A link between transcription and intermediary metabolism: a role for Sir2 in the control of acetyl-coenzyme A synthetase

The silent information regulator protein (Sir2) and its homologs (collectively known as sirtuins) are NAD +-dependent deacetylase enzymes involved in chromosome stability, gene silencing and cell aging in eukaryotes and archaea. The discovery that sirtuin-dependent protein deacetylation is a NAD +-c...

Full description

Saved in:

Bibliographic Details
Published in:	Current opinion in microbiology Vol. 7; no. 2; pp. 115 - 119
Main Authors:	Starai, VJ, Takahashi, H, Boeke, JD, Escalante-Semerena, JC
Format:	Journal Article
Language:	English
Published:	England Elsevier Ltd 01-04-2004
Subjects:	Acetate-CoA Ligase - metabolism Amino Acid Sequence Molecular Sequence Data Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Salmonella enterica - genetics Salmonella enterica - metabolism Sirtuins Sirtuins - genetics Sirtuins - metabolism Transcription, Genetic - physiology Acs NAD Sir2 NADH AMP CoA OAADPr
Online Access:	Get full text
Tags:	Add Tag No Tags, Be the first to tag this record!

Abstract	The silent information regulator protein (Sir2) and its homologs (collectively known as sirtuins) are NAD +-dependent deacetylase enzymes involved in chromosome stability, gene silencing and cell aging in eukaryotes and archaea. The discovery that sirtuin-dependent protein deacetylation is a NAD +-consuming reaction established a link with the energy generation systems of the cell. This link to metabolism was recently extended to the post-translational control of the activity of short-chain fatty acyl-coenzyme A (adenosine monophosphate-forming) synthetases in bacteria and yeast. The crystal structure of the Sir protein complexed with a peptide of a protein substrate provided insights into how sirtuins interact with their protein substrates.
AbstractList	The silent information regulator protein (Sir2) and its homologs (collectively known as sirtuins) are NAD super(+)-dependent deacetylase enzymes involved in chromosome stability, gene silencing and cell aging in eukaryotes and archaea. The discovery that sirtuin-dependent protein deacetylation is a NAD super(+)-consuming reaction established a link with the energy generation systems of the cell. This link to metabolism was recently extended to the post-translational control of the activity of short-chain fatty acyl-coenzyme A (adenosine monophosphate-forming) synthetases in bacteria and yeast. The crystal structure of the Sir protein complexed with a peptide of a protein substrate provided insights into how sirtuins interact with their protein substrates. The silent information regulator protein (Sir2) and its homologs (collectively known as sirtuins) are NAD+-dependent deacetylase enzymes involved in chromosome stability, gene silencing and cell aging in eukaryotes and archaea. The discovery that sirtuin-dependent protein deacetylation is a NAD+-consuming reaction established a link with the energy generation systems of the cell. This link to metabolism was recently extended to the post-translational control of the activity of short-chain fatty acyl-coenzyme A (adenosine monophosphate-forming) synthetases in bacteria and yeast. The crystal structure of the Sir protein complexed with a peptide of a protein substrate provided insights into how sirtuins interact with their protein substrates. The silent information regulator protein (Sir2) and its homologs (collectively known as sirtuins) are NAD +-dependent deacetylase enzymes involved in chromosome stability, gene silencing and cell aging in eukaryotes and archaea. The discovery that sirtuin-dependent protein deacetylation is a NAD +-consuming reaction established a link with the energy generation systems of the cell. This link to metabolism was recently extended to the post-translational control of the activity of short-chain fatty acyl-coenzyme A (adenosine monophosphate-forming) synthetases in bacteria and yeast. The crystal structure of the Sir protein complexed with a peptide of a protein substrate provided insights into how sirtuins interact with their protein substrates.
Author	Escalante-Semerena, JC Takahashi, H Boeke, JD Starai, VJ
