Tail-tape-fused virion and non-virion RNA polymerases of a thermophilic virus with an extremely long tail

Tail-tape-fused virion and non-virion RNA polymerases of a thermophilic virus with an extremely long tail

Thermus thermophilus bacteriophage P23-45 encodes a giant 5,002-residue tail tape measure protein (TMP) that defines the length of its extraordinarily long tail. Here, we show that the N-terminal portion of P23-45 TMP is an unusual RNA polymerase (RNAP) homologous to cellular RNAPs. The TMP-fused vi...

Full description

Saved in:
Bibliographic Details
Published in:Nature communications Vol. 15; no. 1; p. 317
Main Authors: Chaban, Anastasiia, Minakhin, Leonid, Goldobina, Ekaterina, Bae, Brain, Hao, Yue, Borukhov, Sergei, Putzeys, Leena, Boon, Maarten, Kabinger, Florian, Lavigne, Rob, Makarova, Kira S., Koonin, Eugene V., Nair, Satish K., Tagami, Shunsuke, Severinov, Konstantin, Sokolova, Maria L.
Format: Journal Article
Language:English
Published: London Nature Publishing Group UK 05-01-2024
Nature Publishing Group
Nature Portfolio
Subjects:
38
38/15
49/91
631/326/1321
631/337/572
631/45/535/1266
82/1
82/16
82/80
82/83
96
Adaptability
Bacterial Typing Techniques
Bacteriophages - genetics
DNA-directed RNA polymerase
DNA-Directed RNA Polymerases - genetics
Gene duplication
Genes
Humanities and Social Sciences
multidisciplinary
Phages
Proteins
Pyridinolcarbamate
Ribonucleic acid
RNA
RNA polymerase
Science
Science (multidisciplinary)
Structure-function relationships
Virion - genetics
Virions
Viruses
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Abstract Thermus thermophilus bacteriophage P23-45 encodes a giant 5,002-residue tail tape measure protein (TMP) that defines the length of its extraordinarily long tail. Here, we show that the N-terminal portion of P23-45 TMP is an unusual RNA polymerase (RNAP) homologous to cellular RNAPs. The TMP-fused virion RNAP transcribes pre-early phage genes, including a gene that encodes another, non-virion RNAP, that transcribes early and some middle phage genes. We report the crystal structures of both P23-45 RNAPs. The non-virion RNAP has a crab-claw-like architecture. By contrast, the virion RNAP adopts a unique flat structure without a clamp. Structure and sequence comparisons of the P23-45 RNAPs with other RNAPs suggest that, despite the extensive functional differences, the two P23-45 RNAPs originate from an ancient gene duplication in an ancestral phage. Our findings demonstrate striking adaptability of RNAPs that can be attained within a single virus species. The authors describe the structure and function of two evolutionarily diverged RNA polymerases of a thermophilic phage. One of the polymerases is fused to the phage tape measure protein, a virion component dictating the length of the phage tail.
AbstractList Thermus thermophilus bacteriophage P23-45 encodes a giant 5,002-residue tail tape measure protein (TMP) that defines the length of its extraordinarily long tail. Here, we show that the N-terminal portion of P23-45 TMP is an unusual RNA polymerase (RNAP) homologous to cellular RNAPs. The TMP-fused virion RNAP transcribes pre-early phage genes, including a gene that encodes another, non-virion RNAP, that transcribes early and some middle phage genes. We report the crystal structures of both P23-45 RNAPs. The non-virion RNAP has a crab-claw-like architecture. By contrast, the virion RNAP adopts a unique flat structure without a clamp. Structure and sequence comparisons of the P23-45 RNAPs with other RNAPs suggest that, despite the extensive functional differences, the two P23-45 RNAPs originate from an ancient gene duplication in an ancestral phage. Our findings demonstrate striking adaptability of RNAPs that can be attained within a single virus species.
Thermus thermophilus bacteriophage P23-45 encodes a giant 5,002-residue tail tape measure protein (TMP) that defines the length of its extraordinarily long tail. Here, we show that the N-terminal portion of P23-45 TMP is an unusual RNA polymerase (RNAP) homologous to cellular RNAPs. The TMP-fused virion RNAP transcribes pre-early phage genes, including a gene that encodes another, non-virion RNAP, that transcribes early and some middle phage genes. We report the crystal structures of both P23-45 RNAPs. The non-virion RNAP has a crab-claw-like architecture. By contrast, the virion RNAP adopts a unique flat structure without a clamp. Structure and sequence comparisons of the P23-45 RNAPs with other RNAPs suggest that, despite the extensive functional differences, the two P23-45 RNAPs originate from an ancient gene duplication in an ancestral phage. Our findings demonstrate striking adaptability of RNAPs that can be attained within a single virus species.
Abstract Thermus thermophilus bacteriophage P23-45 encodes a giant 5,002-residue tail tape measure protein (TMP) that defines the length of its extraordinarily long tail. Here, we show that the N-terminal portion of P23-45 TMP is an unusual RNA polymerase (RNAP) homologous to cellular RNAPs. The TMP-fused virion RNAP transcribes pre-early phage genes, including a gene that encodes another, non-virion RNAP, that transcribes early and some middle phage genes. We report the crystal structures of both P23-45 RNAPs. The non-virion RNAP has a crab-claw-like architecture. By contrast, the virion RNAP adopts a unique flat structure without a clamp. Structure and sequence comparisons of the P23-45 RNAPs with other RNAPs suggest that, despite the extensive functional differences, the two P23-45 RNAPs originate from an ancient gene duplication in an ancestral phage. Our findings demonstrate striking adaptability of RNAPs that can be attained within a single virus species.
Thermus thermophilus bacteriophage P23-45 encodes a giant 5,002-residue tail tape measure protein (TMP) that defines the length of its extraordinarily long tail. Here, we show that the N-terminal portion of P23-45 TMP is an unusual RNA polymerase (RNAP) homologous to cellular RNAPs. The TMP-fused virion RNAP transcribes pre-early phage genes, including a gene that encodes another, non-virion RNAP, that transcribes early and some middle phage genes. We report the crystal structures of both P23-45 RNAPs. The non-virion RNAP has a crab-claw-like architecture. By contrast, the virion RNAP adopts a unique flat structure without a clamp. Structure and sequence comparisons of the P23-45 RNAPs with other RNAPs suggest that, despite the extensive functional differences, the two P23-45 RNAPs originate from an ancient gene duplication in an ancestral phage. Our findings demonstrate striking adaptability of RNAPs that can be attained within a single virus species.The authors describe the structure and function of two evolutionarily diverged RNA polymerases of a thermophilic phage. One of the polymerases is fused to the phage tape measure protein, a virion component dictating the length of the phage tail.
Thermus thermophilus bacteriophage P23-45 encodes a giant 5,002-residue tail tape measure protein (TMP) that defines the length of its extraordinarily long tail. Here, we show that the N-terminal portion of P23-45 TMP is an unusual RNA polymerase (RNAP) homologous to cellular RNAPs. The TMP-fused virion RNAP transcribes pre-early phage genes, including a gene that encodes another, non-virion RNAP, that transcribes early and some middle phage genes. We report the crystal structures of both P23-45 RNAPs. The non-virion RNAP has a crab-claw-like architecture. By contrast, the virion RNAP adopts a unique flat structure without a clamp. Structure and sequence comparisons of the P23-45 RNAPs with other RNAPs suggest that, despite the extensive functional differences, the two P23-45 RNAPs originate from an ancient gene duplication in an ancestral phage. Our findings demonstrate striking adaptability of RNAPs that can be attained within a single virus species. The authors describe the structure and function of two evolutionarily diverged RNA polymerases of a thermophilic phage. One of the polymerases is fused to the phage tape measure protein, a virion component dictating the length of the phage tail.
