/jbc.273.33.21203 10.1038/362709a0 10.1104/pp.107.101980 10.1016/0378-1119(91)90030-F 10.1016/S0921-8777(00)00025-2 10.1021/bi0492612 10.1016/j.dnarep.2004.10.004 10.1016/j.dnarep.2006.10.008 10.1016/j.dnarep.2007.09.009 10.1101/cshperspect.a012583 10.1016/0092-8674(95)90467-0 10.1074/jbc.272.38.23970 |
| ContentType | Journal Article |
| Copyright | 2018 Elsevier B.V. Copyright © 2018 Elsevier B.V. All rights reserved. |
| Copyright_xml | – notice: 2018 Elsevier B.V. – notice: Copyright © 2018 Elsevier B.V. All rights reserved. |
| DBID | CGR CUY CVF ECM EIF NPM AAYXX CITATION 7X8 |
| DOI | 10.1016/j.dnarep.2018.02.011 |
| DatabaseName | Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed CrossRef MEDLINE - Academic |
| DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) CrossRef MEDLINE - Academic |
| DatabaseTitleList | MEDLINE - Academic MEDLINE |
| Database_xml | – sequence: 1 dbid: ECM name: MEDLINE url: https://search.ebscohost.com/login.aspx?direct=true&db=cmedm&site=ehost-live sourceTypes: Index Database |
| DeliveryMethod | fulltext_linktorsrc |
| Discipline | Anatomy & Physiology Chemistry Biology |
| EISSN | 1568-7856 |
| EndPage | 41 |
| ExternalDocumentID | 10_1016_j_dnarep_2018_02_011 29547780 S1568786417304196 |
| Genre | Research Support, Non-U.S. Gov't Journal Article |
| GroupedDBID | --- --K --M -~X .~1 0R~ 1B1 1RT 1~. 1~5 29G 4.4 457 4G. 53G 5GY 5RE 5VS 7-5 71M 8P~ AACTN AAEDT AAEDW AAIAV AAIKJ AAKOC AALRI AAOAW AAQFI AATCM AAXUO ABFNM ABFRF ABFYP ABGSF ABJNI ABLST ABMAC ABUDA ABXDB ABYKQ ABZDS ACDAQ ACGFO ACGFS ACIUM ACRLP ADBBV ADEZE ADMUD ADUVX AEBSH AEFWE AEHWI AEKER AENEX AFKWA AFTJW AFXIZ AGHFR AGRDE AGUBO AGYEJ AHEUO AIEXJ AIKHN AITUG AJBFU AJOXV AKIFW ALCLG ALMA_UNASSIGNED_HOLDINGS AMFUW AMRAJ AXJTR BKOJK BLECG BLXMC CS3 DOVZS DU5 EBS EFJIC EFLBG EJD EO8 EO9 EP2 EP3 F5P FDB FEDTE FIRID FNPLU FYGXN G-Q GBLVA HVGLF HZ~ H~9 IH2 IHE J1W KCYFY KOM M41 MO0 N9A O-L O9- OAUVE OGGZJ OZT P-8 P-9 P2P PC. Q38 RIG ROL RPZ SCC SDF SDG SDP SES SEW SPCBC SSJ SSP SSU SSZ T5K ZGI ~G- AAXKI AFJKZ AKRWK CGR CUY CVF ECM EIF NPM AAYXX CITATION 7X8 |
| ID | FETCH-LOGICAL-c474t-f3d6757cda7c1c860069cfe7efaba5c872f26db38330fbdf5cd7961870f122393 |
| ISSN | 1568-7864 |
| IngestDate | Sun Sep 29 07:28:15 EDT 2024 Thu Sep 26 19:54:57 EDT 2024 Wed Oct 16 00:59:12 EDT 2024 Fri Feb 23 02:32:38 EST 2024 |
| IsDoiOpenAccess | false |
| IsOpenAccess | true |
| IsPeerReviewed | true |
| IsScholarly | true |
| Keywords | DTT Ugi Base excision repair DNA repair BER Chlamydomonas AP UNG |
| Language | English |
| License | Copyright © 2018 Elsevier B.V. All rights reserved. |
| LinkModel | OpenURL |
| MergedId | FETCHMERGED-LOGICAL-c474t-f3d6757cda7c1c860069cfe7efaba5c872f26db38330fbdf5cd7961870f122393 |
| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
| ORCID | 0000-0002-0338-7306 |
| OpenAccessLink | http://helvia.uco.es/xmlui/bitstream/10396/27297/5/2018_DNA%20Repair.pdf |
| PMID | 29547780 |
| PQID | 2014950215 |
| PQPubID | 23479 |
| PageCount | 8 |
| ParticipantIDs | proquest_miscellaneous_2014950215 crossref_primary_10_1016_j_dnarep_2018_02_011 pubmed_primary_29547780 elsevier_sciencedirect_doi_10_1016_j_dnarep_2018_02_011 |
| PublicationCentury | 2000 |
| PublicationDate | May 2018 2018-05-00 20180501 |
| PublicationDateYYYYMMDD | 2018-05-01 |
| PublicationDate_xml | – month: 05 year: 2018 text: May 2018 |
| PublicationDecade | 2010 |
| PublicationPlace | Netherlands |
| PublicationPlace_xml | – name: Netherlands |
| PublicationTitle | DNA repair |
| PublicationTitleAlternate | DNA Repair (Amst) |
| PublicationYear | 2018 |
| Publisher | Elsevier B.V |
| Publisher_xml | – name: Elsevier B.V |
| References | Visnes, Akbari, Hagen, Slupphaug, Krokan (bib0165) 2008; 7 Dalhus, Laerdahl, Backe, Bjoras (bib0025) 2009; 33 Takahashi, Sakamoto, Tanaka, Shimizu (bib0200) 2007; 145 Krokan, Bjoras (bib0015) 2013; 5 Pascucci, Maga, Hubscher, Bjoras, Seeberg, Hickson, Villani, Giordano, Cellai, Dogliotti (bib0055) 2002; 30 Cordoba-Canero, Roldan-Arjona, Ariza (bib0225) 2014; 79 Lindahl (bib0030) 1974; 71 Fortini, Dogliotti (bib0070) 2007; 6 Cordoba-Cañero, Dubois, Ariza, Doutriaux, Roldan-Arjona (bib0170) 2010; 285 Haushalter, Stukenberg, Kirschner, Verdine (bib0150) 1999; 9 Dianov, Price, Lindahl (bib0035) 1992; 12 Cordoba-Cañero, Morales-Ruiz, Roldan-Arjona, Ariza (bib0095) 2009; 60 Gallinari, Jiricny (bib0145) 1996; 383 Nash, Caldecott, Barnes, Lindahl (bib0060) 1997; 36 Kelley, Kow, Wilson (bib0265) 2003; 63 Drohat, Jagadeesh, Ferguson, Stivers (bib0130) 1999; 38 Zhigang, Smith, Mosbaugh (bib0140) 1991; 99 Krokan, Drablos, Slupphaug (bib0175) 2002; 21 Parsons, Dianov (bib0020) 2013; 12 Gellon, Carson, Carson, Demple (bib0275) 2008; 7 Pascucci, Stucki, Jonsson, Dogliotti, Hubscher (bib0185) 1999; 274 Gonzalez-Barrera, Sanchez, Ruiz, Juarez, Picher, Terrados, Andrade, Blanco (bib0270) 2005; 33 Levin, Bai, Yao, O'Donnell, Tomkinson (bib0065) 1997; 94 Cordoba-Cañero, Roldan-Arjona, Ariza, Arabidopsis (bib0100) 2011; 68 Frost, Small (bib0205) 1984; 782 Thompson, Higgins, Gibson (bib0285) 1994; 22 Wiederhold, Leppard, Kedar, Karimi-Busheri, Rasouli-Nia, Weinfeld, Tomkinson, Izumi, Prasad, Wilson, Mitra, Hazra (bib0050) 2004; 15 Braithwaite, Prasad, Shock, Hou, Beard, Wilson (bib0230) 2005; 280 Prasad, Dianov, Bohr, Wilson (bib0245) 2000; 275 Hendrich, Hardeland, Ng, Jiricny, Bird (bib0155) 1999; 401 Pearl (bib0120) 2000; 460 Cappelli, Taylor, Cevasco, Abbondandolo, Caldecott, Frosina (bib0260) 1997; 272 Merchant, Prochnik, Vallon, Harris, Karpowicz, Witman, Terry, Salamov, Fritz-Laylin, Marechal-Drouard, Marshall, Qu, Nelson, Sanderfoot, Spalding, Kapitonov, Ren, Ferris, Lindquist, Shapiro, Lucas, Grimwood, Schmutz, Cardol, Cerutti, Chanfreau, Chen, Cognat, Croft, Dent, Dutcher, Fernandez, Fukuzawa, Gonzalez-Ballester, Gonzalez-Halphen, Hallmann, Hanikenne, Hippler, Inwood, Jabbari, Kalanon, Kuras, Lefebvre, Lemaire, Lobanov, Lohr, Manuell, Meier, Mets, Mittag, Mittelmeier, Moroney, Moseley, Napoli, Nedelcu, Niyogi, Novoselov, Paulsen, Pazour, Purton, Ral, Riano-Pachon, Riekhof, Rymarquis, Schroda, Stern, Umen, Willows, Wilson, Zimmer, Allmer, Balk, Bisova, Chen, Elias, Gendler, Hauser, Lamb, Ledford, Long, Minagawa, Page, Pan, Pootakham, Roje, Rose, Stahlberg, Terauchi, Yang, Ball, Bowler, Dieckmann, Gladyshev, Green, Jorgensen, Mayfield, Mueller-Roeber, Rajamani, Sayre, Brokstein, Dubchak, Goodstein, Hornick, Huang, Jhaveri, Luo, Martinez, Ngau, Otillar, Poliakov, Porter, Szajkowski, Werner, Zhou, Grigoriev, Rokhsar, Grossman (bib0110) 2007; 318 Harris (bib0115) 1989 Britt (bib0105) 2002 Pettersen, Sundheim, Gilljam, Slupphaug, Krokan, Kavli (bib0160) 2007; 35 Uchiyama, Kimura, Yamamoto, Ishibashi, Sakaguchi (bib0235) 2004; 271 Zhang, Dianov (bib0075) 2005; 4 Levin, Demple (bib0040) 1990; 18 Martinez-Macías, Cordoba-Cañero, Ariza, Roldan-Arjona (bib0280) 2013; 288 Cordoba-Canero, Morales-Ruiz, Roldan-Arjona, Ariza (bib0215) 2009; 60 Friedberg, Walker, Siede, Wood, Schultz, Ellenberger (bib0010) 2006 Alseth, Korvald, Osman, Seeberg, Bjoras (bib0085) 2004; 32 Jilani, Ramotar, Slack, Ong, Yang, Scherer, Lasko (bib0190) 1999; 274 Lindahl (bib0005) 1993; 362 Mol, Arvai, Sanderson, Slupphaug, Kavli, Krokan, Mosbaugh, Tainer (bib0125) 1995; 82 Wang, Wu, Friedberg (bib0090) 1993; 13 Uchiyama, Takeuchi, Kodera, Sakaguchi (bib0240) 2009; 91 Wang, Mosbaugh (bib0135) 1989; 264 Chaudhari, Raghavan, Rao (bib0210) 2014; 9 Martinez-Macias, Qian, Miki, Pontes, Liu, Tang, Liu, Morales-Ruiz, Ariza, Roldan-Arjona, Zhu (bib0195) 2012; 45 Chan, Zhang, Dianov (bib0080) 2006; 21 Cordoba-Cañero, Roldan-Arjona, Ariza (bib0180) 2012; 920 Sleeth, Robson, Dianov (bib0255) 2004; 43 Murphy, Belmonte, Shu, Britt, Hatteroth (bib0220) 2009; 4 Srivastava, Berg, Prasad, Molina, Beard, Tomkinson, Wilson (bib0045) 1998; 273 Klungland, Lindahl (bib0250) 1997; 16 Pascucci (10.1016/j.dnarep.2018.02.011_bib0185) 1999; 274 Wiederhold (10.1016/j.dnarep.2018.02.011_bib0050) 2004; 15 Mol (10.1016/j.dnarep.2018.02.011_bib0125) 1995; 82 Uchiyama (10.1016/j.dnarep.2018.02.011_bib0240) 2009; 91 Zhang (10.1016/j.dnarep.2018.02.011_bib0075) 2005; 4 Visnes (10.1016/j.dnarep.2018.02.011_bib0165) 2008; 7 Pearl (10.1016/j.dnarep.2018.02.011_bib0120) 2000; 460 Alseth (10.1016/j.dnarep.2018.02.011_bib0085) 2004; 32 Wang (10.1016/j.dnarep.2018.02.011_bib0135) 1989; 264 Braithwaite (10.1016/j.dnarep.2018.02.011_bib0230) 2005; 280 Levin (10.1016/j.dnarep.2018.02.011_bib0065) 1997; 94 Thompson (10.1016/j.dnarep.2018.02.011_bib0285) 1994; 22 Haushalter (10.1016/j.dnarep.2018.02.011_bib0150) 1999; 9 Cordoba-Canero (10.1016/j.dnarep.2018.02.011_bib0225) 2014; 79 Zhigang (10.1016/j.dnarep.2018.02.011_bib0140) 1991; 99 Chaudhari (10.1016/j.dnarep.2018.02.011_bib0210) 2014; 9 Britt (10.1016/j.dnarep.2018.02.011_bib0105) 2002 Kelley (10.1016/j.dnarep.2018.02.011_bib0265) 2003; 63 Gellon (10.1016/j.dnarep.2018.02.011_bib0275) 2008; 7 Nash (10.1016/j.dnarep.2018.02.011_bib0060) 1997; 36 Harris (10.1016/j.dnarep.2018.02.011_bib0115) 1989 Pascucci (10.1016/j.dnarep.2018.02.011_bib0055) 2002; 30 Gonzalez-Barrera (10.1016/j.dnarep.2018.02.011_bib0270) 2005; 33 Lindahl (10.1016/j.dnarep.2018.02.011_bib0005) 1993; 362 Hendrich (10.1016/j.dnarep.2018.02.011_bib0155) 1999; 401 Dianov (10.1016/j.dnarep.2018.02.011_bib0035) 1992; 12 Cordoba-Cañero (10.1016/j.dnarep.2018.02.011_bib0170) 2010; 285 Frost (10.1016/j.dnarep.2018.02.011_bib0205) 1984; 782 Prasad (10.1016/j.dnarep.2018.02.011_bib0245) 2000; 275 Gallinari (10.1016/j.dnarep.2018.02.011_bib0145) 1996; 383 Dalhus (10.1016/j.dnarep.2018.02.011_bib0025) 2009; 33 Srivastava (10.1016/j.dnarep.2018.02.011_bib0045) 1998; 273 Levin (10.1016/j.dnarep.2018.02.011_bib0040) 1990; 18 Krokan (10.1016/j.dnarep.2018.02.011_bib0015) 2013; 5 Merchant (10.1016/j.dnarep.2018.02.011_bib0110) 2007; 318 Murphy (10.1016/j.dnarep.2018.02.011_bib0220) 2009; 4 Takahashi (10.1016/j.dnarep.2018.02.011_bib0200) 2007; 145 Krokan (10.1016/j.dnarep.2018.02.011_bib0175) 2002; 21 Martinez-Macias (10.1016/j.dnarep.2018.02.011_bib0195) 2012; 45 Cappelli (10.1016/j.dnarep.2018.02.011_bib0260) 1997; 272 Pettersen (10.1016/j.dnarep.2018.02.011_bib0160) 2007; 35 Cordoba-Cañero (10.1016/j.dnarep.2018.02.011_bib0100) 2011; 68 Lindahl (10.1016/j.dnarep.2018.02.011_bib0030) 1974; 71 Jilani (10.1016/j.dnarep.2018.02.011_bib0190) 1999; 274 Cordoba-Canero (10.1016/j.dnarep.2018.02.011_bib0215) 2009; 60 Cordoba-Cañero (10.1016/j.dnarep.2018.02.011_bib0180) 2012; 920 Parsons (10.1016/j.dnarep.2018.02.011_bib0020) 2013; 12 Cordoba-Cañero (10.1016/j.dnarep.2018.02.011_bib0095) 2009; 60 Sleeth (10.1016/j.dnarep.2018.02.011_bib0255) 2004; 43 Martinez-Macías (10.1016/j.dnarep.2018.02.011_bib0280) 2013; 288 Chan (10.1016/j.dnarep.2018.02.011_bib0080) 2006; 21 Friedberg (10.1016/j.dnarep.2018.02.011_bib0010) 2006 Drohat (10.1016/j.dnarep.2018.02.011_bib0130) 1999; 38 Wang (10.1016/j.dnarep.2018.02.011_bib0090) 1993; 13 Fortini (10.1016/j.dnarep.2018.02.011_bib0070) 2007; 6 Klungland (10.1016/j.dnarep.2018.02.011_bib0250) 1997; 16 Uchiyama (10.1016/j.dnarep.2018.02.011_bib0235) 2004; 271 |