Author_xml	– sequence: 1 givenname: VJ surname: Starai fullname: Starai, VJ organization: Department of Bacteriology, University of Wisconsin-Madison, 264 Enzyme Institute, 1710 University Avenue, Madison, WI 53726-4087, USA – sequence: 2 givenname: H surname: Takahashi fullname: Takahashi, H organization: Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, 617 Hunterian Building, 725 N. Wolfe St., Baltimore, MD 21205-2185, USA – sequence: 3 givenname: JD surname: Boeke fullname: Boeke, JD organization: Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, 617 Hunterian Building, 725 N. Wolfe St., Baltimore, MD 21205-2185, USA – sequence: 4 givenname: JC surname: Escalante-Semerena fullname: Escalante-Semerena, JC email: escalante@bact.wisc.edu organization: Department of Bacteriology, University of Wisconsin-Madison, 264 Enzyme Institute, 1710 University Avenue, Madison, WI 53726-4087, USA
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/15063846$$D View this record in MEDLINE/PubMed
BookMark	eNqFkUtrHDEQhEWwiZ8_wJegU24z0Ws0I_u0mLzAkIN9F5KmB2szI60lrePNr4_MLvjmnLqhvyroqjN0FGIAhK4oaSmh8su6XbxtGSGiJawlpPuATunQq4ZwKY7qzqVqOtaLE3SW85pUUHXyIzqhHZF8EPIUvazw7MNvbKH8AQi4JBOyS35TfAzYhBH7UCAtMHqTdniBYmycfV6uscEpzoCnmPC9T6yCuDwCdjGUesBxwsZB2c2NixD-7hbAK5x3oTLFZLhAx5OZM1we5jl6-Pb14fZHc_fr-8_b1V3jhJCl4VZ1k7RSOQfjpIw1tqPAOJ-4E2xkjoq-J2JwwLvBjZwzM0iqOgZ0pHbg5-jz3naT4tMWctGLzw7m2QSI26x7OhBOevVfkPaKSjnwCtI96FLMOcGkN8kvNRxNiX6tRa-r1OrXWjRhutZSNZ8O5ltbo3xTHHqowM0egBrFs4eks_MQ6s8-gSt6jP4d-3-4QaCf
CitedBy_id	crossref_primary_10_1007_s00792_019_01090_y crossref_primary_10_3389_fcimb_2024_1408947 crossref_primary_10_1016_j_ymben_2014_11_009 crossref_primary_10_1128_ecosalplus_3_6_3_10 crossref_primary_10_1002_pmic_201200001 crossref_primary_10_1128_mBio_00216_11 crossref_primary_10_1111_j_1749_6632_2009_04538_x crossref_primary_10_1021_acs_jproteome_5b00359 crossref_primary_10_1016_j_resmic_2012_05_008 crossref_primary_10_1021_jm050100l crossref_primary_10_1111_j_1365_2958_2010_07204_x crossref_primary_10_1146_annurev_micro_020518_115526 crossref_primary_10_1002_emmm_201100180 crossref_primary_10_1111_j_1365_2958_2010_07125_x crossref_primary_10_1111_j_1365_2958_2010_07148_x crossref_primary_10_1128_EC_00189_14 crossref_primary_10_1128_MMBR_00029_06 crossref_primary_10_1039_C4MB00620H crossref_primary_10_1074_jbc_M407484200 crossref_primary_10_1128_JB_00402_15 crossref_primary_10_1007_s11010_009_0209_z crossref_primary_10_1128_IAI_00999_12 crossref_primary_10_1111_j_1365_2958_2011_07566_x crossref_primary_10_1007_s00253_016_7832_x crossref_primary_10_1016_j_cbpa_2005_08_010 crossref_primary_10_1007_s00436_006_0280_2 crossref_primary_10_1021_jp1054183 crossref_primary_10_1016_j_tplants_2012_03_008 crossref_primary_10_1007_s12013_008_9041_4 crossref_primary_10_1128_JB_00333_21 crossref_primary_10_1016_j_mib_2010_12_013 crossref_primary_10_1002_cbic_201500611 crossref_primary_10_1002_cbic_201300744 crossref_primary_10_1128_JB_188_8_3012_3023_2006 crossref_primary_10_1128_ecosalplus_3_4_4
Cites_doi	10.1016/S0378-1119(01)00358-4 10.1021/bi011858j 10.1073/pnas.0730689100 10.1074/jbc.M111830200 10.1128/MCB.23.19.7044-7054.2003 10.1046/j.1365-2958.2001.02425.x 10.1074/jbc.M004160200 10.1016/S0955-0674(03)00006-1 10.1126/science.1088697 10.1074/jbc.273.48.31788 10.1126/science.1077650 10.1074/jbc.M205670200 10.1101/gad.970902 10.1016/S0092-8674(01)00524-4 10.1111/j.1432-1033.1995.tb20751.x 10.1073/pnas.97.12.6658 10.1074/jbc.M200671200 10.1016/S1097-2765(03)00038-8 10.1126/science.1070506 10.1016/S1097-2765(02)00628-7 10.1021/bi0271603 10.1073/pnas.110148297 10.1093/nar/22.22.4673 10.1128/MMBR.67.3.376-399.2003 10.1074/jbc.M208997200 10.1021/bi015647q 10.1021/bi034959l 10.1074/jbc.M306552200 10.1074/jbc.M008782200 10.1093/genetics/163.2.545 10.1093/emboj/20.6.1353 10.1002/yea.320081207 10.1016/S0969-2126(00)00560-8 10.1038/35001622 10.1016/S0092-8674(01)00527-X
ContentType	Journal Article
Copyright	2004 Elsevier Ltd
Copyright_xml	– notice: 2004 Elsevier Ltd
DBID	CGR CUY CVF ECM EIF NPM AAYXX CITATION 7QL 7TM C1K M7N 7X8
DOI	10.1016/j.mib.2004.02.005
DatabaseName	Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed CrossRef Bacteriology Abstracts (Microbiology B) Nucleic Acids Abstracts Environmental Sciences and Pollution Management Algology Mycology and Protozoology Abstracts (Microbiology C) MEDLINE - Academic
DatabaseTitle	MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) CrossRef Bacteriology Abstracts (Microbiology B) Algology Mycology and Protozoology Abstracts (Microbiology C) Nucleic Acids Abstracts Environmental Sciences and Pollution Management MEDLINE - Academic
DatabaseTitleList	Bacteriology Abstracts (Microbiology B) 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	Biology
EISSN	1879-0364
EndPage	119