ArticleNumber 317
Author Severinov, Konstantin
Borukhov, Sergei
Koonin, Eugene V.
Goldobina, Ekaterina
Bae, Brain
Nair, Satish K.
Putzeys, Leena
Hao, Yue
Sokolova, Maria L.
Chaban, Anastasiia
Tagami, Shunsuke
Minakhin, Leonid
Lavigne, Rob
Kabinger, Florian
Boon, Maarten
Makarova, Kira S.
Author_xml – sequence: 1
  givenname: Anastasiia
  orcidid: 0000-0001-7024-2724
  surname: Chaban
  fullname: Chaban, Anastasiia
  organization: Center of Life Sciences, Skolkovo Institute of Science and Technology, RIKEN Center for Biosystems Dynamics Research, Structural and Computational Biology Unit, European Molecular Biology Laboratory (EMBL)
– sequence: 2
  givenname: Leonid
  surname: Minakhin
  fullname: Minakhin, Leonid
  organization: Waksman Institute for Microbiology, Rutgers, The State University of New Jersey, Department of Biochemistry and Molecular Biology, Thomas Jefferson University
– sequence: 3
  givenname: Ekaterina
  surname: Goldobina
  fullname: Goldobina, Ekaterina
  organization: Center of Life Sciences, Skolkovo Institute of Science and Technology, APC Microbiome Ireland, University College Cork
– sequence: 4
  givenname: Brain
  surname: Bae
  fullname: Bae, Brain
  organization: Department of Biochemistry, University of Illinois at Urbana−Champaign
– sequence: 5
  givenname: Yue
  surname: Hao
  fullname: Hao, Yue
  organization: Department of Biochemistry, University of Illinois at Urbana−Champaign
– sequence: 6
  givenname: Sergei
  orcidid: 0000-0002-3517-3003
  surname: Borukhov
  fullname: Borukhov, Sergei
  organization: Department of Cell Biology and Neuroscience, Rowan University School of Osteopathic Medicine at Stratford
– sequence: 7
  givenname: Leena
  surname: Putzeys
  fullname: Putzeys, Leena
  organization: Department of Biosystems, Laboratory of Gene Technology, KU Leuven
– sequence: 8
  givenname: Maarten
  surname: Boon
  fullname: Boon, Maarten
  organization: Department of Biosystems, Laboratory of Gene Technology, KU Leuven
– sequence: 9
  givenname: Florian
  orcidid: 0000-0002-3053-8253
  surname: Kabinger
  fullname: Kabinger, Florian
  organization: Department of Molecular Biology, Max Planck Institute for Multidisciplinary Sciences
– sequence: 10
  givenname: Rob
  orcidid: 0000-0001-7377-1314
  surname: Lavigne
  fullname: Lavigne, Rob
  organization: Department of Biosystems, Laboratory of Gene Technology, KU Leuven
– sequence: 11
  givenname: Kira S.
  orcidid: 0000-0002-8174-2844
  surname: Makarova
  fullname: Makarova, Kira S.
  organization: National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health
– sequence: 12
  givenname: Eugene V.
  orcidid: 0000-0003-3943-8299
  surname: Koonin
  fullname: Koonin, Eugene V.
  organization: National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health
– sequence: 13
  givenname: Satish K.
  orcidid: 0000-0003-1790-1334
  surname: Nair
  fullname: Nair, Satish K.
  email: snair@illinois.edu
  organization: Department of Biochemistry, University of Illinois at Urbana−Champaign
– sequence: 14
  givenname: Shunsuke
  orcidid: 0000-0002-1720-3627
  surname: Tagami
  fullname: Tagami, Shunsuke
  email: shunsuke.tagami@riken.jp
  organization: RIKEN Center for Biosystems Dynamics Research
– sequence: 15
  givenname: Konstantin
  orcidid: 0000-0001-9706-450X
  surname: Severinov
  fullname: Severinov, Konstantin
  email: severik@waksman.rutgers.edu
  organization: Waksman Institute for Microbiology, Rutgers, The State University of New Jersey, Institute of Molecular Genetics National Kurchatov Center
– sequence: 16
  givenname: Maria L.
  orcidid: 0000-0001-7251-6952
  surname: Sokolova
  fullname: Sokolova, Maria L.
  email: maria.sokolova@mpinat.mpg.de
  organization: Center of Life Sciences, Skolkovo Institute of Science and Technology, Department of Molecular Biology, Max Planck Institute for Multidisciplinary Sciences
BackLink https://www.ncbi.nlm.nih.gov/pubmed/38182597$$D View this record in MEDLINE/PubMed
BookMark eNp9kUtv1DAUhS1URMvQP8ACWWLTTcCvxMmyqnhUqkBCZW3ZzvWMR0kc7KQw_fV1mqEgFnjj13fOvfZ5iU6GMABCryl5Rwmv3ydBRSULwnghRMVJcf8MnTEiaEEl4yd_rU_ReUp7kgdvaC3EC3TKa1qzspFnyN9q3xWTHqFwc4IW3_now4D10OJcsThuv325xGPoDj1EnSDh4LDG0w5iH8ad77xddHPCP_20y1oMv6YIPXQH3IVhi6dc5BV67nSX4Pw4b9D3jx9urz4XN18_XV9d3hRW1OVU5Ma0NtQKUzaiZM5Cy0sqoGLWmkoawhkIY6XUDalN2VaMGskYbwQjunaCb9D16tsGvVdj9L2OBxW0V48HIW6VjpO3HajWMU1kKxqopbDS1doY7UgDTra2yv-1QRer1xjDjxnSpHqfLHSdHiDMSbGG5h_NeSzo23_QfZjjkF-6UERyUrOFYitlY0gpgntqkBK15KrWXFXOVT3mqu6z6M3RejY9tE-S3ylmgK9AylfDFuKf2v-xfQAGQq_A
CitedBy_id crossref_primary_10_1093_femsml_uqae002
Cites_doi 10.1016/j.virol.2016.04.030
10.1038/s41586-020-2921-5
10.1006/jmbi.1993.1012
10.1107/S2059798318017795
10.1107/S2059798318004576
10.1107/S0021889807021206
10.1101/gad.233916.113
10.1371/journal.pbio.3000122
10.1038/nature05931
10.1093/nar/gkx264
10.1016/j.jmb.2008.02.018
10.1007/978-3-319-46503-6_9
10.1093/bioinformatics/btr064
10.1016/j.cell.2019.11.023
10.1107/S0907444909012098
10.1073/pnas.98.3.892
10.1016/j.jmb.2009.10.063
10.4161/bact.29399
10.1016/j.tim.2008.03.008
10.1093/nar/gkx1162
10.1261/rna.078937.121
10.1038/ncomms15774
10.1093/nar/gkac727
10.1371/journal.pbio.0040434
10.1038/ncomms12227
10.1038/s41564-017-0053-y
10.1007/978-1-4614-0980-9_6
10.1038/nrmicro2507
10.1093/nar/gkv416
10.1016/j.jsb.2011.12.013
10.3390/biom5020647
10.1093/nar/gkq201
10.1016/j.csbj.2022.05.034
10.1038/s41467-020-15392-9
10.1074/jbc.M115.685933
10.1107/S2059798319011471
10.1016/j.coviro.2020.06.010
10.1038/nmeth1008-853
10.1107/S0907444909047337
10.1107/S0907444910007493
10.1016/j.jmb.2010.10.049
10.1107/S1744309107022506
10.4161/rna.8.1.13346
10.1021/acssynbio.2c00176
10.1038/s41467-022-31214-6
10.1038/s41579-019-0299-x
10.1128/MMBR.00010-17
10.1016/j.jmb.2019.05.017
ContentType Journal Article
Copyright The Author(s) 2024
2024. The Author(s).
The Author(s) 2024. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.