| References_xml | – volume: 79 start-page: 824 year: 2014 end-page: 834 ident: bib0225 article-title: Arabidopsis ZDP DNA 3'-phosphatase and ARP endonuclease function in 8-oxoG repair initiated by FPG and OGG1 DNA glycosylases publication-title: Plant J. Cell Mol. Biol. contributor: fullname: Ariza – volume: 82 start-page: 701 year: 1995 end-page: 708 ident: bib0125 article-title: Crystal structure of human uracil-DNA glycosylase in complex with a protein inhibitor: protein mimicry of DNA publication-title: Cell contributor: fullname: Tainer – volume: 7 start-page: 187 year: 2008 end-page: 198 ident: bib0275 article-title: Intrinsic 5'-deoxyribose-5-phosphate lyase activity in Saccharomyces cerevisiae Trf4 protein with a possible role in base excision DNA repair publication-title: DNA Repair (Amst.) contributor: fullname: Demple – volume: 6 start-page: 398 year: 2007 end-page: 409 ident: bib0070 article-title: Base damage and single-strand break repair: mechanisms and functional significance of short- and long-patch repair subpathways publication-title: DNA Repair (Amst.) contributor: fullname: Dogliotti – volume: 60 start-page: 716 year: 2009 end-page: 728 ident: bib0215 article-title: Single-nucleotide and long-patch base excision repair of DNA damage in plants publication-title: Plant J. Cell Mol. Biol. contributor: fullname: Ariza – volume: 275 start-page: 4460 year: 2000 end-page: 4466 ident: bib0245 article-title: FEN1 stimulation of DNA polymerase beta mediates an excision step in mammalian long patch base excision repair publication-title: J. Biol. Chem. contributor: fullname: Wilson – volume: 4 start-page: e4297 year: 2009 ident: bib0220 article-title: Requirement for abasic endonuclease gene homologues in Arabidopsis seed development publication-title: PLoS One contributor: fullname: Hatteroth – volume: 288 start-page: 5496 year: 2013 end-page: 5505 ident: bib0280 article-title: The DNA repair protein XRCC1 functions in the plant DNA demethylation pathway by stimulating cytosine methylation (5-meC) excision, gap tailoring, and DNA ligation publication-title: J. Biol. Chem. contributor: fullname: Roldan-Arjona – year: 1989 ident: bib0115 article-title: The Chlamydomonas Sourcebook contributor: fullname: Harris – volume: 285 start-page: 7475 year: 2010 end-page: 7483 ident: bib0170 article-title: Arabidopsis uracil DNA glycosylase (UNG) is required for base excision repair of uracil and increases plant sensitivity to 5-fluorouracil publication-title: J. Biol. Chem. contributor: fullname: Roldan-Arjona – volume: 71 start-page: 3649 year: 1974 end-page: 3653 ident: bib0030 article-title: An N-glycosidase from Escherichia coli that releases free uracil from DNA containing deaminated cytosine residues publication-title: Proc. Natl. Acad. Sci. U. S. A. contributor: fullname: Lindahl – volume: 15 start-page: 209 year: 2004 end-page: 220 ident: bib0050 article-title: AP endonuclease-independent DNA base excision repair in human cells publication-title: Mol. Cell contributor: fullname: Hazra – volume: 273 start-page: 21203 year: 1998 end-page: 21209 ident: bib0045 article-title: Mammalian abasic site base excision repair. Identification of the reaction sequence and rate-determining steps publication-title: J. Biol. Chem. contributor: fullname: Wilson – volume: 272 start-page: 23970 year: 1997 end-page: 23975 ident: bib0260 article-title: Involvement of XRCC1 and DNA ligase III gene products in DNA base excision repair publication-title: J. Biol. Chem. contributor: fullname: Frosina – volume: 99 start-page: 31 year: 1991 end-page: 37 ident: bib0140 article-title: Overproduction and characterization of the uracil-DNA glycosylase inhibitor of bacteriophage PBS2 publication-title: Gene contributor: fullname: Mosbaugh – volume: 383 start-page: 735 year: 1996 ident: bib0145 article-title: A new class of uracil-DNA glycosylases related to human thymine = DNA glycosylase publication-title: Nature contributor: fullname: Jiricny – volume: 274 start-page: 24176 year: 1999 end-page: 24186 ident: bib0190 article-title: Molecular cloning of the human gene PNKP, encoding a polynucleotide kinase 3′-phosphatase and evidence for its role in repair of DNA strand breaks caused by oxidative damage publication-title: J. Biol. Chem. contributor: fullname: Lasko – volume: 33 start-page: 4762 year: 2005 end-page: 4774 ident: bib0270 article-title: Characterization of SpPol4, a unique X-family DNA polymerase in Schizosaccharomyces pombe publication-title: Nucleic Acids Res. contributor: fullname: Blanco – volume: 21 start-page: 8935 year: 2002 end-page: 8948 ident: bib0175 article-title: Uracil in DNA–occurrence, consequences and repair publication-title: Oncogene contributor: fullname: Slupphaug – volume: 13 start-page: 1051 year: 1993 end-page: 1058 ident: bib0090 article-title: DNA repair synthesis during base excision repair in vitro is catalyzed by DNA polymerase epsilon and is influenced by DNA polymerases alpha and delta in Saccharomyces cerevisiae publication-title: Mol. Cell. Biol. contributor: fullname: Friedberg – volume: 16 start-page: 3341 year: 1997 end-page: 3348 ident: bib0250 article-title: Second pathway for completion of human DNA base excision-repair: reconstitution with purified proteins and requirement for DNase