ExternalDocumentID	10_1016_j_mib_2004_02_005 15063846 S1369527404000189
Genre	Research Support, U.S. Gov't, P.H.S Review Research Support, Non-U.S. Gov't Journal Article
GrantInformation_xml	– fundername: National Institute of General Medical Sciences grantid: R01 GM062203 – fundername: NIGMS NIH HHS grantid: GM 62203 – fundername: NIGMS NIH HHS grantid: GM 40313 – fundername: NIGMS NIH HHS grantid: GM 62385
GroupedDBID	--- --K --M .1- .FO .~1 0R~ 1B1 1P~ 1RT 1~. 1~5 29F 4.4 457 4G. 53G 5GY 5VS 7-5 71M 8P~ AAAJQ AABNK AACTN AAEDT AAEDW AAIAV AAIKJ AAKOC AALRI AAOAW AAQFI AAQXK AARKO AAXUO ABBQC ABFRF ABJNI ABLVK ABMAC ABMZM ABXDB ABYKQ ACDAQ ACGFO ACGFS ACRLP ADBBV ADEZE ADMUD AEBSH AEFWE AEKER AENEX AEVXI AFCTW AFKWA AFRHN AFTJW AFXIZ AGEKW AGHFR AGUBO AGYEJ AIEXJ AIKHN AITUG AJBFU AJOXV AJRQY AJUYK ALMA_UNASSIGNED_HOLDINGS AMFUW AMRAJ ANZVX ASPBG AVWKF AXJTR AZFZN BKOJK BLXMC BNPGV CJTIS CS3 DU5 EBS EFJIC EFLBG EJD EO8 EO9 EP2 EP3 F5P FDB FEDTE FGOYB FIRID FNPLU FYGXN G-Q GBLVA HVGLF HZ~ IHE J1W KOM LCYCR LUGTX M41 MO0 N9A O-L O9- O9. OAUVE OK~ OZT P-8 P-9 P2P PC. Q38 R2- RIG ROL RPZ SCC SDF SDG SDP SES SEW SPCBC SSH SSI SSZ T5K Z5R ~G- AAHBH AAXKI AFJKZ AKRWK CGR CUY CVF ECM EIF NPM AAYXX CITATION 7QL 7TM C1K M7N 7X8
ID	FETCH-LOGICAL-c446t-3b95f6b69ccedf9abab51e233f3c42d2c1477048ce358cd332a861952e1d1b83
ISSN	1369-5274
IngestDate	Thu Oct 24 22:14:29 EDT 2024 Fri Oct 25 11:58:53 EDT 2024 Thu Sep 26 17:50:50 EDT 2024 Sat Sep 28 08:39:23 EDT 2024 Fri Feb 23 02:30:55 EST 2024
IsPeerReviewed	true
IsScholarly	true
Issue	2
Keywords	Acs NAD Sir2 NADH AMP CoA OAADPr
Language	English
LinkModel	OpenURL
MergedId	FETCHMERGED-LOGICAL-c446t-3b95f6b69ccedf9abab51e233f3c42d2c1477048ce358cd332a861952e1d1b83
Notes	ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 ObjectType-Review-3 content type line 23 ObjectType-Feature-3 ObjectType-Review-1
PMID	15063846
PQID	17916683
PQPubID	23462
PageCount	5
ParticipantIDs	proquest_miscellaneous_71803079 proquest_miscellaneous_17916683 crossref_primary_10_1016_j_mib_2004_02_005 pubmed_primary_15063846 elsevier_sciencedirect_doi_10_1016_j_mib_2004_02_005
PublicationCentury	2000
PublicationDate	2004-04-01
PublicationDateYYYYMMDD	2004-04-01
PublicationDate_xml	– month: 04 year: 2004 text: 2004-04-01 day: 01
PublicationDecade	2000
PublicationPlace	England
PublicationPlace_xml	– name: England
PublicationTitle	Current opinion in microbiology
PublicationTitleAlternate	Curr Opin Microbiol
PublicationYear	2004
Publisher	Elsevier Ltd
Publisher_xml	– name: Elsevier Ltd
References	De Virgilio, Burckert, Barth, Neuhaus, Boller, Wiemken (BIB23) 1992; 8 Jackson, Denu (BIB33) 2002; 277 Bedalov, Hirao, Posakony, Nelson, Simon (BIB18) 2003; 23 Vaziri, Dessain, Ng Eaton, Imai, Frye, Pandita, Guarente, Weinberg (BIB5) 2001; 107 Horswill, Escalante-Semerena (BIB20) 2002; 41 North, Marshall, Borra, Denu, Verdin (BIB9) 2003; 11 Starai, Takahashi, Boeke, Escalante-Semerena (BIB21) 2003; 163 Landry, Sutton, Tafrov, Heller, Stebbins, Pillus, Sternglanz (BIB2) 2000; 97 Van den Berg, Steensma (BIB22) 1995; 231 Sauve, Celic, Avalos, Deng, Boeke, Schramm (BIB31) 2001; 40 Sauve, Schramm (BIB14) 2003; 42 Luo, Nikolaev, Imai, Chen, Su, Shiloh, Guarente, Gu (BIB6) 2001; 107 Anderson, Latorre-Esteves, Neves, Lavu, Medvedik, Taylor, Howitz, Santos, Sinclair (BIB16) 2003; 302 Rafty, Schmidt, Perraud, Scharenberg, Denu (BIB34) 2002; 277 Karan, David, Capy (BIB25) 2001; 265 Fujino, Kondo, Ishikawa, Morikawa, Yamamoto (BIB26) 2001; 276 Weber, Marahiel (BIB28) 2001; 9 Starai, Celic, Cole, Boeke, Escalante-Semerena (BIB11) 2002; 298 Bitterman, Anderson, Cohen, Latorre-Esteves, Sinclair (BIB15) 2002; 277 Borra, O’Neill, Jackson, Marshall, Verdin, Foltz, Denu (BIB32) 2002; 277 Luong, Hannah, Brown, Goldstein (BIB27) 2000; 275 Kumar, Agarwal, Heyman, Matson, Heidtman, Piccirillo, Umansky, Drawid, Jansen, Liu (BIB24) 2002; 16 Gulick, Starai, Horswill, Homick, Escalante-Semerena (BIB19) 2003; 42 Lin, Guarente (BIB12) 2003; 15 Hutchinson (BIB29) 2003; 100 Muth, Nadaud, Grummt, Voit (BIB8) 2001; 20 Bitterman, Medvedik, Sinclair (BIB17) 2003; 67 Imai, Armstrong, Kaeberlein, Guarente (BIB4) 2000; 403 Tsang, Escalante-Semerena (BIB1) 1998; 273 Thompson, Higgins, Gibson (BIB35) 1994; 22 Jackson, Schmidt, Oppenheimer, Denu (BIB13) 2003; 278 Bell, Botting, Wardleworth, Jackson, White (BIB10) 2002; 296 Barak, Eisenbach (BIB30) 2001; 40 Smith, Brachmann, Celic, Kenna, Muhammad, Starai, Avalos, Escalante-Semerena, Grubmeyer, Wolberger (BIB3) 2000; 97 Avalos, Celic, Muhammad, Cosgrove, Boeke, Wolberger (BIB7) 2002; 10 Barak (10.1016/j.mib.2004.02.005_BIB30) 2001; 40 Vaziri (10.1016/j.mib.2004.02.005_BIB5) 2001; 107 Kumar (10.1016/j.mib.2004.02.005_BIB24) 2002; 16 Luong (10.1016/j.mib.2004.02.005_BIB27) 2000; 275 Rafty (10.1016/j.mib.2004.02.005_BIB34) 2002; 277 Sauve (10.1016/j.mib.2004.02.005_BIB14) 2003; 42 Borra (10.1016/j.mib.2004.02.005_BIB32) 2002; 277 Thompson (10.1016/j.mib.2004.02.005_BIB35) 1994; 22 Fujino (10.1016/j.mib.2004.02.005_BIB26) 2001; 276 Jackson (10.1016/j.mib.2004.02.005_BIB33) 2002; 277 Tsang (10.1016/j.mib.2004.02.005_BIB1) 1998; 273 Jackson (10.1016/j.mib.2004.02.005_BIB13) 2003; 278 Lin (10.1016/j.mib.2004.02.005_BIB12) 2003; 15 North (10.1016/j.mib.2004.02.005_BIB9) 2003; 11 Luo (10.1016/j.mib.2004.02.005_BIB6) 2001; 107 Anderson (10.1016/j.mib.2004.02.005_BIB16) 2003; 302 Weber (10.1016/j.mib.2004.02.005_BIB28) 2001; 9 Starai (10.1016/j.mib.2004.02.005_BIB21_1) 2003; 163 Smith (10.1016/j.mib.2004.02.005_BIB3) 2000; 97 Avalos (10.1016/j.mib.2004.02.005_BIB7_1) 2002; 10 Sauve (10.1016/j.mib.2004.02.005_BIB31) 2001; 40 Muth (10.1016/j.mib.2004.02.005_BIB8) 2001; 20 Bedalov (10.1016/j.mib.2004.02.005_BIB18) 2003; 23 Karan (10.1016/j.mib.2004.02.005_BIB25) 2001; 265 Hutchinson (10.1016/j.mib.2004.02.005_BIB29) 2003; 100 Bitterman (10.1016/j.mib.2004.02.005_BIB15) 2002; 277 De Virgilio (10.1016/j.mib.2004.02.005_BIB23) 1992; 8 Starai (10.1016/j.mib.2004.02.005_BIB11_1) 2002; 298 Bitterman (10.1016/j.mib.2004.02.005_BIB17) 2003; 67 Horswill (10.1016/j.mib.2004.02.005_BIB20) 2002; 41 Landry (10.1016/j.mib.2004.02.005_BIB2) 2000; 97 Gulick (10.1016/j.mib.2004.02.005_BIB19_1) 2003; 42 Bell (10.1016/j.mib.2004.02.005_BIB10) 2002; 296 Van den Berg (10.1016/j.mib.2004.02.005_BIB22) 1995; 231 Imai (10.1016/j.mib.2004.02.005_BIB4) 2000; 403
References_xml	– volume: 277 start-page: 45099 year: 2002 end-page: 45107 ident: BIB15 article-title: Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast publication-title: J Biol Chem contributor: fullname: Sinclair – volume: 9 start-page: R3 year: 2001 end-page: R9 ident: BIB28 article-title: Exploring the domain structure of modular nonribosomal peptide synthetases publication-title: Structure (Camb) contributor: fullname: Marahiel – volume: 97 start-page: 6658 year: 2000 end-page: 6663 ident: BIB3 article-title: A phylogenetically conserved NAD publication-title: Proc Natl Acad Sci U S A contributor: fullname: Wolberger – volume: 42 start-page: 2866 year: 2003 end-page: 2873 ident: BIB19 article-title: The 1.75Å crystal structure of acetyl-CoA synthetase bound to adenosine-5′-propylphosphate and coenzyme A publication-title: Biochemistry contributor: fullname: Escalante-Semerena – volume: 298 start-page: 2390 year: 2002 end-page: 2392 ident: BIB11 article-title: Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine publication-title: Science contributor: fullname: Escalante-Semerena – volume: 231 start-page: 704 year: 1995 end-page: 713 ident: BIB22 article-title: publication-title: Eur J Biochem contributor: fullname: Steensma – volume: 273 start-page: 31788 year: 1998 end-page: 31794 ident: BIB1 article-title: CobB, a new member of the SIR2 family of eucaryotic regulatory proteins, is required to compensate for the lack of nicotinate mononucleotide:5,6-dimethylbenzimidazole phosphoribosyltransferase activity in publication-title: J Biol Chem contributor: fullname: Escalante-Semerena – volume: 276 start-page: 11420 year: 2001 end-page: 11426 ident: BIB26 article-title: Acetyl-CoA synthetase 2, a mitochondrial matrix enzyme involved in the oxidation of acetate publication-title: J Biol Chem contributor: fullname: Yamamoto – volume: 20 start-page: 1353 year: 2001 end-page: 1362 ident: BIB8 article-title: Acetylation of TAF(I)68, a subunit of TIF-IB/SL1, activates RNA polymerase I transcription publication-title: EMBO J contributor: fullname: Voit – volume: 42 start-page: 9249 year: 2003 end-page: 9256 ident: BIB14 article-title: Sir2 regulation by nicotinamide results from switching between base exchange and deacetylation chemistry publication-title: Biochemistry contributor: fullname: Schramm – volume: 67 start-page: 376 year: 2003 end-page: 399 ident: BIB17 article-title: Longevity regulation in publication-title: Microbiol Mol Biol Rev contributor: fullname: Sinclair – volume: 277 start-page: 18535 year: 2002 end-page: 18544 ident: BIB33 article-title: Structural identification of 2′- and 3′-O-acetyl-ADP-ribose as novel metabolites derived from the Sir2 family of