Copyright_xml – notice: The Author(s) 2024
– notice: 2024. The Author(s).
– notice: The Author(s) 2024. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.
DBID C6C
CGR
CUY
CVF
ECM
EIF
NPM
AAYXX
CITATION
3V.
7QL
7QP
7QR
7SN
7SS
7ST
7T5
7T7
7TM
7TO
7X7
7XB
88E
8AO
8FD
8FE
8FG
8FH
8FI
8FJ
8FK
ABUWG
AFKRA
ARAPS
AZQEC
BBNVY
BENPR
BGLVJ
BHPHI
C1K
CCPQU
DWQXO
FR3
FYUFA
GHDGH
GNUQQ
H94
HCIFZ
K9.
LK8
M0S
M1P
M7P
P5Z
P62
P64
PIMPY
PQEST
PQQKQ
PQUKI
RC3
SOI
7X8
DOA
DOI 10.1038/s41467-023-44630-z
DatabaseName Springer Nature OA Free Journals
Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
CrossRef
ProQuest Central (Corporate)
Bacteriology Abstracts (Microbiology B)
Calcium & Calcified Tissue Abstracts
Chemoreception Abstracts
Ecology Abstracts
Entomology Abstracts (Full archive)
Environment Abstracts
Immunology Abstracts
Industrial and Applied Microbiology Abstracts (Microbiology A)
Nucleic Acids Abstracts
Oncogenes and Growth Factors Abstracts
Health & Medical Collection (Proquest)
ProQuest Central (purchase pre-March 2016)
Medical Database (Alumni Edition)
ProQuest Pharma Collection
Technology Research Database
ProQuest SciTech Collection
ProQuest Technology Collection
ProQuest Natural Science Collection
Hospital Premium Collection
Hospital Premium Collection (Alumni Edition)
ProQuest Central (Alumni) (purchase pre-March 2016)
ProQuest Central (Alumni)
ProQuest Central UK/Ireland
Advanced Technologies & Aerospace Collection
ProQuest Central Essentials
Biological Science Collection
ProQuest Central
Technology Collection
ProQuest Natural Science Collection
Environmental Sciences and Pollution Management
ProQuest One Community College
ProQuest Central
Engineering Research Database
Health Research Premium Collection
Health Research Premium Collection (Alumni)
ProQuest Central Student
AIDS and Cancer Research Abstracts
SciTech Premium Collection
ProQuest Health & Medical Complete (Alumni)
Biological Sciences
Health & Medical Collection (Alumni Edition)
PML(ProQuest Medical Library)
Biological Science Database
Advanced Technologies & Aerospace Database
ProQuest Advanced Technologies & Aerospace Collection
Biotechnology and BioEngineering Abstracts
Publicly Available Content Database
ProQuest One Academic Eastern Edition (DO NOT USE)
ProQuest One Academic
ProQuest One Academic UKI Edition
Genetics Abstracts
Environment Abstracts
MEDLINE - Academic
Directory of Open Access Journals
DatabaseTitle MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
CrossRef
Publicly Available Content Database
ProQuest Central Student
Oncogenes and Growth Factors Abstracts
ProQuest Advanced Technologies & Aerospace Collection
ProQuest Central Essentials
Nucleic Acids Abstracts
SciTech Premium Collection
Environmental Sciences and Pollution Management
Health Research Premium Collection
Natural Science Collection
Biological Science Collection
Chemoreception Abstracts
Industrial and Applied Microbiology Abstracts (Microbiology A)
ProQuest Medical Library (Alumni)
Advanced Technologies & Aerospace Collection
ProQuest Biological Science Collection
ProQuest One Academic Eastern Edition
ProQuest Hospital Collection
ProQuest Technology Collection
Health Research Premium Collection (Alumni)
Biological Science Database
Ecology Abstracts
ProQuest Hospital Collection (Alumni)
Biotechnology and BioEngineering Abstracts
Entomology Abstracts
ProQuest Health & Medical Complete
ProQuest One Academic UKI Edition
Engineering Research Database
ProQuest One Academic
Calcium & Calcified Tissue Abstracts
Technology Collection
Technology Research Database
ProQuest Health & Medical Complete (Alumni)
ProQuest Central (Alumni Edition)
ProQuest One Community College
ProQuest Natural Science Collection
ProQuest Pharma Collection
ProQuest Central
Genetics Abstracts
Health and Medicine Complete (Alumni Edition)
ProQuest Central Korea
Bacteriology Abstracts (Microbiology B)
AIDS and Cancer Research Abstracts
ProQuest SciTech Collection
Advanced Technologies & Aerospace Database
ProQuest Medical Library
Immunology Abstracts
Environment Abstracts
ProQuest Central (Alumni)
MEDLINE - Academic
DatabaseTitleList CrossRef
MEDLINE - Academic
MEDLINE

Publicly Available Content Database
Database_xml – sequence: 1
  dbid: DOA
  name: Directory of Open Access Journals
  url: http://www.doaj.org/
  sourceTypes: Open Website
– sequence: 2
  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 2041-1723
EndPage 317
ExternalDocumentID oai_doaj_org_article_df2a07d49e874c7f8abbaf09ef7dc600
10_1038_s41467_023_44630_z
38182597
Genre Journal Article
GrantInformation_xml – fundername: NIGMS NIH HHS
  grantid: R01 GM059295
GroupedDBID ---
0R~
39C
3V.
53G
5VS
70F
7X7
88E
8AO
8FE
8FG
8FH
8FI
8FJ
AAHBH
AAJSJ
ABUWG
ACGFO
ACGFS
ACIWK
ACMJI
ACPRK
ACSMW
ADBBV
ADFRT
ADRAZ
AENEX
AFKRA
AFRAH
AHMBA
AJTQC
ALIPV
ALMA_UNASSIGNED_HOLDINGS
AMTXH
AOIJS
ARAPS
ASPBG
AVWKF
AZFZN
BBNVY
BCNDV
BENPR
BGLVJ
BHPHI
BPHCQ
BVXVI
C6C
CCPQU
DIK
EBLON
EBS
EE.
EMOBN
F5P
FEDTE
FYUFA
GROUPED_DOAJ
HCIFZ
HMCUK
HVGLF
HYE
HZ~
KQ8
LGEZI
LK8
LOTEE
M1P
M48
M7P
M~E
NADUK
NAO
NXXTH
O9-
OK1
P2P
P62
PIMPY
PQQKQ
PROAC
PSQYO
RNS
RNT
RNTTT
RPM
SNYQT
SV3
TSG
UKHRP
CGR
CUY
CVF
ECM
EIF
NPM
AAYXX
CITATION
7QL
7QP
7QR
7SN
7SS
7ST
7T5
7T7
7TM
7TO
7XB
8FD
8FK
AZQEC
C1K
DWQXO
FR3
GNUQQ
H94
K9.
