Difference between revisions of "RpoB"
Line 107: | Line 107: | ||
** [[YvrI]]-[[RpoB]] {{PubMed|19940246}}, | ** [[YvrI]]-[[RpoB]] {{PubMed|19940246}}, | ||
** [[Mfd]]-[[RpoB]] {{PubMed|20702425}} | ** [[Mfd]]-[[RpoB]] {{PubMed|20702425}} | ||
+ | ** [[RpoB]]-[[RpoE]] (demonstrated for ''S. aureus'') {{PubMed|24491578}} | ||
* '''[[Localization]]:''' membrane associated [http://www.ncbi.nlm.nih.gov/pubmed/18763711 PubMed] | * '''[[Localization]]:''' membrane associated [http://www.ncbi.nlm.nih.gov/pubmed/18763711 PubMed] | ||
Line 169: | Line 170: | ||
==Original publications== | ==Original publications== | ||
− | <pubmed> 19680289 17644585 | + | <pubmed> 19680289 17644585 24491578 7657605,12486038,10675340,7592585, 20525796, 17981983, 18763711, 19191541 21512256 21821766 22517742 24572018 22484477,20702425,20817769</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 14:55, 26 April 2015
- Description: RNA polymerase beta subunit
Gene name | rpoB |
Synonyms | |
Essential | yes PubMed |
Product | RNA polymerase beta subunit |
Function | transcription |
Gene expression levels in SubtiExpress: rpoB | |
Interactions involving this protein in SubtInteract: RpoB | |
MW, pI | 133 kDa, 4.731 |
Gene length, protein length | 3579 bp, 1193 aa |
Immediate neighbours | ybxB, rpoC |
Sequences | Protein DNA DNA_with_flanks |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
transcription, essential genes, membrane proteins, phosphoproteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU01070
Phenotypes of a mutant
essential PubMed
Database entries
- BsubCyc: BSU01070
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
- A mutation was found in this gene after evolution under relaxed selection for sporulation PubMed
- mutations in mtrB, sigB, rpoB, and rpoC allow B. subtilis to grow with 4-fluorotryptophan rather than with tryptophan as a canonical amino acid of the genetic code PubMed
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1) (according to Swiss-Prot)
- Protein family: RNA polymerase beta chain family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Modification:
- phosphorylated on (Arg-312 OR Arg-313), Arg-539, (Arg-693 OR Arg-694), Arg-827, and Arg-1106 PubMed
- Effectors of protein activity:
- Interactions:
- RpoA-RpoB-RpoC PubMed, NusA-RpoB PubMed
- SigA-(RpoB-RpoC) PubMed, SigB-(RpoB-RpoC)
- SigD-(RpoB-RpoC), SigE-(RpoB-RpoC)
- SigF-(RpoB-RpoC), SigG-(RpoB-RpoC)
- SigH-(RpoB-RpoC), SigI-(RpoB-RpoC)
- SigK-(RpoB-RpoC), SigL-(RpoB-RpoC)
- SigM-(RpoB-RpoC), SigV-(RpoB-RpoC)
- SigW-(RpoB-RpoC), SigX-(RpoB-RpoC)
- SigY-(RpoB-RpoC), SigZ-(RpoB-RpoC)
- Xpf-(RpoB-RpoC), YlaC-(RpoB-RpoC)
- YvrI-RpoB PubMed,
- Mfd-RpoB PubMed
- RpoB-RpoE (demonstrated for S. aureus) PubMed
- Localization: membrane associated PubMed
Database entries
- BsubCyc: BSU01070
- Structure:
- UniProt: P37870
- KEGG entry: [3]
- E.C. number: 2.7.7.6
Additional information
- subject to Clp-dependent proteolysis upon glucose starvation PubMed
Expression and regulation
- Regulatory mechanism:
- Additional information:
- subject to Clp-dependent proteolysis upon glucose starvation PubMed
- The mRNA has a long 5' leader region. This may indicate RNA-based regulation PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium): 3434 PubMed
- number of protein molecules per cell (complex medium with amino acids, without glucose): 10168 PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 1411 PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 800 PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 802 PubMed
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Fabian Commichau's lab
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Reviews
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)
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)
Original publications