beta –NAD(+)-dependent histone/protein deacetylases publication-title: J Biol Chem contributor: fullname: Denu – volume: 22 start-page: 4673 year: 1994 end-page: 4680 ident: BIB35 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: 302 start-page: 2124 year: 2003 end-page: 2126 ident: BIB16 article-title: Yeast life-span extension by calorie restriction is independent of NAD fluctuation publication-title: Science contributor: fullname: Sinclair – volume: 277 start-page: 47114 year: 2002 end-page: 47122 ident: BIB34 article-title: Analysis of publication-title: J Biol Chem contributor: fullname: Denu – volume: 10 start-page: 523 year: 2002 end-page: 535 ident: BIB7 article-title: Structure of a Sir2 enzyme bound to an acetylated p53 peptide publication-title: Mol Cell contributor: fullname: Wolberger – volume: 41 start-page: 2379 year: 2002 end-page: 2387 ident: BIB20 article-title: Characterization of the propionyl-CoA synthetase (PrpE) enzyme of publication-title: Biochemistry contributor: fullname: Escalante-Semerena – volume: 275 start-page: 26458 year: 2000 end-page: 26466 ident: BIB27 article-title: Molecular characterization of human acetyl-CoA synthetase, an enzyme regulated by sterol regulatory element-binding proteins publication-title: J Biol Chem contributor: fullname: Goldstein – volume: 107 start-page: 137 year: 2001 end-page: 148 ident: BIB6 article-title: Negative control of p53 by Sir2alpha promotes cell survival under stress publication-title: Cell contributor: fullname: Gu – volume: 100 start-page: 3010 year: 2003 end-page: 3012 ident: BIB29 article-title: Polyketide and non-ribosomal peptide synthases: falling together by coming apart publication-title: Proc Natl Acad Sci U S A contributor: fullname: Hutchinson – volume: 163 start-page: 545 year: 2003 end-page: 555 ident: BIB21 article-title: Short-chain fatty acid activation by acyl-coenzyme A synthetases requires SIR2 protein function in publication-title: Genetics contributor: fullname: Escalante-Semerena – volume: 278 start-page: 50985 year: 2003 end-page: 50998 ident: BIB13 article-title: Mechanism of nicotinamide inhibition and transglycosidation by Sir2 histone/protein deacetylases publication-title: J Biol Chem contributor: fullname: Denu – volume: 403 start-page: 795 year: 2000 end-page: 800 ident: BIB4 article-title: Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase publication-title: Nature contributor: fullname: Guarente – volume: 97 start-page: 5807 year: 2000 end-page: 5811 ident: BIB2 article-title: The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases publication-title: Proc Natl Acad Sci U S A contributor: fullname: Sternglanz – volume: 296 start-page: 148 year: 2002 end-page: 151 ident: BIB10 article-title: The interaction of Alba, a conserved archaeal chromatin protein, with Sir2 and its regulation by acetylation publication-title: Science contributor: fullname: White – volume: 8 start-page: 1043 year: 1992 end-page: 1051 ident: BIB23 article-title: Cloning and disruption of a gene required for growth on acetate but not on ethanol: the acetyl-coenzyme A synthetase gene of publication-title: Yeast contributor: fullname: Wiemken – volume: 40 start-page: 15456 year: 2001 end-page: 15463 ident: BIB31 article-title: Chemistry of gene silencing: the mechanism of NAD(+)-dependent deacetylation reactions publication-title: Biochemistry contributor: fullname: Schramm – volume: 265 start-page: 95 year: 2001 end-page: 101 ident: BIB25 article-title: Molecular evolution of the AMP-forming acetyl-CoA synthetase publication-title: Gene contributor: fullname: Capy – volume: 277 start-page: 12632 year: 2002 end-page: 12641 ident: BIB32 article-title: Conserved enzymatic production and biological effect of O-acetyl-ADP-ribose by silent information regulator 2-like NAD(+)-dependent deacetylases publication-title: J Biol Chem contributor: fullname: Denu – volume: 15 start-page: 241 year: 2003 end-page: 246 ident: BIB12 article-title: Nicotinamide adenine dinucleotide, a metabolic regulator of transcription, longevity and disease publication-title: Curr Opin Cell Biol contributor: fullname: Guarente – volume: 107 start-page: 149 year: 2001 end-page: 159 ident: BIB5 article-title: hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase publication-title: Cell contributor: fullname: Weinberg – volume: 23 start-page: 7044 year: 2003 end-page: 7054 ident: BIB18 article-title: NAD+-dependent deacetylase Hst1p controls biosynthesis and cellular NAD+ levels