IV (FEN1) publication-title: EMBO J. contributor: fullname: Lindahl – volume: 5 start-page: a012583 year: 2013 ident: bib0015 article-title: Base excision repair publication-title: Cold Spring Harb. Perspect. Biol. contributor: fullname: Bjoras – volume: 45 start-page: 357 year: 2012 end-page: 370 ident: bib0195 article-title: A DNA 3' phosphatase functions in active DNA demethylation in Arabidopsis publication-title: Mol. Cell contributor: fullname: Zhu – volume: 63 start-page: 549 year: 2003 end-page: 554 ident: bib0265 article-title: Disparity between DNA base excision repair in yeast and mammals: translational implications publication-title: Cancer Res. contributor: fullname: Wilson – volume: 782 start-page: 170 year: 1984 end-page: 176 ident: bib0205 article-title: Partial purification and characterization of the major AP endonuclease from Chlamydomonas reinhardi publication-title: Biochim. Biophys. Acta contributor: fullname: Small – volume: 362 start-page: 709 year: 1993 end-page: 715 ident: bib0005 article-title: Instability and decay of the primary structure of DNA publication-title: Nature contributor: fullname: Lindahl – volume: 36 start-page: 5207 year: 1997 end-page: 5211 ident: bib0060 article-title: XRCC1 protein interacts with one of two distinct forms of DNA ligase III publication-title: Biochemistry contributor: fullname: Lindahl – volume: 460 start-page: 165 year: 2000 end-page: 181 ident: bib0120 article-title: Structure and function in the uracil-DNA glycosylase superfamily publication-title: Mutat. Res. DNA Repair contributor: fullname: Pearl – volume: 9 start-page: 174 year: 1999 end-page: 185 ident: bib0150 article-title: Identification of a new uracil-DNA glycosylase family by expression cloning using synthetic inhibitors publication-title: Curr. Biol. contributor: fullname: Verdine – volume: 4 start-page: 263 year: 2005 end-page: 270 ident: bib0075 article-title: DNA repair fidelity of base excision repair pathways in human cell extracts publication-title: DNA Repair (Amst.) contributor: fullname: Dianov – volume: 38 start-page: 11866 year: 1999 end-page: 11875 ident: bib0130 article-title: Role of electrophilic and general base catalysis in the mechanism of Escherichia coli uracil DNA glycosylase publication-title: Biochemistry contributor: fullname: Stivers – volume: 145 start-page: 1052 year: 2007 end-page: 1060 ident: bib0200 article-title: AtREV1, a Y-family DNA polymerase in Arabidopsis, has deoxynucleotidyl transferase activity in vitro publication-title: Plant Physiol. contributor: fullname: Shimizu – volume: 280 start-page: 18469 year: 2005 end-page: 18475 ident: bib0230 article-title: DNA polymerase λ mediates a back-up base excision repair activity in extracts of mouse embryonic fibroblasts publication-title: J. Biol. Chem. contributor: fullname: Wilson – volume: 60 start-page: 716 year: 2009 end-page: 728 ident: bib0095 article-title: Single-nucleotide and long-patch base excision repair of DNA damage in plants publication-title: Plant J. contributor: fullname: Ariza – volume: 22 start-page: 4673 year: 1994 end-page: 4680 ident: bib0285 article-title: CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice publication-title: Nucleic Acids Res. contributor: fullname: Gibson – volume: 33 start-page: 1044 year: 2009 end-page: 1078 ident: bib0025 article-title: DNA base repair–recognition and initiation of catalysis publication-title: FEMS Microbiol. Rev. contributor: fullname: Bjoras – volume: 35 start-page: 3879 year: 2007 end-page: 3892 ident: bib0160 article-title: Uracil-DNA glycosylases SMUG1 and UNG2 coordinate the initial steps of base excision repair by distinct mechanisms publication-title: Nucleic Acids Res. contributor: fullname: Kavli – volume: 12 start-page: 326 year: 2013 end-page: 333 ident: bib0020 article-title: Co-ordination of base excision repair and genome stability publication-title: DNA Repair (Amst.) contributor: fullname: Dianov – volume: 43 start-page: 12924 year: 2004 end-page: 12930 ident: bib0255 article-title: Exchangeability of mammalian DNA ligases between base excision repair pathways publication-title: Biochemistry contributor: fullname: Dianov – volume: 920 start-page: 263 year: 2012 end-page: 277 ident: bib0180 article-title: Using Arabidopsis cell extracts to monitor repair of DNA base damage in vitro publication-title: Methods Mol. Biol. contributor: fullname: Ariza – volume: 32 start-page: 5119 year: 2004 end-page: 5125 ident: bib0085 article-title: A general role of the DNA glycosylase Nth1 in the abasic sites cleavage step of base excision repair in Schizosaccharomyces pombe publication-title: Nucleic Acids Res. contributor: fullname: Bjoras – volume: 9 start-page: e109160 year: 2014 ident: bib0210 article-title: Preparation of efficient excision repair competent cell-free extracts from C. reinhardtii cells publication-title: PLoS One contributor: fullname: Rao – volume: 94 start-page: 12863 year: 1997 end-page: 12868 ident: bib0065 article-title: An interaction between DNA ligase I and proliferating cell nuclear antigen: implications for Okazaki fragment synthesis and joining publication-title: Proc. Natl. Acad. Sci. U. S. A. contributor: fullname: Tomkinson – volume: 68 start-page: 693 year: 2011 end-page: 702 ident: bib0100 article-title: endonuclease functions in a branched base excision DNA repair pathway completed by LIG1 publication-title: Plant J.: Cell Mol. Biol. contributor: fullname: Arabidopsis – year: 2002 ident: bib0105 article-title: Repair of damaged bases publication-title: The Arabidopsis Book contributor: fullname: Britt – volume: 401 start-page: 301 year: 1999 end-page: 304 ident: bib0155 article-title: The thymine glycosylase MBD4 can bind to the product of deamination at methylated CpG sites publication-title: Nature contributor: fullname: Bird – volume: 274 start-page: 33696 year: 1999 end-page: 33702 ident: bib0185 article-title: Long patch base excision repair with purified human proteins. DNA ligase I as patch size mediator for DNA polymerases delta and epsilon publication-title: J. Biol. Chem. contributor: fullname: Hubscher – volume: 271 start-page: 2799 year: 2004 end-page: 2807 ident: bib0235 article-title: Plant DNA polymerase lambda, a DNA repair enzyme that functions in plant meristematic and meiotic tissues publication-title: Eur. J. Biochem. contributor: fullname: Sakaguchi – volume: 18 start-page: 5069 year: 1990 end-page: 5075 ident: bib0040 article-title: Analysis of class II (hydrolytic) and class I (beta-lyase) apurinic/apyrimidinic endonucleases with a synthetic DNA substrate publication-title: Nucleic Acids Res. contributor: fullname: Demple – volume: 12 start-page: 1605 year: 1992 end-page: 1612 ident: bib0035 article-title: Generation of single-nucleotide repair patches following excision of uracil residues from DNA publication-title: Mol. Cell. Biol. contributor: fullname: Lindahl – volume: 30 start-page: 2124 year: 2002 end-page: 2130 ident: bib0055 article-title: Reconstitution of the base excision repair pathway for 7,8-dihydro-8-oxoguanine with purified human proteins publication-title: Nucleic Acids Res. contributor: fullname: Dogliotti – year: 2006 ident: bib0010 article-title: DNA Repair and Mutagenesis contributor: fullname: Ellenberger – volume: 91 start-page: 165 year: 2009 end-page: 170 ident: bib0240 article-title: Distribution and roles of X-family DNA polymerases in eukaryotes publication-title: Biochimie contributor: fullname: Sakaguchi – volume: 264 start-page: 1163 year: 1989 end-page: 1171 ident: bib0135 article-title: Uracil-DNA glycosylase inhibitor gene of bacteriophage PBS2 encodes a binding protein specific for uracil-DNA glycosylase publication-title: J. Biol. Chem. contributor: fullname: Mosbaugh – volume: 318 start-page: 245 year: 2007 end-page: 250 ident: bib0110 article-title: The Chlamydomonas genome reveals the evolution of key animal and plant functions publication-title: Science contributor: fullname: Grossman – volume: 7 start-page: 1869 year: 2008 end-page: 1881 ident: bib0165 article-title: The rate of base excision repair of uracil is controlled by the initiating glycosylase publication-title: DNA Repair (Amst.) contributor: fullname: Krokan – volume: 21 start-page: 173 year: 2006 end-page: 178 ident: bib0080 article-title: Base excision repair fidelity in normal and cancer cells publication-title: Mutagenesis contributor: fullname: Dianov – volume: 18 start-page: 5069 year: 1990 ident: 10.1016/j.dnarep.2018.02.011_bib0040 article-title: Analysis of class II (hydrolytic) and class I (beta-lyase) apurinic/apyrimidinic endonucleases with a synthetic DNA substrate publication-title: Nucleic Acids Res. doi: 10.1093/nar/18.17.5069 contributor: fullname: Levin – volume: 318 start-page: 245 year: 2007 ident: 10.1016/j.dnarep.2018.02.011_bib0110 article-title: The Chlamydomonas genome reveals the evolution of key animal and plant functions publication-title: Science doi: 10.1126/science.1143609 contributor: fullname: Merchant – volume: 4 start-page: e4297 year: 2009 ident: 10.1016/j.dnarep.2018.02.011_bib0220 article-title: Requirement for abasic endonuclease gene homologues in Arabidopsis seed development publication-title: PLoS One doi: 10.1371/journal.pone.0004297 contributor: fullname: Murphy – volume: 275 start-page: 4460 year: 2000 ident: 10.1016/j.dnarep.2018.02.011_bib0245 article-title: FEN1 stimulation of DNA polymerase beta mediates an excision step in mammalian long patch base excision repair publication-title: J. Biol. Chem. doi: 10.1074/jbc.275.6.4460 contributor: fullname: Prasad – volume: 38 start-page: 11866 year: 1999 ident: 10.1016/j.dnarep.2018.02.011_bib0130 article-title: Role of electrophilic and general base catalysis in the mechanism of Escherichia coli uracil DNA glycosylase publication-title: Biochemistry doi: 10.1021/bi9910878 contributor: fullname: Drohat – volume: 280 start-page: 18469 year: 2005 ident: 10.1016/j.dnarep.2018.02.011_bib0230 article-title: DNA polymerase λ mediates a back-up base excision repair activity in extracts of mouse embryonic fibroblasts publication-title: J. Biol. Chem. doi: 10.1074/jbc.M411864200 contributor: fullname: Braithwaite – volume: 12 start-page: 326 year: 2013 ident: 10.1016/j.dnarep.2018.02.011_bib0020 article-title: Co-ordination of base excision repair and genome stability publication-title: DNA Repair (Amst.) doi: 10.1016/j.dnarep.2013.02.001 contributor: fullname: Parsons – volume: 12 start-page: 1605 year: 1992 ident: 10.1016/j.dnarep.2018.02.011_bib0035 article-title: Generation of single-nucleotide repair patches following excision of uracil residues from DNA publication-title: Mol. Cell. Biol. doi: 10.1128/MCB.12.4.1605 contributor: fullname: Dianov – volume: 288 start-page: 5496 year: 2013 ident: 10.1016/j.dnarep.2018.02.011_bib0280 article-title: The DNA repair protein XRCC1 functions in the plant DNA demethylation