P64
PQEST
PQUKI
RC3
SOI
7X8
ID FETCH-LOGICAL-c485t-182aab1c4b59452fced3514e62ccb67b032e4bc77a908b5d621b72239420a8f43
IEDL.DBID DOA
ISSN 2041-1723
IngestDate Tue Oct 22 15:05:31 EDT 2024
Fri Oct 25 09:22:27 EDT 2024
Sat Oct 26 22:25:21 EDT 2024
Thu Nov 21 23:30:02 EST 2024
Sat Nov 02 12:30:09 EDT 2024
Fri Oct 11 20:46:00 EDT 2024
IsDoiOpenAccess true
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Issue 1
Language English
License 2024. The Author(s).
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c485t-182aab1c4b59452fced3514e62ccb67b032e4bc77a908b5d621b72239420a8f43
Notes ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ORCID 0000-0002-8174-2844
0000-0001-7024-2724
0000-0002-3053-8253
0000-0001-9706-450X
0000-0002-3517-3003
0000-0002-1720-3627
0000-0001-7251-6952
0000-0001-7377-1314
0000-0003-3943-8299
0000-0003-1790-1334
OpenAccessLink https://doaj.org/article/df2a07d49e874c7f8abbaf09ef7dc600
PMID 38182597
PQID 2910730820
PQPubID 546298
PageCount 1
ParticipantIDs doaj_primary_oai_doaj_org_article_df2a07d49e874c7f8abbaf09ef7dc600
proquest_miscellaneous_2911841030
proquest_journals_2910730820
crossref_primary_10_1038_s41467_023_44630_z
pubmed_primary_38182597
springer_journals_10_1038_s41467_023_44630_z
PublicationCentury 2000
PublicationDate 2024-01-05
PublicationDateYYYYMMDD 2024-01-05
PublicationDate_xml – month: 01
  year: 2024
  text: 2024-01-05
  day: 05
PublicationDecade 2020
PublicationPlace London
PublicationPlace_xml – name: London
– name: England
PublicationTitle Nature communications
PublicationTitleAbbrev Nat Commun
PublicationTitleAlternate Nat Commun
PublicationYear 2024
Publisher Nature Publishing Group UK
Nature Publishing Group
Nature Portfolio
Publisher_xml – name: Nature Publishing Group UK
– name: Nature Publishing Group
– name: Nature Portfolio
References Sauguet, Raia, Henneke, Delarue (CR29) 2016; 7
Severinov, Minakhin, Sekine, Lopatina, Yokoyama (CR20) 2014; 4
Forrest, James, Yuzenkova, Zenkin (CR14) 2017; 8
Ruprich-Robert, Thuriaux (CR11) 2010; 38
Emsley, Lohkamp, Scott, Cowtan (CR46) 2010; 66
Kim (CR40) 2008; 5
Iyer, Aravind (CR8) 2012; 179
Hillen (CR13) 2019; 179
Werner, Grohmann (CR3) 2011; 9
CR30
Cui (CR23) 2022; 50
Drobysheva (CR18) 2021; 589
Putzeys (CR26) 2022; 20
Raia (CR28) 2019; 17
CR48
Ooi (CR19) 2018; 46
Van Duyne, Standaert, Karplus, Schreiber, Clardy (CR39) 1993; 229
Madru (CR31) 2020; 11
Lane, Darst (CR5) 2010; 395
Naville, Ghuillot-Gaudeffroy, Marchais, Gautheret (CR38) 2011; 8
Yakunina (CR17) 2015; 43
Ishihama (CR4) 1981; 14
Berdygulova (CR7) 2011; 405
Bailey, Elkan (CR51) 1994; 2
Alfi (CR27) 2022; 11
Rauert, Eddine, Kaufmann, Weiss, Janowski (CR41) 2007; 63
Davidson, Cardarelli, Pell, Radford, Maxwell (CR32) 2012; 726
Minakhin (CR22) 2008; 378
CR10
Sokolova (CR16) 2017; 45
Griesenbeck, Tschochner, Grohmann (CR1) 2017; 83
McCoy (CR49) 2007; 40
Qian (CR24) 2016; 291
Grunberger, Ferreira-Cerca, Grohmann (CR35) 2022; 28
Linares, Arnaud, Degroux, Schoehn, Breyton (CR33) 2020; 45
Grant, Bailey, Noble (CR37) 2011; 27
Vassylyev (CR50) 2007; 448
Yamashita, Hirata, Yamamoto (CR43) 2018; 74
Minakhin (CR6) 2001; 98
Hirata (CR42) 2019; 75
Tagami (CR21) 2014; 28
Fraser (CR15) 2022; 13
Lavysh (CR9) 2016; 495
Makarova (CR52) 2020; 18
Terwilliger (CR45) 2009; 65
Bailey, Johnson, Grant, Noble (CR36) 2015; 43
Kabsch (CR44) 2010; 66
Salgado (CR25) 2006; 4
Liebschner (CR47) 2019; 75
Werner (CR2) 2008; 16
Lenneman, Rothman-Denes (CR34) 2015; 5
Yutin (CR12) 2018; 3
M Yakunina (44630_CR17) 2015; 43
L Sauguet (44630_CR29) 2016; 7
P Emsley (44630_CR46) 2010; 66
44630_CR10
M Naville (44630_CR38) 2011; 8
P Raia (44630_CR28) 2019; 17
DG Vassylyev (44630_CR50) 2007; 448
L Minakhin (44630_CR6) 2001; 98
TC Terwilliger (44630_CR45) 2009; 65
F Werner (44630_CR2) 2008; 16
PS Salgado (44630_CR25) 2006; 4
K Yamashita (44630_CR43) 2018; 74
D Liebschner (44630_CR47) 2019; 75
44630_CR48
K Severinov (44630_CR20) 2014; 4
F Grunberger (44630_CR35) 2022; 28
TL Bailey (44630_CR51) 1994; 2
K Hirata (44630_CR42) 2019; 75
WY Ooi (44630_CR19) 2018; 46
C Madru (44630_CR31) 2020; 11
WJ Lane (44630_CR5) 2010; 395
AJ McCoy (44630_CR49) 2007; 40
A Ishihama (44630_CR4) 1981; 14
L Minakhin (44630_CR22) 2008; 378
W Rauert (44630_CR41) 2007; 63
44630_CR30
G Ruprich-Robert (44630_CR11) 2010; 38
BR Lenneman (44630_CR34) 2015; 5
M Sokolova (44630_CR16) 2017; 45
W Kabsch (44630_CR44) 2010; 66
R Cui (44630_CR23) 2022; 50
Y Kim (44630_CR40) 2008; 5
J Griesenbeck (44630_CR1) 2017; 83
A Alfi (44630_CR27) 2022; 11
KS Makarova (44630_CR52) 2020; 18
GD Van Duyne (44630_CR39) 1993; 229
A Fraser (44630_CR15) 2022; 13
S Tagami (44630_CR21) 2014; 28
HS Hillen (44630_CR13) 2019; 179
D Forrest (44630_CR14) 2017; 8
F Werner (44630_CR3) 2011; 9
N Yutin (44630_CR12) 2018; 3
AV Drobysheva (44630_CR18) 2021; 589
TL Bailey (44630_CR36) 2015; 43
Z Berdygulova (44630_CR7) 2011; 405
LM Iyer (44630_CR8) 2012; 179
CE Grant (44630_CR37) 2011; 27
X Qian (44630_CR24) 2016; 291
R Linares (44630_CR33) 2020; 45
D Lavysh (44630_CR9) 2016; 495
L Putzeys (44630_CR26) 2022; 20
AR Davidson (44630_CR32) 2012; 726
References_xml – volume: 14
  start-page: 1
  year: 1981
  end-page: 35
  ident: CR4
  article-title: Subunit of assembly of Escherichia coli RNA polymerase
  publication-title: Adv. Biophys.