in publication-title: Mol Cell Biol contributor: fullname: Simon – volume: 11 start-page: 437 year: 2003 end-page: 444 ident: BIB9 article-title: The human Sir2 ortholog, publication-title: Mol Cell contributor: fullname: Verdin – volume: 16 start-page: 707 year: 2002 end-page: 719 ident: BIB24 article-title: Subcellular localization of the yeast proteome publication-title: Genes Dev contributor: fullname: Liu – volume: 40 start-page: 731 year: 2001 end-page: 743 ident: BIB30 article-title: Acetylation of the response regulator, CheY, is involved in bacterial chemotaxis publication-title: Mol Microbiol contributor: fullname: Eisenbach – volume: 265 start-page: 95 year: 2001 ident: 10.1016/j.mib.2004.02.005_BIB25 article-title: Molecular evolution of the AMP-forming acetyl-CoA synthetase publication-title: Gene doi: 10.1016/S0378-1119(01)00358-4 contributor: fullname: Karan – volume: 40 start-page: 15456 year: 2001 ident: 10.1016/j.mib.2004.02.005_BIB31 article-title: Chemistry of gene silencing: the mechanism of NAD(+)-dependent deacetylation reactions publication-title: Biochemistry doi: 10.1021/bi011858j contributor: fullname: Sauve – volume: 100 start-page: 3010 year: 2003 ident: 10.1016/j.mib.2004.02.005_BIB29 article-title: Polyketide and non-ribosomal peptide synthases: falling together by coming apart publication-title: Proc Natl Acad Sci U S A doi: 10.1073/pnas.0730689100 contributor: fullname: Hutchinson – volume: 277 start-page: 12632 year: 2002 ident: 10.1016/j.mib.2004.02.005_BIB32 article-title: Conserved enzymatic production and biological effect of O-acetyl-ADP-ribose by silent information regulator 2-like NAD(+)-dependent deacetylases publication-title: J Biol Chem doi: 10.1074/jbc.M111830200 contributor: fullname: Borra – volume: 23 start-page: 7044 year: 2003 ident: 10.1016/j.mib.2004.02.005_BIB18 article-title: NAD+-dependent deacetylase Hst1p controls biosynthesis and cellular NAD+ levels in Saccharomyces cerevisiae publication-title: Mol Cell Biol doi: 10.1128/MCB.23.19.7044-7054.2003 contributor: fullname: Bedalov – volume: 40 start-page: 731 year: 2001 ident: 10.1016/j.mib.2004.02.005_BIB30 article-title: Acetylation of the response regulator, CheY, is involved in bacterial chemotaxis publication-title: Mol Microbiol doi: 10.1046/j.1365-2958.2001.02425.x contributor: fullname: Barak – volume: 275 start-page: 26458 year: 2000 ident: 10.1016/j.mib.2004.02.005_BIB27 article-title: Molecular characterization of human acetyl-CoA synthetase, an enzyme regulated by sterol regulatory element-binding proteins publication-title: J Biol Chem doi: 10.1074/jbc.M004160200 contributor: fullname: Luong – volume: 15 start-page: 241 year: 2003 ident: 10.1016/j.mib.2004.02.005_BIB12 article-title: Nicotinamide adenine dinucleotide, a metabolic regulator of transcription, longevity and disease publication-title: Curr Opin Cell Biol doi: 10.1016/S0955-0674(03)00006-1 contributor: fullname: Lin – volume: 302 start-page: 2124 year: 2003 ident: 10.1016/j.mib.2004.02.005_BIB16 article-title: Yeast life-span extension by calorie restriction is independent of NAD fluctuation publication-title: Science doi: 10.1126/science.1088697 contributor: fullname: Anderson – volume: 273 start-page: 31788 year: 1998 ident: 10.1016/j.mib.2004.02.005_BIB1 article-title: CobB, a new member of the SIR2 family of eucaryotic regulatory proteins, is required to compensate for the lack of nicotinate mononucleotide:5,6-dimethylbenzimidazole phosphoribosyltransferase activity in cobT mutants during cobalamin biosynthesis in Salmonella typhimurium LT2 publication-title: J Biol Chem doi: 10.1074/jbc.273.48.31788 contributor: fullname: Tsang – volume: 298 start-page: 2390 year: 2002 ident: 10.1016/j.mib.2004.02.005_BIB11_1 article-title: Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine publication-title: Science doi: 10.1126/science.1077650 contributor: fullname: Starai – volume: 277 start-page: 45099 year: 2002 ident: 10.1016/j.mib.2004.02.005_BIB15 article-title: Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1 publication-title: J Biol Chem doi: 10.1074/jbc.M205670200 contributor: fullname: Bitterman – volume: 16 start-page: 707 year: 2002 ident: 10.1016/j.mib.2004.02.005_BIB24 article-title: Subcellular localization of the yeast proteome publication-title: Genes Dev doi: 10.1101/gad.970902 contributor: fullname: Kumar – volume: 107 start-page: 137 year: 2001 ident: 10.1016/j.mib.2004.02.005_BIB6 article-title: Negative control of p53 by Sir2alpha promotes