pathway by stimulating cytosine methylation (5-meC) excision, gap tailoring, and DNA ligation publication-title: J. Biol. Chem. doi: 10.1074/jbc.M112.427617 contributor: fullname: Martinez-Macías – volume: 79 start-page: 824 year: 2014 ident: 10.1016/j.dnarep.2018.02.011_bib0225 article-title: Arabidopsis ZDP DNA 3'-phosphatase and ARP endonuclease function in 8-oxoG repair initiated by FPG and OGG1 DNA glycosylases publication-title: Plant J. Cell Mol. Biol. doi: 10.1111/tpj.12588 contributor: fullname: Cordoba-Canero – volume: 22 start-page: 4673 year: 1994 ident: 10.1016/j.dnarep.2018.02.011_bib0285 article-title: CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice publication-title: Nucleic Acids Res. doi: 10.1093/nar/22.22.4673 contributor: fullname: Thompson – volume: 33 start-page: 4762 year: 2005 ident: 10.1016/j.dnarep.2018.02.011_bib0270 article-title: Characterization of SpPol4, a unique X-family DNA polymerase in Schizosaccharomyces pombe publication-title: Nucleic Acids Res. doi: 10.1093/nar/gki780 contributor: fullname: Gonzalez-Barrera – volume: 36 start-page: 5207 year: 1997 ident: 10.1016/j.dnarep.2018.02.011_bib0060 article-title: XRCC1 protein interacts with one of two distinct forms of DNA ligase III publication-title: Biochemistry doi: 10.1021/bi962281m contributor: fullname: Nash – volume: 60 start-page: 716 year: 2009 ident: 10.1016/j.dnarep.2018.02.011_bib0095 article-title: Single-nucleotide and long-patch base excision repair of DNA damage in plants publication-title: Plant J. doi: 10.1111/j.1365-313X.2009.03994.x contributor: fullname: Cordoba-Cañero – volume: 21 start-page: 173 year: 2006 ident: 10.1016/j.dnarep.2018.02.011_bib0080 article-title: Base excision repair fidelity in normal and cancer cells publication-title: Mutagenesis doi: 10.1093/mutage/gel020 contributor: fullname: Chan – year: 2002 ident: 10.1016/j.dnarep.2018.02.011_bib0105 article-title: Repair of damaged bases contributor: fullname: Britt – volume: 91 start-page: 165 year: 2009 ident: 10.1016/j.dnarep.2018.02.011_bib0240 article-title: Distribution and roles of X-family DNA polymerases in eukaryotes publication-title: Biochimie doi: 10.1016/j.biochi.2008.07.005 contributor: fullname: Uchiyama – year: 2006 ident: 10.1016/j.dnarep.2018.02.011_bib0010 contributor: fullname: Friedberg – volume: 21 start-page: 8935 year: 2002 ident: 10.1016/j.dnarep.2018.02.011_bib0175 article-title: Uracil in DNA–occurrence, consequences and repair publication-title: Oncogene doi: 10.1038/sj.onc.1205996 contributor: fullname: Krokan – year: 1989 ident: 10.1016/j.dnarep.2018.02.011_bib0115 contributor: fullname: Harris – volume: 271 start-page: 2799 year: 2004 ident: 10.1016/j.dnarep.2018.02.011_bib0235 article-title: Plant DNA polymerase lambda, a DNA repair enzyme that functions in plant meristematic and meiotic tissues publication-title: Eur. J. Biochem. doi: 10.1111/j.1432-1033.2004.04214.x contributor: fullname: Uchiyama – volume: 13 start-page: 1051 year: 1993 ident: 10.1016/j.dnarep.2018.02.011_bib0090 article-title: DNA repair synthesis during base excision repair in vitro is catalyzed by DNA polymerase epsilon and is influenced by DNA polymerases alpha and delta in Saccharomyces cerevisiae publication-title: Mol. Cell. Biol. doi: 10.1128/MCB.13.2.1051 contributor: fullname: Wang – volume: 401 start-page: 301 year: 1999 ident: 10.1016/j.dnarep.2018.02.011_bib0155 article-title: The thymine glycosylase MBD4 can bind to the product of deamination at methylated CpG sites publication-title: Nature doi: 10.1038/45843 contributor: fullname: Hendrich – volume: 45 start-page: 357 year: 2012 ident: 10.1016/j.dnarep.2018.02.011_bib0195 article-title: A DNA 3' phosphatase functions in active DNA demethylation in Arabidopsis publication-title: Mol. Cell doi: 10.1016/j.molcel.2011.11.034 contributor: fullname: Martinez-Macias – volume: 383 start-page: 735 year: 1996 ident: 10.1016/j.dnarep.2018.02.011_bib0145 article-title: A new class of uracil-DNA glycosylases related to human thymine = DNA glycosylase publication-title: Nature doi: 10.1038/383735a0 contributor: fullname: Gallinari – volume: 9 start-page: e109160 year: 2014 ident: 10.1016/j.dnarep.2018.02.011_bib0210 article-title: Preparation of efficient excision repair competent cell-free extracts from C. reinhardtii cells publication-title: PLoS One doi: 10.1371/journal.pone.0109160 contributor: fullname: Chaudhari – volume: 60 start-page: 716 year: 2009 ident: 10.1016/j.dnarep.2018.02.011_bib0215 article-title: Single-nucleotide and long-patch base excision repair of DNA damage in plants publication-title: Plant J. Cell Mol. Biol. doi: 10.1111/j.1365-313X.2009.03994.x contributor: fullname: Cordoba-Canero – volume: 9 start-page: 174 year: 1999 ident: 10.1016/j.dnarep.2018.02.011_bib0150 article-title: Identification of a new uracil-DNA glycosylase family by expression cloning using synthetic inhibitors publication-title: Curr. Biol. doi: 10.1016/S0960-9822(99)80087-6 contributor: fullname: Haushalter – volume: 94 start-page: 12863 year: 1997 ident: 10.1016/j.dnarep.2018.02.011_bib0065 article-title: An interaction between DNA ligase I and proliferating cell nuclear antigen: implications for Okazaki fragment synthesis and joining publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.94.24.12863 contributor: fullname: Levin – volume: 264 start-page: 1163 year: 1989 ident: 10.1016/j.dnarep.2018.02.011_bib0135 article-title: Uracil-DNA