  contributor:
    fullname: Ishihama
– volume: 495
  start-page: 185
  year: 2016
  end-page: 196
  ident: CR9
  article-title: The genome of AR9, a giant transducing Bacillus phage encoding two multisubunit RNA polymerases
  publication-title: Virology
  doi: 10.1016/j.virol.2016.04.030
  contributor:
    fullname: Lavysh
– volume: 589
  start-page: 306
  year: 2021
  end-page: 309
  ident: CR18
  article-title: Structure and function of virion RNA polymerase of a crAss-like phage
  publication-title: Nature
  doi: 10.1038/s41586-020-2921-5
  contributor:
    fullname: Drobysheva
– volume: 229
  start-page: 105
  year: 1993
  end-page: 124
  ident: CR39
  article-title: Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin
  publication-title: J. Mol. Biol.
  doi: 10.1006/jmbi.1993.1012
  contributor:
    fullname: Clardy
– volume: 75
  start-page: 138
  year: 2019
  end-page: 150
  ident: CR42
  article-title: ZOO: an automatic data-collection system for high-throughput structure analysis in protein microcrystallography
  publication-title: Acta. Crystallogr. Sect. D.
  doi: 10.1107/S2059798318017795
  contributor:
    fullname: Hirata
– volume: 74
  start-page: 441
  year: 2018
  end-page: 449
  ident: CR43
  article-title: KAMO: towards automated data processing for microcrystals
  publication-title: Acta. Crystallogr. Sect. D.
  doi: 10.1107/S2059798318004576
  contributor:
    fullname: Yamamoto
– volume: 40
  start-page: 658
  year: 2007
  end-page: 674
  ident: CR49
  article-title: Phaser crystallographic software
  publication-title: J. Appl. Crystallogr.
  doi: 10.1107/S0021889807021206
  contributor:
    fullname: McCoy
– volume: 28
  start-page: 521
  year: 2014
  end-page: 531
  ident: CR21
  article-title: Structural basis for promoter specificity switching of RNA polymerase by a phage factor
  publication-title: Genes Dev.
  doi: 10.1101/gad.233916.113
  contributor:
    fullname: Tagami
– volume: 17
  start-page: e3000122
  year: 2019
  ident: CR28
  article-title: Structure of the DP1-DP2 PolD complex bound with DNA and its implications for the evolutionary history of DNA and RNA polymerases
  publication-title: PLoS Biol.
  doi: 10.1371/journal.pbio.3000122
  contributor:
    fullname: Raia
– volume: 448
  start-page: 163
  year: 2007
  end-page: 168
  ident: CR50
  article-title: Structural basis for substrate loading in bacterial RNA polymerase
  publication-title: Nature
  doi: 10.1038/nature05931
  contributor:
    fullname: Vassylyev
– volume: 45
  start-page: 5958
  year: 2017
  end-page: 5967
  ident: CR16
  article-title: A non-canonical multisubunit RNA polymerase encoded by the AR9 phage recognizes the template strand of its uracil-containing promoters
  publication-title: Nuc. Acids Res.
  doi: 10.1093/nar/gkx264
  contributor:
    fullname: Sokolova
– volume: 378
  start-page: 468
  year: 2008
  end-page: 480
  ident: CR22
  article-title: Genome comparison and proteomic characterization of Thermus thermophilus bacteriophages P23-45 and P74-26: siphoviruses with triplex-forming sequences and the longest known tails
  publication-title: J. Mol. Biol.
  doi: 10.1016/j.jmb.2008.02.018
  contributor:
    fullname: Minakhin
– volume: 83
  start-page: 225
  year: 2017
  end-page: 270
  ident: CR1
  article-title: Structure and function of RNA polymerases and the transcription machineries
  publication-title: Subcell. Biochem.
  doi: 10.1007/978-3-319-46503-6_9
  contributor:
    fullname: Grohmann
– volume: 27
  start-page: 1017
  year: 2011
  end-page: 1018
  ident: CR37
  article-title: FIMO: scanning for occurrences of a given motif
  publication-title: Bioinformatics
  doi: 10.1093/bioinformatics/btr064
  contributor:
    fullname: Noble
– volume: 179
  start-page: 1525
  year: 2019
  end-page: 1536.e1512
  ident: CR13
  article-title: Structural basis of Poxvirus transcription: transcribing and capping vaccinia complexes
  publication-title: Cell
  doi: 10.1016/j.cell.2019.11.023
  contributor:
    fullname: Hillen
– volume: 65
  start-page: 582
  year: 2009
  end-page: 601
  ident: CR45
  article-title: Decision-making in structure solution using Bayesian estimates of map quality: the phenix autoSol wizard
  publication-title: Acta. Crystallogr. Sect. D.
  doi: 10.1107/S0907444909012098
  contributor:
    fullname: Terwilliger
– volume: 98
  start-page: 892
  year: 2001
  end-page: 897
  ident: CR6
  article-title: Bacterial RNA polymerase subunit omega and eukaryotic RNA polymerase subunit RPB6 are sequence, structural, and functional homologs and promote RNA polymerase assembly
  publication-title: Proc. Natl Acad. Sci. USA
  doi: 10.1073/pnas.98.3.892
  contributor:
    fullname: Minakhin
– volume: 395
  start-page: 686
  year: 2010
  end-page: 704
  ident: CR5
  article-title: Molecular evolution of multisubunit RNA polymerases: structural analysis
  publication-title: J. Mol. Biol.
  doi: 10.1016/j.jmb.2009.10.063
  contributor:
    fullname: Darst
– volume: 4
  start-page: e29399
  year: 2014
  ident: CR20
  article-title: Molecular basis of RNA polymerase promoter specificity switch revealed through studies of Thermus bacteriophage transcription regulator
  publication-title: Bacteriophage
  doi: 10.4161/bact.29399
  contributor:
    fullname: Yokoyama
– volume: 16
  start-page: 247
  year: 2008
  end-page: 250
  ident: CR2
  article-title: Structural evolution of multisubunit RNA polymerases
  publication-title: Trends Microbiol.
  doi: 10.1016/j.tim.2008.03.008
  contributor:
    fullname: Werner
– volume: 46
  start-page: 431
  year: 2018
  end-page: 441
  ident: CR19
  article-title: A thermus phage protein inhibits host RNA polymerase by preventing template DNA strand loading during open promoter complex formation
  publication-title: Nuc. Acids Res.
  doi: 10.1093/nar/gkx1162
  contributor:
    fullname: Ooi
– volume: 28
  start-page: 400
  year: 2022
  end-page: 417
  ident: CR35
  article-title: Nanopore sequencing of RNA and cDNA molecules in escherichia coli
  publication-title: RNA
  doi: 10.1261/rna.078937.121
  contributor:
    fullname: Grohmann
– volume: 8
  year: 2017
  ident: CR14
  article-title: Single-peptide DNA-dependent RNA polymerase homologous to multi-subunit RNA polymerase
  publication-title: Nat. Commun.
  doi: 10.1038/ncomms15774
  contributor:
    fullname: Zenkin
– volume: 50
  start-page: 10169
  year: 2022
  end-page: 10186
  ident: CR23
  article-title: Structural insights into the dual activities of the two-barrel RNA polymerase QDE-1
  publication-title: Nuc. Acids Res.
