Difference between revisions of "RNA polymerase"
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<br><br><br><br><br> | <br><br><br><br><br> | ||
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=='''The enzyme responsible for [[transcription]]'''== | =='''The enzyme responsible for [[transcription]]'''== | ||
| + | * As an important difference as compared to the ''E. coli'' enzyme, the ''B. subtilis'' RNA polymerase has a strong preference for G as first nucleotides in transcripts {{PubMed|23761441}} | ||
==Components of the RNA polymerase== | ==Components of the RNA polymerase== | ||
| Line 29: | Line 29: | ||
===Small accessory subunits=== | ===Small accessory subunits=== | ||
* [[RpoE]]: delta subunit | * [[RpoE]]: delta subunit | ||
| + | * [[RpoY]]: epsilon subunit | ||
* [[YloH]]: omega subunit | * [[YloH]]: omega subunit | ||
| − | ===Other | + | ===Other interaction partners=== |
* [[NusA]]: essential elongation factor | * [[NusA]]: essential elongation factor | ||
| + | * [[NusG]]: transcription elongation factor {{PubMed|36745813}} | ||
| + | * [[GreA]]: resolves promoter proximal pausing of RNA polymerase {{PubMed|21515770}} | ||
| + | * [[CshA]]: [[DEAD-box RNA helicases|DEAD-box RNA helicase]] {{PubMed|21710567}} | ||
| + | * [[PcrA]]: ATP-dependent DNA helicase {{PubMed|24147116,21710567}} | ||
| + | |||
| + | ===Temporary interaction partners=== | ||
| + | * [[Spx]]: transcription regulator, interacts with [[RpoA]] | ||
| + | * [[MgsR]]: transcription regulator orthologous to [[Spx]], interacts with [[RpoA]] | ||
| + | * [[Btr]]: transcription activator {{PubMed|22210890}} | ||
| + | * [[YlyA]]: modulates [[SigG]]-dependent transcription {{PubMed|23678950}} | ||
| + | |||
| + | * '''Additional interaction partners of the RNA polymerase (no specific subunit specified)''' | ||
| + | ** [[HelD]], [[TopA]], [[CssR]], [[RnhC]], [[YpsC]], [[Mfd]], [[YpiA]], [[YdjO]], [[ResD]] {{PubMed|21710567}} | ||
==Back to [[protein-protein interactions]]== | ==Back to [[protein-protein interactions]]== | ||
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==References== | ==References== | ||
===Reviews=== | ===Reviews=== | ||
| − | <pubmed> 18599813 7708009 18410247 19889534 19489723 18280161 21233849 </pubmed> | + | <pubmed> 18599813 7708009 18410247 19889534 19489723 18280161 21233849 22210308 23433801 23768203 24763425 25878038 26132790 26010401 16524917,28657884,29856930 32920946</pubmed> |
| + | |||
===The structure of RNA polymerase=== | ===The structure of RNA polymerase=== | ||
| − | <pubmed> 12732296 12581657 11297923 19735077 </pubmed> | + | <pubmed> 12732296 12581657 11297923 19735077 26293966 28652344 36745813 |
| − | ===Important original publications | + | </pubmed> |
| − | <pubmed> 21350489 </pubmed> | + | |
| + | === Important original publications === | ||
| + | <pubmed> 21350489 21515770 22333917,20817769,20724389,21710567 23761441 23875654 23771146 24789973 25961799 26400263 27622946 27977677 29454936 31548377 32848247 33243850,36972428, 37949068 </pubmed> | ||
Latest revision as of 17:54, 20 November 2023
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Contents
The enzyme responsible for transcription
- As an important difference as compared to the E. coli enzyme, the B. subtilis RNA polymerase has a strong preference for G as first nucleotides in transcripts PubMed
Components of the RNA polymerase
Core subunits
Sigma factors
- In addition to the housekeeping sigma factor, SigA, there are several other sigma factors with different promoter recognition specifiity that are active under specific conditions (such as stress or sporulation)
Small accessory subunits
Other interaction partners
- NusA: essential elongation factor
- NusG: transcription elongation factor PubMed
- GreA: resolves promoter proximal pausing of RNA polymerase PubMed
- CshA: DEAD-box RNA helicase PubMed
- PcrA: ATP-dependent DNA helicase PubMed
Temporary interaction partners
- Spx: transcription regulator, interacts with RpoA
- MgsR: transcription regulator orthologous to Spx, interacts with RpoA
- Btr: transcription activator PubMed
- YlyA: modulates SigG-dependent transcription PubMed
- Additional interaction partners of the RNA polymerase (no specific subunit specified)
Back to protein-protein interactions
References
Reviews
Juha Kurkela, Julia Fredman, Tiina A Salminen, Taina Tyystjärvi
Revealing secrets of the enigmatic omega subunit of bacterial RNA polymerase.