glycosylase inhibitor gene of bacteriophage PBS2 encodes a binding protein specific for uracil-DNA glycosylase publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)85067-6 contributor: fullname: Wang – volume: 35 start-page: 3879 year: 2007 ident: 10.1016/j.dnarep.2018.02.011_bib0160 article-title: Uracil-DNA glycosylases SMUG1 and UNG2 coordinate the initial steps of base excision repair by distinct mechanisms publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkm372 contributor: fullname: Pettersen – volume: 274 start-page: 24176 year: 1999 ident: 10.1016/j.dnarep.2018.02.011_bib0190 article-title: Molecular cloning of the human gene PNKP, encoding a polynucleotide kinase 3′-phosphatase and evidence for its role in repair of DNA strand breaks caused by oxidative damage publication-title: J. Biol. Chem. doi: 10.1074/jbc.274.34.24176 contributor: fullname: Jilani – volume: 16 start-page: 3341 year: 1997 ident: 10.1016/j.dnarep.2018.02.011_bib0250 article-title: Second pathway for completion of human DNA base excision-repair: reconstitution with purified proteins and requirement for DNase IV (FEN1) publication-title: EMBO J. doi: 10.1093/emboj/16.11.3341 contributor: fullname: Klungland – volume: 71 start-page: 3649 year: 1974 ident: 10.1016/j.dnarep.2018.02.011_bib0030 article-title: An N-glycosidase from Escherichia coli that releases free uracil from DNA containing deaminated cytosine residues publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.71.9.3649 contributor: fullname: Lindahl – volume: 782 start-page: 170 year: 1984 ident: 10.1016/j.dnarep.2018.02.011_bib0205 article-title: Partial purification and characterization of the major AP endonuclease from Chlamydomonas reinhardi publication-title: Biochim. Biophys. Acta doi: 10.1016/0167-4781(84)90021-6 contributor: fullname: Frost – volume: 30 start-page: 2124 year: 2002 ident: 10.1016/j.dnarep.2018.02.011_bib0055 article-title: Reconstitution of the base excision repair pathway for 7,8-dihydro-8-oxoguanine with purified human proteins publication-title: Nucleic Acids Res. doi: 10.1093/nar/30.10.2124 contributor: fullname: Pascucci – volume: 15 start-page: 209 year: 2004 ident: 10.1016/j.dnarep.2018.02.011_bib0050 article-title: AP endonuclease-independent DNA base excision repair in human cells publication-title: Mol. Cell doi: 10.1016/j.molcel.2004.06.003 contributor: fullname: Wiederhold – volume: 63 start-page: 549 year: 2003 ident: 10.1016/j.dnarep.2018.02.011_bib0265 article-title: Disparity between DNA base excision repair in yeast and mammals: translational implications publication-title: Cancer Res. contributor: fullname: Kelley – volume: 285 start-page: 7475 year: 2010 ident: 10.1016/j.dnarep.2018.02.011_bib0170 article-title: Arabidopsis uracil DNA glycosylase (UNG) is required for base excision repair of uracil and increases plant sensitivity to 5-fluorouracil publication-title: J. Biol. Chem. doi: 10.1074/jbc.M109.067173 contributor: fullname: Cordoba-Cañero – volume: 32 start-page: 5119 year: 2004 ident: 10.1016/j.dnarep.2018.02.011_bib0085 article-title: A general role of the DNA glycosylase Nth1 in the abasic sites cleavage step of base excision repair in Schizosaccharomyces pombe publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkh851 contributor: fullname: Alseth – volume: 274 start-page: 33696 year: 1999 ident: 10.1016/j.dnarep.2018.02.011_bib0185 article-title: Long patch base excision repair with purified human proteins. DNA ligase I as patch size mediator for DNA polymerases delta and epsilon publication-title: J. Biol. Chem. doi: 10.1074/jbc.274.47.33696 contributor: fullname: Pascucci – volume: 920 start-page: 263 year: 2012 ident: 10.1016/j.dnarep.2018.02.011_bib0180 article-title: Using Arabidopsis cell extracts to monitor repair of DNA base damage in vitro publication-title: Methods Mol. Biol. doi: 10.1007/978-1-61779-998-3_18 contributor: fullname: Cordoba-Cañero – volume: 33 start-page: 1044 year: 2009 ident: 10.1016/j.dnarep.2018.02.011_bib0025 article-title: DNA base repair–recognition and initiation of catalysis publication-title: FEMS Microbiol. Rev. doi: 10.1111/j.1574-6976.2009.00188.x contributor: fullname: Dalhus – volume: 7 start-page: 1869 year: 2008 ident: 10.1016/j.dnarep.2018.02.011_bib0165 article-title: The rate of base excision repair of uracil is controlled by the initiating glycosylase publication-title: DNA Repair (Amst.) doi: 10.1016/j.dnarep.2008.07.012 contributor: fullname: Visnes – volume: 68 start-page: 693 year: 2011 ident: 10.1016/j.dnarep.2018.02.011_bib0100 article-title: endonuclease functions in a branched base excision DNA repair pathway completed by LIG1 publication-title: Plant J.: Cell Mol. Biol. doi: 10.1111/j.1365-313X.2011.04720.x contributor: fullname: Cordoba-Cañero – volume: 273 start-page: 21203 year: 1998 ident: 10.1016/j.dnarep.2018.02.011_bib0045 article-title: Mammalian abasic site base excision repair. Identification of the reaction sequence and rate-determining steps publication-title: J. Biol. Chem. doi: 10.1074/jbc.273.33.21203 contributor: fullname: Srivastava – volume: 362 start-page: 709 year: 1993 ident: 10.1016/j.dnarep.2018.02.011_bib0005 article-title: Instability and decay of the primary structure of DNA publication-title: Nature doi: 10.1038/362709a0 contributor: fullname: Lindahl – volume: 145 start-page: 1052 year: 2007 ident: 10.1016/j.dnarep.2018.02.011_bib0200 article-title: AtREV1, a Y-family DNA polymerase