cell survival under stress publication-title: Cell doi: 10.1016/S0092-8674(01)00524-4 contributor: fullname: Luo – volume: 231 start-page: 704 year: 1995 ident: 10.1016/j.mib.2004.02.005_BIB22 article-title: ACS2, a Saccharomyces cerevisiae gene encoding acetyl-coenzyme A synthetase, essential for growth on glucose publication-title: Eur J Biochem doi: 10.1111/j.1432-1033.1995.tb20751.x contributor: fullname: Van den Berg – volume: 97 start-page: 6658 year: 2000 ident: 10.1016/j.mib.2004.02.005_BIB3 article-title: A phylogenetically conserved NAD+-dependent protein deacetylase activity in the Sir2 protein family publication-title: Proc Natl Acad Sci U S A doi: 10.1073/pnas.97.12.6658 contributor: fullname: Smith – volume: 277 start-page: 18535 year: 2002 ident: 10.1016/j.mib.2004.02.005_BIB33 article-title: Structural identification of 2′- and 3′-O-acetyl-ADP-ribose as novel metabolites derived from the Sir2 family of beta –NAD(+)-dependent histone/protein deacetylases publication-title: J Biol Chem doi: 10.1074/jbc.M200671200 contributor: fullname: Jackson – volume: 11 start-page: 437 year: 2003 ident: 10.1016/j.mib.2004.02.005_BIB9 article-title: The human Sir2 ortholog, SIRT2, is an NAD(+)-dependent tubulin deacetylase publication-title: Mol Cell doi: 10.1016/S1097-2765(03)00038-8 contributor: fullname: North – volume: 296 start-page: 148 year: 2002 ident: 10.1016/j.mib.2004.02.005_BIB10 article-title: The interaction of Alba, a conserved archaeal chromatin protein, with Sir2 and its regulation by acetylation publication-title: Science doi: 10.1126/science.1070506 contributor: fullname: Bell – volume: 10 start-page: 523 year: 2002 ident: 10.1016/j.mib.2004.02.005_BIB7_1 article-title: Structure of a Sir2 enzyme bound to an acetylated p53 peptide publication-title: Mol Cell doi: 10.1016/S1097-2765(02)00628-7 contributor: fullname: Avalos – volume: 42 start-page: 2866 year: 2003 ident: 10.1016/j.mib.2004.02.005_BIB19_1 article-title: The 1.75Å crystal structure of acetyl-CoA synthetase bound to adenosine-5′-propylphosphate and coenzyme A publication-title: Biochemistry doi: 10.1021/bi0271603 contributor: fullname: Gulick – volume: 97 start-page: 5807 year: 2000 ident: 10.1016/j.mib.2004.02.005_BIB2 article-title: The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases publication-title: Proc Natl Acad Sci U S A doi: 10.1073/pnas.110148297 contributor: fullname: Landry – volume: 22 start-page: 4673 year: 1994 ident: 10.1016/j.mib.2004.02.005_BIB35 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: 67 start-page: 376 year: 2003 ident: 10.1016/j.mib.2004.02.005_BIB17 article-title: Longevity regulation in Saccharomyces cerevisiae: linking metabolism, genome stability, and heterochromatin publication-title: Microbiol Mol Biol Rev doi: 10.1128/MMBR.67.3.376-399.2003 contributor: fullname: Bitterman – volume: 277 start-page: 47114 year: 2002 ident: 10.1016/j.mib.2004.02.005_BIB34 article-title: Analysis of O-acetyl-ADP-ribose as a target for nudix ADP-ribose hydrolases publication-title: J Biol Chem doi: 10.1074/jbc.M208997200 contributor: fullname: Rafty – volume: 41 start-page: 2379 year: 2002 ident: 10.1016/j.mib.2004.02.005_BIB20 article-title: Characterization of the propionyl-CoA synthetase (PrpE) enzyme of Salmonella enterica: residue Lys592 is required for propionyl-AMP synthesis publication-title: Biochemistry doi: 10.1021/bi015647q contributor: fullname: Horswill – volume: 42 start-page: 9249 year: 2003 ident: 10.1016/j.mib.2004.02.005_BIB14 article-title: Sir2 regulation by nicotinamide results from switching between base exchange and deacetylation chemistry publication-title: Biochemistry doi: 10.1021/bi034959l contributor: fullname: Sauve – volume: 278 start-page: 50985 year: 2003 ident: 10.1016/j.mib.2004.02.005_BIB13 article-title: Mechanism of nicotinamide inhibition and transglycosidation by Sir2 histone/protein deacetylases publication-title: J Biol Chem doi: 10.1074/jbc.M306552200 contributor: fullname: Jackson – volume: 276 start-page: 11420 year: 2001 ident: 10.1016/j.mib.2004.02.005_BIB26 article-title: Acetyl-CoA synthetase 2, a mitochondrial matrix enzyme involved in the oxidation of acetate publication-title: J Biol Chem doi: 10.1074/jbc.M008782200 contributor: fullname: Fujino – volume: 163 start-page: 545 year: 2003 ident: 10.1016/j.mib.2004.02.005_BIB21_1 article-title: Short-chain fatty acid activation by acyl-coenzyme A synthetases requires SIR2 protein function in Salmonella enterica and Saccharomyces