  doi: 10.1093/nar/gkac727
  contributor:
    fullname: Cui
– volume: 4
  start-page: e434
  year: 2006
  ident: CR25
  article-title: The structure of an RNAi polymerase links RNA silencing and transcription
  publication-title: PLoS Biol.
  doi: 10.1371/journal.pbio.0040434
  contributor:
    fullname: Salgado
– volume: 7
  year: 2016
  ident: CR29
  article-title: Shared active site architecture between archaeal PolD and multi-subunit RNA polymerases revealed by X-ray crystallography
  publication-title: Nat. Commun.
  doi: 10.1038/ncomms12227
  contributor:
    fullname: Delarue
– ident: CR30
– ident: CR10
– volume: 3
  start-page: 38
  year: 2018
  end-page: 46
  ident: CR12
  article-title: Discovery of an expansive bacteriophage family that includes the most abundant viruses from the human gut
  publication-title: Nat. Microbiol.
  doi: 10.1038/s41564-017-0053-y
  contributor:
    fullname: Yutin
– volume: 726
  start-page: 115
  year: 2012
  end-page: 142
  ident: CR32
  article-title: Long noncontractile tail machines of bacteriophages
  publication-title: Adv. Exp. Med. Biol.
  doi: 10.1007/978-1-4614-0980-9_6
  contributor:
    fullname: Maxwell
– volume: 9
  start-page: 85
  year: 2011
  end-page: 98
  ident: CR3
  article-title: Evolution of multisubunit RNA polymerases in the three domains of life
  publication-title: Nat. Rev. Microbiol.
  doi: 10.1038/nrmicro2507
  contributor:
    fullname: Grohmann
– volume: 43
  start-page: W39
  year: 2015
  end-page: W49
  ident: CR36
  article-title: The MEME suite
  publication-title: Nuc. Acids Res.
  doi: 10.1093/nar/gkv416
  contributor:
    fullname: Noble
– volume: 179
  start-page: 299
  year: 2012
  end-page: 319
  ident: CR8
  article-title: Insights from the architecture of the bacterial transcription apparatus
  publication-title: J. Struct. Biol.
  doi: 10.1016/j.jsb.2011.12.013
  contributor:
    fullname: Aravind
– volume: 5
  start-page: 647
  year: 2015
  end-page: 667
  ident: CR34
  article-title: Structural and biochemical investigation of bacteriophage N4-encoded RNA polymerases
  publication-title: Biomolecules
  doi: 10.3390/biom5020647
  contributor:
    fullname: Rothman-Denes
– volume: 38
  start-page: 4559
  year: 2010
  end-page: 4569
  ident: CR11
  article-title: Non-canonical DNA transcription enzymes and the conservation of two-barrel RNA polymerases
  publication-title: Nuc. Acids Res.
  doi: 10.1093/nar/gkq201
  contributor:
    fullname: Thuriaux
– volume: 20
  start-page: 2624
  year: 2022
  end-page: 2638
  ident: CR26
  article-title: Development of ONT-cappable-seq to unravel the transcriptional landscape of Pseudomonas phages
  publication-title: Comput. Struct. Biotechnol. J.
  doi: 10.1016/j.csbj.2022.05.034
  contributor:
    fullname: Putzeys
– volume: 11
  year: 2020
  ident: CR31
  article-title: Structural basis for the increased processivity of D-family DNA polymerases in complex with PCNA
  publication-title: Nat. Commun.
  doi: 10.1038/s41467-020-15392-9
  contributor:
    fullname: Madru
– volume: 291
  start-page: 9295
  year: 2016
  end-page: 9309
  ident: CR24
  article-title: Functional evolution in orthologous cell-encoded RNA-dependent RNA polymerases
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M115.685933
  contributor:
    fullname: Qian
– volume: 75
  start-page: 861
  year: 2019
  end-page: 877
  ident: CR47
  article-title: Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix
  publication-title: Acta. Crystallogr. Sect. D.
  doi: 10.1107/S2059798319011471
  contributor:
    fullname: Liebschner
– volume: 45
  start-page: 34
  year: 2020
  end-page: 42
  ident: CR33
  article-title: Structure, function and assembly of the long, flexible tail of siphophages
  publication-title: Curr. Opin. Virol.
  doi: 10.1016/j.coviro.2020.06.010
  contributor:
    fullname: Breyton
– volume: 5
  start-page: 853
  year: 2008
  end-page: 854
  ident: CR40
  article-title: Large-scale evaluation of protein reductive methylation for improving protein crystallization
  publication-title: Nat. Methods
  doi: 10.1038/nmeth1008-853
  contributor:
    fullname: Kim
– ident: CR48
– volume: 66
  start-page: 125
  year: 2010
  end-page: 132
  ident: CR44
  article-title: XDS
  publication-title: Acta. Crystallogr. Sect. D.
  doi: 10.1107/S0907444909047337
  contributor:
    fullname: Kabsch
– volume: 66
  start-page: 486
  year: 2010
  end-page: 501
  ident: CR46
  article-title: Features and development of Coot
  publication-title: Acta. Crystallogr. Sect. D.
  doi: 10.1107/S0907444910007493
  contributor:
    fullname: Cowtan
– volume: 2
  start-page: 28
  year: 1994
  end-page: 36
  ident: CR51
  article-title: Fitting a mixture model by expectation maximization to discover motifs in biopolymers
  publication-title: Proc. Int. Conf. Intell. Syst. Mol. Biol.
  contributor:
    fullname: Elkan
– volume: 405
  start-page: 125
  year: 2011
  end-page: 142
  ident: CR7
  article-title: Temporal regulation of gene expression of the thermus thermophilus bacteriophage P23-45
  publication-title: J. Mol. Biol.
  doi: 10.1016/j.jmb.2010.10.049
  contributor:
    fullname: Berdygulova
– volume: 63
  start-page: 507
  year: 2007
  end-page: 511
  ident: CR41
  article-title: Reductive methylation to improve crystallization of the putative oxidoreductase Rv0765c from mycobacterium tuberculosis
  publication-title: Acta. Crystallogr. Sect. F. Struct. Biol. Cryst. Commun.
  doi: 10.1107/S1744309107022506
  contributor:
    fullname: Janowski
– volume: 8
  start-page: 11
  year: 2011
  end-page: 13
  ident: CR38
  article-title: ARNold: a web tool for the prediction of Rho-independent transcription terminators
  publication-title: RNA Biol.
  doi: 10.4161/rna.8.1.13346
  contributor:
    fullname: Gautheret
– volume: 43
  start-page: 10411
  year: 2015
  end-page: 10420
  ident: CR17
  article-title: A non-canonical multisubunit RNA polymerase encoded by a giant bacteriophage
  publication-title: Nuc. Acids Res.
  contributor:
    fullname: Yakunina
– volume: 11
  start-page: 2022
  year: 2022
  end-page: 2028
  ident: CR27
  article-title: Cell-free mutant analysis combined with structure prediction of a lasso peptide biosynthetic protease B2
  publication-title: ACS Synth. Biol.
  doi: 10.1021/acssynbio.2c00176
  contributor:
    fullname: Alfi
– volume: 13
  year: 2022
  ident: CR15
  article-title: Structural basis of template strand deoxyuridine promoter recognition by a viral RNA polymerase
  publication-title: Nat. Commun.
  doi: 10.1038/s41467-022-31214-6
  contributor:
    fullname: Fraser
– volume: 18
  start-page: 67
  year: 2020
  end-page: 83
  ident: CR52
  article-title: Evolutionary classification of CRISPR-cas systems: a burst of class 2 and derived variants
  publication-title: Nat. Rev. Microbiol
  doi: 10.1038/s41579-019-0299-x
  contributor:
    fullname: Makarova
– volume: 66
  start-page: 486
  year: 2010
  ident: 44630_CR46
  publication-title: Acta. Crystallogr. Sect. D.