Mol Microbiol: 2021, 115(1);1-11
[PubMed:32920946]
[WorldCat.org]
[DOI]
(I p)
Kevin S Lang, Houra Merrikh
The Clash of Macromolecular Titans: Replication-Transcription Conflicts in Bacteria.
Annu Rev Microbiol: 2018, 72;71-88
[PubMed:29856930]
[WorldCat.org]
[DOI]
(I p)
Thomas Fouqueau, Fabian Blombach, Finn Werner
Evolutionary Origins of Two-Barrel RNA Polymerases and Site-Specific Transcription Initiation.
Annu Rev Microbiol: 2017, 71;331-348
[PubMed:28657884]
[WorldCat.org]
[DOI]
(I p)
Georgiy A Belogurov, Irina Artsimovitch
Regulation of Transcript Elongation.
Annu Rev Microbiol: 2015, 69;49-69
[PubMed:26132790]
[WorldCat.org]
[DOI]
(I p)
Nan Zhang, Martin Buck
A perspective on the enhancer dependent bacterial RNA polymerase.
Biomolecules: 2015, 5(2);1012-9
[PubMed:26010401]
[WorldCat.org]
[DOI]
(I e)
Andy Weiss, Lindsey N Shaw
Small things considered: the small accessory subunits of RNA polymerase in Gram-positive bacteria.
FEMS Microbiol Rev: 2015, 39(4);541-54
[PubMed:25878038]
[WorldCat.org]
[DOI]
(I p)
Nikolay Zenkin
Multiple personalities of the RNA polymerase active centre.
Microbiology (Reading): 2014, 160(Pt 7);1316-1320
[PubMed:24763425]
[WorldCat.org]
[DOI]
(I p)
Kimberly B Decker, Deborah M Hinton
Transcription regulation at the core: similarities among bacterial, archaeal, and eukaryotic RNA polymerases.
Annu Rev Microbiol: 2013, 67;113-39
[PubMed:23768203]
[WorldCat.org]
[DOI]
(I p)
Katelyn McGary, Evgeny Nudler
RNA polymerase and the ribosome: the close relationship.
Curr Opin Microbiol: 2013, 16(2);112-7
[PubMed:23433801]
[WorldCat.org]
[DOI]
(I p)
Lakshminarayan M Iyer, L Aravind
Insights from the architecture of the bacterial transcription apparatus.
J Struct Biol: 2012, 179(3);299-319
[PubMed:22210308]
[WorldCat.org]
[DOI]
(I p)
Finn Werner, Dina Grohmann
Evolution of multisubunit RNA polymerases in the three domains of life.
Nat Rev Microbiol: 2011, 9(2);85-98
[PubMed:21233849]
[WorldCat.org]
[DOI]
(I p)
Vladimir Svetlov, Evgeny Nudler
Macromolecular micromovements: how RNA polymerase translocates.
Curr Opin Struct Biol: 2009, 19(6);701-7
[PubMed:19889534]
[WorldCat.org]
[DOI]
(I p)
Evgeny Nudler
RNA polymerase active center: the molecular engine of transcription.
Annu Rev Biochem: 2009, 78;335-61
[PubMed:19489723]
[WorldCat.org]
[DOI]
(I p)
P J Lewis, G P Doherty, J Clarke
Transcription factor dynamics.
Microbiology (Reading): 2008, 154(Pt 7);1837-1844
[PubMed:18599813]
[WorldCat.org]
[DOI]
(P p)
Kristina M Herbert, William J Greenleaf, Steven M Block
Single-molecule studies of RNA polymerase: motoring along.
Annu Rev Biochem: 2008, 77;149-76
[PubMed:18410247]
[WorldCat.org]
[DOI]
(P p)
Sergei Borukhov, Evgeny Nudler
RNA polymerase: the vehicle of transcription.
Trends Microbiol: 2008, 16(3);126-34
[PubMed:18280161]
[WorldCat.org]
[DOI]
(P p)
Vincent Trinh, Marie-France Langelier, Jacques Archambault, Benoit Coulombe
Structural perspective on mutations affecting the function of multisubunit RNA polymerases.
Microbiol Mol Biol Rev: 2006, 70(1);12-36
[PubMed:16524917]
[WorldCat.org]
[DOI]
(P p)
W G Haldenwang
The sigma factors of Bacillus subtilis.
Microbiol Rev: 1995, 59(1);1-30
[PubMed:7708009]
[WorldCat.org]
[DOI]
(P p)
The structure of RNA polymerase
Important original publications