cerevisiae publication-title: Genetics doi: 10.1093/genetics/163.2.545 contributor: fullname: Starai – volume: 20 start-page: 1353 year: 2001 ident: 10.1016/j.mib.2004.02.005_BIB8 article-title: Acetylation of TAF(I)68, a subunit of TIF-IB/SL1, activates RNA polymerase I transcription publication-title: EMBO J doi: 10.1093/emboj/20.6.1353 contributor: fullname: Muth – volume: 8 start-page: 1043 year: 1992 ident: 10.1016/j.mib.2004.02.005_BIB23 article-title: Cloning and disruption of a gene required for growth on acetate but not on ethanol: the acetyl-coenzyme A synthetase gene of Saccharomyces cerevisiae publication-title: Yeast doi: 10.1002/yea.320081207 contributor: fullname: De Virgilio – volume: 9 start-page: R3 year: 2001 ident: 10.1016/j.mib.2004.02.005_BIB28 article-title: Exploring the domain structure of modular nonribosomal peptide synthetases publication-title: Structure (Camb) doi: 10.1016/S0969-2126(00)00560-8 contributor: fullname: Weber – volume: 403 start-page: 795 year: 2000 ident: 10.1016/j.mib.2004.02.005_BIB4 article-title: Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase publication-title: Nature doi: 10.1038/35001622 contributor: fullname: Imai – volume: 107 start-page: 149 year: 2001 ident: 10.1016/j.mib.2004.02.005_BIB5 article-title: hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase publication-title: Cell doi: 10.1016/S0092-8674(01)00527-X contributor: fullname: Vaziri
SSID	ssj0004956
Score	1.9787964
SecondaryResourceType	review_article
Snippet	The silent information regulator protein (Sir2) and its homologs (collectively known as sirtuins) are NAD +-dependent deacetylase enzymes involved in... The silent information regulator protein (Sir2) and its homologs (collectively known as sirtuins) are NAD+-dependent deacetylase enzymes involved in chromosome... The silent information regulator protein (Sir2) and its homologs (collectively known as sirtuins) are NAD super(+)-dependent deacetylase enzymes involved in...
SourceID	proquest crossref pubmed elsevier
SourceType	Aggregation Database Index Database Publisher
StartPage	115
SubjectTerms	Acetate-CoA Ligase - metabolism Amino Acid Sequence Molecular Sequence Data Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Salmonella enterica - genetics Salmonella enterica - metabolism Sirtuins Sirtuins - genetics Sirtuins - metabolism Transcription, Genetic - physiology
Title	A link between transcription and intermediary metabolism: a role for Sir2 in the control of acetyl-coenzyme A synthetase
URI	https://dx.doi.org/10.1016/j.mib.2004.02.005 https://www.ncbi.nlm.nih.gov/pubmed/15063846 https://search.proquest.com/docview/17916683 https://search.proquest.com/docview/71803079
Volume	7
hasFullText	1
inHoldings	1
isFullTextHit
isPrint
link	http://sdu.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwtV1Lj9MwELa6XSFxQbwpTx84gbJq4jwcbhEELRy4tEJ7ixzbES3bFLWpRPj1zMR2kl1UBEhcrMp1WtfzdewZfzNDyEs4dVesnCtPSI1JteelJ7gW0IhIc6HngURX9vki-XTB3-VhPpm4mnND33-VNPSBrDFy9i-k3X8odMBrkDm0IHVo_0ju2Wu8k-35Vw3uRb1mMKmWUBtjwMiuxQLSgIJLS78QhmyIzMPFahc4DqSjsyNlQOqmvfTkVtc_2o0GtbJvaxjTuEue9dVkphiOZdmUm9WQ86n36zRiZ-phf-791UvxFcPMvgzltA2dUdvUoD1FOd9L5GU22ltglLM20W22-LJzZIz5L513zUXYDHQmVMgsTsFYNpV8zrTp40nq4f3pWIsnI7AGI43sm2hRu7n7Rj__sm8YF8b6bLMqO5-ByeMaDZtkT11c4IxwQqj95j5PT8hpAEoumpLT7EN-8XGIyk272sH9L3B36h278NoXHTsVHbN6utPP8ja5Zc0Wmhm83SETXd8lN0wh0_Ye-Z5RRB21qKNXUEcBdXSMOjqg7g0VFDFHAXMUMQcDKeCJWszRbUWvYY5mdMDcfbJ8ny_fnnu2pocnwzBuPFamURWXcSqlVlUqSlFGvg4Yq5gMAxVIP0wS2FWkZhGXirFAcLDxo0D7yi85e0Cm9bbWjwgVqgRrQKZg86oQHhVKKxVFXChfchn7M_LKLWnxzWRuKRylcV3A-mMF1rCYBwWs_4yEbtELe_Q0R8oCEPK7x144AcFbe7xrE7XeHvYFZv2NY86Oj4BDIW6w6Yw8NJIdZhmhHRHGj_9tUk_IzeHv9ZRMm91BPyMne3V4biH6E-L0yAM
link.rule.ids	315,782,786,27935,27936
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=A+link+between+transcription+and+intermediary+metabolism%3A+a+role+for+Sir2+in+the+control+of+acetyl-coenzyme+A+synthetase&rft.jtitle=Current+opinion+in+microbiology&rft.au=Starai%2C+VJ&rft.au=Takahashi%2C+H&rft.au=Boeke%2C+JD&rft.au=Escalante-Semerena%2C+JC&rft.date=2004-04-01&rft.pub=Elsevier+Ltd&rft.issn=1369-5274&rft.eissn=1879-0364&rft.volume=7&rft.issue=2&rft.spage=115&rft.epage=119&rft_id=info:doi/10.1016%2Fj.mib.2004.02.005&rft.externalDocID=S1369527404000189
thumbnail_l	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1369-5274&client=summon
thumbnail_m	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1369-5274&client=summon
thumbnail_s	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1369-5274&client=summon