  doi: 10.1107/S0907444910007493
  contributor:
    fullname: P Emsley
– volume: 405
  start-page: 125
  year: 2011
  ident: 44630_CR7
  publication-title: J. Mol. Biol.
  doi: 10.1016/j.jmb.2010.10.049
  contributor:
    fullname: Z Berdygulova
– volume: 11
  start-page: 2022
  year: 2022
  ident: 44630_CR27
  publication-title: ACS Synth. Biol.
  doi: 10.1021/acssynbio.2c00176
  contributor:
    fullname: A Alfi
– volume: 13
  year: 2022
  ident: 44630_CR15
  publication-title: Nat. Commun.
  doi: 10.1038/s41467-022-31214-6
  contributor:
    fullname: A Fraser
– volume: 75
  start-page: 861
  year: 2019
  ident: 44630_CR47
  publication-title: Acta. Crystallogr. Sect. D.
  doi: 10.1107/S2059798319011471
  contributor:
    fullname: D Liebschner
– volume: 20
  start-page: 2624
  year: 2022
  ident: 44630_CR26
  publication-title: Comput. Struct. Biotechnol. J.
  doi: 10.1016/j.csbj.2022.05.034
  contributor:
    fullname: L Putzeys
– volume: 726
  start-page: 115
  year: 2012
  ident: 44630_CR32
  publication-title: Adv. Exp. Med. Biol.
  doi: 10.1007/978-1-4614-0980-9_6
  contributor:
    fullname: AR Davidson
– volume: 17
  start-page: e3000122
  year: 2019
  ident: 44630_CR28
  publication-title: PLoS Biol.
  doi: 10.1371/journal.pbio.3000122
  contributor:
    fullname: P Raia
– volume: 2
  start-page: 28
  year: 1994
  ident: 44630_CR51
  publication-title: Proc. Int. Conf. Intell. Syst. Mol. Biol.
  contributor:
    fullname: TL Bailey
– volume: 229
  start-page: 105
  year: 1993
  ident: 44630_CR39
  publication-title: J. Mol. Biol.
  doi: 10.1006/jmbi.1993.1012
  contributor:
    fullname: GD Van Duyne
– volume: 43
  start-page: 10411
  year: 2015
  ident: 44630_CR17
  publication-title: Nuc. Acids Res.
  contributor:
    fullname: M Yakunina
– volume: 14
  start-page: 1
  year: 1981
  ident: 44630_CR4
  publication-title: Adv. Biophys.
  contributor:
    fullname: A Ishihama
– volume: 16
  start-page: 247
  year: 2008
  ident: 44630_CR2
  publication-title: Trends Microbiol.
  doi: 10.1016/j.tim.2008.03.008
  contributor:
    fullname: F Werner
– volume: 45
  start-page: 5958
  year: 2017
  ident: 44630_CR16
  publication-title: Nuc. Acids Res.
  doi: 10.1093/nar/gkx264
  contributor:
    fullname: M Sokolova
– volume: 5
  start-page: 853
  year: 2008
  ident: 44630_CR40
  publication-title: Nat. Methods
  doi: 10.1038/nmeth1008-853
  contributor:
    fullname: Y Kim
– volume: 40
  start-page: 658
  year: 2007
  ident: 44630_CR49
  publication-title: J. Appl. Crystallogr.
  doi: 10.1107/S0021889807021206
  contributor:
    fullname: AJ McCoy
– volume: 74
  start-page: 441
  year: 2018
  ident: 44630_CR43
  publication-title: Acta. Crystallogr. Sect. D.
  doi: 10.1107/S2059798318004576
  contributor:
    fullname: K Yamashita
– volume: 38
  start-page: 4559
  year: 2010
  ident: 44630_CR11
  publication-title: Nuc. Acids Res.
  doi: 10.1093/nar/gkq201
  contributor:
    fullname: G Ruprich-Robert
– volume: 4
  start-page: e434
  year: 2006
  ident: 44630_CR25
  publication-title: PLoS Biol.
  doi: 10.1371/journal.pbio.0040434
  contributor:
    fullname: PS Salgado
– volume: 179
  start-page: 299
  year: 2012
  ident: 44630_CR8
  publication-title: J. Struct. Biol.
  doi: 10.1016/j.jsb.2011.12.013
  contributor:
    fullname: LM Iyer
– volume: 98
  start-page: 892
  year: 2001
  ident: 44630_CR6
  publication-title: Proc. Natl Acad. Sci. USA
  doi: 10.1073/pnas.98.3.892
  contributor:
    fullname: L Minakhin
– volume: 4
  start-page: e29399
  year: 2014
  ident: 44630_CR20
  publication-title: Bacteriophage
  doi: 10.4161/bact.29399
  contributor:
    fullname: K Severinov
– ident: 44630_CR10
  doi: 10.1128/MMBR.00010-17
– volume: 3
  start-page: 38
  year: 2018
  ident: 44630_CR12
  publication-title: Nat. Microbiol.
  doi: 10.1038/s41564-017-0053-y
  contributor:
    fullname: N Yutin
– volume: 9
  start-page: 85
  year: 2011
  ident: 44630_CR3
  publication-title: Nat. Rev. Microbiol.
  doi: 10.1038/nrmicro2507
  contributor:
    fullname: F Werner
– volume: 11
  year: 2020
  ident: 44630_CR31
  publication-title: Nat. Commun.
  doi: 10.1038/s41467-020-15392-9
  contributor:
    fullname: C Madru
– volume: 28
  start-page: 400
  year: 2022
  ident: 44630_CR35
  publication-title: RNA
  doi: 10.1261/rna.078937.121
  contributor:
    fullname: F Grunberger
– volume: 28
  start-page: 521
  year: 2014
  ident: 44630_CR21
  publication-title: Genes Dev.
  doi: 10.1101/gad.233916.113
  contributor:
    fullname: S Tagami
– volume: 448
  start-page: 163
  year: 2007
  ident: 44630_CR50
  publication-title: Nature
  doi: 10.1038/nature05931
  contributor:
    fullname: DG Vassylyev
– volume: 75
  start-page: 138
  year: 2019
  ident: 44630_CR42
  publication-title: Acta. Crystallogr. Sect. D.
  doi: 10.1107/S2059798318017795
  contributor:
    fullname: K Hirata
– volume: 495
  start-page: 185
  year: 2016
  ident: 44630_CR9
  publication-title: Virology
  doi: 10.1016/j.virol.2016.04.030
  contributor:
    fullname: D Lavysh
– volume: 7
  year: 2016
  ident: 44630_CR29
  publication-title: Nat. Commun.
  doi: 10.1038/ncomms12227
  contributor:
    fullname: L Sauguet
– volume: 46
  start-page: 431
  year: 2018
  ident: 44630_CR19
  publication-title: Nuc. Acids Res.
  doi: 10.1093/nar/gkx1162
  contributor:
    fullname: WY Ooi
– volume: 18
  start-page: 67
  year: 2020
  ident: 44630_CR52
  publication-title: Nat. Rev. Microbiol
  doi: 10.1038/s41579-019-0299-x
  contributor:
    fullname: KS Makarova
– volume: 83
  start-page: 225
  year: 2017
  ident: 44630_CR1
  publication-title: Subcell. Biochem.