in Arabidopsis, has deoxynucleotidyl transferase activity in vitro publication-title: Plant Physiol. doi: 10.1104/pp.107.101980 contributor: fullname: Takahashi – volume: 99 start-page: 31 year: 1991 ident: 10.1016/j.dnarep.2018.02.011_bib0140 article-title: Overproduction and characterization of the uracil-DNA glycosylase inhibitor of bacteriophage PBS2 publication-title: Gene doi: 10.1016/0378-1119(91)90030-F contributor: fullname: Zhigang – volume: 460 start-page: 165 year: 2000 ident: 10.1016/j.dnarep.2018.02.011_bib0120 article-title: Structure and function in the uracil-DNA glycosylase superfamily publication-title: Mutat. Res. DNA Repair doi: 10.1016/S0921-8777(00)00025-2 contributor: fullname: Pearl – volume: 43 start-page: 12924 year: 2004 ident: 10.1016/j.dnarep.2018.02.011_bib0255 article-title: Exchangeability of mammalian DNA ligases between base excision repair pathways publication-title: Biochemistry doi: 10.1021/bi0492612 contributor: fullname: Sleeth – volume: 4 start-page: 263 year: 2005 ident: 10.1016/j.dnarep.2018.02.011_bib0075 article-title: DNA repair fidelity of base excision repair pathways in human cell extracts publication-title: DNA Repair (Amst.) doi: 10.1016/j.dnarep.2004.10.004 contributor: fullname: Zhang – volume: 6 start-page: 398 year: 2007 ident: 10.1016/j.dnarep.2018.02.011_bib0070 article-title: Base damage and single-strand break repair: mechanisms and functional significance of short- and long-patch repair subpathways publication-title: DNA Repair (Amst.) doi: 10.1016/j.dnarep.2006.10.008 contributor: fullname: Fortini – volume: 7 start-page: 187 year: 2008 ident: 10.1016/j.dnarep.2018.02.011_bib0275 article-title: Intrinsic 5'-deoxyribose-5-phosphate lyase activity in Saccharomyces cerevisiae Trf4 protein with a possible role in base excision DNA repair publication-title: DNA Repair (Amst.) doi: 10.1016/j.dnarep.2007.09.009 contributor: fullname: Gellon – volume: 5 start-page: a012583 year: 2013 ident: 10.1016/j.dnarep.2018.02.011_bib0015 article-title: Base excision repair publication-title: Cold Spring Harb. Perspect. Biol. doi: 10.1101/cshperspect.a012583 contributor: fullname: Krokan – volume: 82 start-page: 701 year: 1995 ident: 10.1016/j.dnarep.2018.02.011_bib0125 article-title: Crystal structure of human uracil-DNA glycosylase in complex with a protein inhibitor: protein mimicry of DNA publication-title: Cell doi: 10.1016/0092-8674(95)90467-0 contributor: fullname: Mol – volume: 272 start-page: 23970 year: 1997 ident: 10.1016/j.dnarep.2018.02.011_bib0260 article-title: Involvement of XRCC1 and DNA ligase III gene products in DNA base excision repair publication-title: J. Biol. Chem. doi: 10.1074/jbc.272.38.23970 contributor: fullname: Cappelli |
| SSID | ssj0015766 |
| Score | 2.3046904 |
| Snippet | •Base excision repair can be detected in cells extracts of Chlamydomonas reinhardtii.•An uracil DNA glycosylase belonging to Family-1 initiates BER of... Base excision repair (BER) is a major defense pathway against spontaneous DNA damage. This multistep process is initiated by DNA glycosylases that recognise... |
| SourceID | proquest crossref pubmed elsevier |
| SourceType | Aggregation Database Index Database Publisher |
| StartPage | 34 |
| SubjectTerms | Base excision repair Chlamydomonas Chlamydomonas reinhardtii - genetics Chlamydomonas reinhardtii - metabolism DNA Damage DNA Repair DNA, Plant - metabolism Uracil - metabolism |
| Title | Monitoring base excision repair in Chlamydomonas reinhardtii cell extracts |
| URI | https://dx.doi.org/10.1016/j.dnarep.2018.02.011 https://www.ncbi.nlm.nih.gov/pubmed/29547780 https://search.proquest.com/docview/2014950215 |
| Volume | 65 |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| link | http://sdu.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwtR1da9swUKQtY3sZW7uP7AsNxl6CQuzYlvKYpdm6wvrQZqVvRrZk5pDaw4nHml-_O8lyUkLZB-zFGKEv7k6n-xYh77IMhPA0UgyuV8mC0BcsgZuMDUPUFtLIT4zB7eSCn12J42kw7XTcK3ubtv-KaWgDXGPm7F9gu50UGuAfcA5fwDp8_wjv9pCaqDq8oXr6p31EB70DMq9Mlt83IIMbVcKeJHoN8gJTr1Z53kMzPoxYYerUcltuPT4bNxO0GMLUfr1k53VubNAzDYp7y-PPy2tdlewSuhTrWi-MiIpOeeEtfsiq7E36ruul8dV7a7ig1m3oxacKjdsmCFciM5a9L_3N3AtlxxRsXM1Lm9W2tX5jxPDEJmTQWtZ2smssM44E48JWOe_r7TZbjNxx8CjcYsGNbdRe5rao1s41YS0W874qJMAOA_yEqdza8P3bBbgvcE3chgfcMACOtUcOfGBrwFUPxp-nV6et1wp0N5PN5vbtUjVNPOHuWneJQnepOkbkmT0iDxtdhY4tkT0mHV0ckqNxIVfl9Q19T030sHHLHJJ7H9zf_Yl7Q_CInG6okSI1UkeN1BITzQt6ixrpFjVSpEbqqPEJ-fpxOpucsOb1DpYGPFixbKhAGeWpkjz1UhFhTew001xnMpFhKrif-ZFKhmI4HGSJysJUcXx-iA8yz8fCfE_JflEW-jmhgyTSoPjKgPMo0HokRlynHiguqc8zNcq6hDlAxt9tkZbYRS_OYwv4GAEfD_wYAN8l3EE7bgRNK0DGQCC_GfnWIScGUCIc4BSU9RI7BaMQJegueWax1u4Ffemci8GLf173JXmwOTavyP6qqvVrsrdU9ZuGCH8BNJmzBQ |
| link.rule.ids | 315,782,786,27933,27934 |
| linkProvider | Elsevier |
| openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Monitoring+base+excision+repair+in+Chlamydomonas+reinhardtii+cell+extracts&rft.jtitle=DNA+repair&rft.au=Morales-Ruiz%2C+Teresa&rft.au=Romero-Valenzuela%2C+%C3%81lvaro+C.&rft.au=V%C3%A1zquez%E2%80%90Grande%2C+Vanessa+M.&rft.au=Rold%C3%A1n-Arjona%2C+Teresa&rft.date=2018-05-01&rft.pub=Elsevier+B.V&rft.issn=1568-7864&rft.eissn=1568-7856&rft.volume=65&rft.spage=34&rft.epage=41&rft_id=info:doi/10.1016%2Fj.dnarep.2018.02.011&rft.externalDocID=S1568786417304196 |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1568-7864&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1568-7864&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1568-7864&client=summon |