Difference between revisions of "RpoB"

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Line 96: Line 96:
 
** [[Xpf]]-([[RpoB]]-[[RpoC]]), [[YlaC]]-([[RpoB]]-[[RpoC]])
 
** [[Xpf]]-([[RpoB]]-[[RpoC]]), [[YlaC]]-([[RpoB]]-[[RpoC]])
 
** [[YvrI]]-[[RpoB]] {{PubMed|19940246}},
 
** [[YvrI]]-[[RpoB]] {{PubMed|19940246}},
 +
** [[Mfd]]-[[RpoB]] {{PubMed|20702425}}
  
 
* '''Localization:''' membrane associated [http://www.ncbi.nlm.nih.gov/pubmed/18763711 PubMed]
 
* '''Localization:''' membrane associated [http://www.ncbi.nlm.nih.gov/pubmed/18763711 PubMed]
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* '''Structure:'''
 
* '''Structure:'''
 +
** [http://www.pdb.org/pdb/explore/explore.do?structureId=3MLQ 3MLQ] (RNA polymerase interacting domain
 +
of ''Thermus thermophilus'' [[Mfd]] with the ''Thermus aquaticus'' [[RpoB]] beta1 domain) {{PubMed|20702425}}
  
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P37870 P37870]
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P37870 P37870]
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<pubmed> 19680289 17644585  7657605,12486038,10675340,7592585, 20525796, 17981983, 18763711, 19191541 20817769 </pubmed>
 
<pubmed> 19680289 17644585  7657605,12486038,10675340,7592585, 20525796, 17981983, 18763711, 19191541 20817769 </pubmed>
−
 
+
'''Additional publications:''' {{PubMed|20702425}}
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 13:19, 16 December 2010

Gene name rpoB
Synonyms
Essential yes PubMed
Product RNA polymerase beta subunit
Function transcription
MW, pI 133 kDa, 4.731
Gene length, protein length 3579 bp, 1193 aa
Immediate neighbours ybxB, rpoC
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
RpoB context.gif
This image was kindly provided by SubtiList



Categories containing this gene/protein

transcription, essential genes, membrane proteins

This gene is a member of the following regulons

stringent response

The gene

Basic information

  • Locus tag: BSU01070

Phenotypes of a mutant

essential PubMed

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

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:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization: membrane associated PubMed

Database entries

  • Structure:
    • 3MLQ (RNA polymerase interacting domain 
of Thermus thermophilus Mfd with the Thermus aquaticus RpoB beta1 domain) PubMed
  • KEGG entry: [3]

Additional information

  • subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

  • Regulation:
    • RelA dependent downregulation (Class I) during stringent response PubMed
  • 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

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Shu Ishikawa, Taku Oshima, Ken Kurokawa, Yoko Kusuya, Naotake Ogasawara
RNA polymerase trafficking in Bacillus subtilis cells.
J Bacteriol: 2010, 192(21);5778-87
[PubMed:20817769] [WorldCat.org] [DOI] (I p)

Irnov Irnov, Cynthia M Sharma, Jörg Vogel, Wade C Winkler
Identification of regulatory RNAs in Bacillus subtilis.
Nucleic Acids Res: 2010, 38(19);6637-51
[PubMed:20525796] [WorldCat.org] [DOI] (I p)

Xiao Yang, Seeseei Molimau, Geoff P Doherty, Elecia B Johnston, Jon Marles-Wright, Rosalba Rothnagel, Ben Hankamer, Richard J Lewis, Peter J Lewis
The structure of bacterial RNA polymerase in complex with the essential transcription elongation factor NusA.
EMBO Rep: 2009, 10(9);997-1002
[PubMed:19680289] [WorldCat.org] [DOI] (I p)

Amy E Perkins, Andrew C Schuerger, Wayne L Nicholson
Isolation of rpoB mutations causing rifampicin resistance in Bacillus subtilis spores exposed to simulated Martian surface conditions.
Astrobiology: 2008, 8(6);1159-67
[PubMed:19191541] [WorldCat.org] [DOI] (I p)

Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711] [WorldCat.org] [DOI] (I p)

Ulf Gerth, Holger Kock, Ilja Kusters, Stephan Michalik, Robert L Switzer, Michael Hecker
Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis.
J Bacteriol: 2008, 190(1);321-31
[PubMed:17981983] [WorldCat.org] [DOI] (I p)

Amy E Perkins, Wayne L Nicholson
Uncovering new metabolic capabilities of Bacillus subtilis using phenotype profiling of rifampin-resistant rpoB mutants.
J Bacteriol: 2008, 190(3);807-14
[PubMed:17644585] [WorldCat.org] [DOI] (I p)

Claudia Rollenhagen, Haike Antelmann, Janine Kirstein, Olivier Delumeau, Michael Hecker, Michael D Yudkin
Binding of sigma(A) and sigma(B) to core RNA polymerase after environmental stress in Bacillus subtilis.
J Bacteriol: 2003, 185(1);35-40
[PubMed:12486038] [WorldCat.org] [DOI] (P p)

P J Lewis, S D Thaker, J Errington
Compartmentalization of transcription and translation in Bacillus subtilis.
EMBO J: 2000, 19(4);710-8
[PubMed:10675340] [WorldCat.org] [DOI] (P p)

X Yang, C W Price
Streptolydigin resistance can be conferred by alterations to either the beta or beta' subunits of Bacillus subtilis RNA polymerase.
J Biol Chem: 1995, 270(41);23930-3
[PubMed:7592585] [WorldCat.org] [DOI] (P p)

K J Boor, M L Duncan, C W Price
Genetic and transcriptional organization of the region encoding the beta subunit of Bacillus subtilis RNA polymerase.
J Biol Chem: 1995, 270(35);20329-36
[PubMed:7657605] [WorldCat.org] [DOI] (P p)

Additional publications: PubMed

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