  doi: 10.1007/978-3-319-46503-6_9
  contributor:
    fullname: J Griesenbeck
– ident: 44630_CR48
– volume: 63
  start-page: 507
  year: 2007
  ident: 44630_CR41
  publication-title: Acta. Crystallogr. Sect. F. Struct. Biol. Cryst. Commun.
  doi: 10.1107/S1744309107022506
  contributor:
    fullname: W Rauert
– volume: 27
  start-page: 1017
  year: 2011
  ident: 44630_CR37
  publication-title: Bioinformatics
  doi: 10.1093/bioinformatics/btr064
  contributor:
    fullname: CE Grant
– volume: 65
  start-page: 582
  year: 2009
  ident: 44630_CR45
  publication-title: Acta. Crystallogr. Sect. D.
  doi: 10.1107/S0907444909012098
  contributor:
    fullname: TC Terwilliger
– volume: 8
  start-page: 11
  year: 2011
  ident: 44630_CR38
  publication-title: RNA Biol.
  doi: 10.4161/rna.8.1.13346
  contributor:
    fullname: M Naville
– volume: 45
  start-page: 34
  year: 2020
  ident: 44630_CR33
  publication-title: Curr. Opin. Virol.
  doi: 10.1016/j.coviro.2020.06.010
  contributor:
    fullname: R Linares
– ident: 44630_CR30
  doi: 10.1016/j.jmb.2019.05.017
– volume: 5
  start-page: 647
  year: 2015
  ident: 44630_CR34
  publication-title: Biomolecules
  doi: 10.3390/biom5020647
  contributor:
    fullname: BR Lenneman
– volume: 589
  start-page: 306
  year: 2021
  ident: 44630_CR18
  publication-title: Nature
  doi: 10.1038/s41586-020-2921-5
  contributor:
    fullname: AV Drobysheva
– volume: 66
  start-page: 125
  year: 2010
  ident: 44630_CR44
  publication-title: Acta. Crystallogr. Sect. D.
  doi: 10.1107/S0907444909047337
  contributor:
    fullname: W Kabsch
– volume: 8
  year: 2017
  ident: 44630_CR14
  publication-title: Nat. Commun.
  doi: 10.1038/ncomms15774
  contributor:
    fullname: D Forrest
– volume: 378
  start-page: 468
  year: 2008
  ident: 44630_CR22
  publication-title: J. Mol. Biol.
  doi: 10.1016/j.jmb.2008.02.018
  contributor:
    fullname: L Minakhin
– volume: 43
  start-page: W39
  year: 2015
  ident: 44630_CR36
  publication-title: Nuc. Acids Res.
  doi: 10.1093/nar/gkv416
  contributor:
    fullname: TL Bailey
– volume: 395
  start-page: 686
  year: 2010
  ident: 44630_CR5
  publication-title: J. Mol. Biol.
  doi: 10.1016/j.jmb.2009.10.063
  contributor:
    fullname: WJ Lane
– volume: 179
  start-page: 1525
  year: 2019
  ident: 44630_CR13
  publication-title: Cell
  doi: 10.1016/j.cell.2019.11.023
  contributor:
    fullname: HS Hillen
– volume: 291
  start-page: 9295
  year: 2016
  ident: 44630_CR24
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M115.685933
  contributor:
    fullname: X Qian
– volume: 50
  start-page: 10169
  year: 2022
  ident: 44630_CR23
  publication-title: Nuc. Acids Res.
  doi: 10.1093/nar/gkac727
  contributor:
    fullname: R Cui
SSID ssj0000391844
Score 2.4964428
Snippet Thermus thermophilus bacteriophage P23-45 encodes a giant 5,002-residue tail tape measure protein (TMP) that defines the length of its extraordinarily long...
Thermus thermophilus bacteriophage P23-45 encodes a giant 5,002-residue tail tape measure protein (TMP) that defines the length of its extraordinarily long...
Abstract Thermus thermophilus bacteriophage P23-45 encodes a giant 5,002-residue tail tape measure protein (TMP) that defines the length of its extraordinarily...
SourceID doaj
proquest
crossref
pubmed
springer
SourceType Open Website
Aggregation Database
Index Database
Publisher
StartPage 317
SubjectTerms 38
38/15
49/91
631/326/1321
631/337/572
631/45/535/1266
82/1
82/16
82/80
82/83
96
Adaptability
Bacterial Typing Techniques
Bacteriophages - genetics
DNA-directed RNA polymerase
DNA-Directed RNA Polymerases - genetics
Gene duplication
Genes
Humanities and Social Sciences
multidisciplinary
Phages
Proteins
Pyridinolcarbamate
Ribonucleic acid
RNA
RNA polymerase
Science
Science (multidisciplinary)
Structure-function relationships
Virion - genetics
Virions
Viruses
Title Tail-tape-fused virion and non-virion RNA polymerases of a thermophilic virus with an extremely long tail
URI https://link.springer.com/article/10.1038/s41467-023-44630-z
https://www.ncbi.nlm.nih.gov/pubmed/38182597
https://www.proquest.com/docview/2910730820
https://search.proquest.com/docview/2911841030
https://doaj.org/article/df2a07d49e874c7f8abbaf09ef7dc600
Volume 15
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://sdu.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV1Lb9QwELagEhIXBJRHoFSuxA2seh07do4FWvXUQykSN8tPtNKyWTWbSttfz4yTXUCAuPSYxI7sb-x5eTxDyFttkk5NcKyppWfS5JYBz_PMiDq3EuSxl3g5-fyzvvhqPp1impxdqS-MCRvTA4_AHccsHNdRtsloGXQ2znuXeZuyjgGkdeG-vPnFmCo8uG7BdJHTLRlem-NeFp4AIoqBBVRzdvubJCoJ-_-mZf5xQloEz9lj8mjSGOnJONIn5F5aPiUPxhqSm30yv3LzBVu7VWJ56FOkN_NrwJq6ZaRg2rPp8fLihK66xQZ9UH3qaZepo6j8fe9W6FMJ2G_oKfploS8Fno2ew8WGLrrlN4pxps_Il7PTq4_nbKqfwII0as3AdHDOz4L0qpVK5JAixu2nRoTgG-15LZL0QWvXcuNVbMTMa4G10gV3Jsv6OdmDgaaXGACFpqHJMx689CDDnIpRy9j4RqnQqoq822JpV2OaDFuOt2tjR-QtIG8L8va2Ih8Q7l1LTHFdXgDh7UR4-z_CV-RgSyw77bveCtB-NGbggc9Hu8-wY_AYxC1TN5Q2sDawvFpFXoxE3o0E9RcwCHVF3m-p_vPn_57Qq7uY0GvyUIDGVPw76oDsra-H9Ibc7-NwWBb3YXFF_QC0w_1w
link.rule.ids 315,782,786,866,2106,27933,27934
linkProvider Directory of Open Access Journals
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=Tail-tape-fused+virion+and+non-virion+RNA+polymerases+of+a+thermophilic+virus+with+an+extremely+long+tail&rft.jtitle=Nature+communications&rft.au=Chaban%2C+Anastasiia&rft.au=Minakhin%2C+Leonid&rft.au=Goldobina%2C+Ekaterina&rft.au=Bae%2C+Brain&rft.date=2024-01-05&rft.pub=Nature+Publishing+Group+UK&rft.eissn=2041-1723&rft.volume=15&rft.issue=1&rft_id=info:doi/10.1038%2Fs41467-023-44630-z&rft.externalDocID=10_1038_s41467_023_44630_z
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=2041-1723&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=2041-1723&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=2041-1723&client=summon