RpoC

• Description: RNA polymerase beta' subunit
  
  

Gene name	rpoC
Synonyms
Essential	yes PubMed
Product	RNA polymerase beta' subunit
Function	transcription
Gene expression levels in SubtiExpress: rpoC
Interactions involving this protein in SubtInteract: RpoC
MW, pI	133 kDa, 8.863
Gene length, protein length	3597 bp, 1199 aa
Immediate neighbours	rpoB, ybxF
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

transcription, essential genes, membrane proteins, phosphoproteins

This gene is a member of the following regulons

stringent response

The gene

Basic information

• Locus tag: BSU01080

Phenotypes of a mutant

essential PubMed

Database entries

• BsubCyc: BSU01080

• DBTBS entry: no entry

• SubtiList entry: [1]

Additional information

• 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:

• Domains:

• Modification:
  • phosphorylated on Arg-335 and Arg-803 PubMed

• Cofactors:

• Effectors of protein activity:

• Interactions:
  • RpoA-RpoB-RpoC 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)
  • YvrHa-RpoC PubMed

• Localization:
  • colocalizes with the nucleoid PubMed
  • membrane associated PubMed

Database entries

• BsubCyc: BSU01080

• Structure:

• UniProt: P37871

• KEGG entry: [2]

• E.C. number: 2.7.7.6

Expression and regulation

• Operon:

• Expression browser: rpoC PubMed

• Sigma factor:

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

• Regulatory mechanism:

• Additional information:
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 2487 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 8264 PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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

Andrew N Keller, Xiao Yang, Jana Wiedermannová, Olivier Delumeau, Libor Krásný, Peter J Lewis
ε, a new subunit of RNA polymerase found in gram-positive bacteria.
J Bacteriol: 2014, 196(20);3622-32
[PubMed:25092033] [WorldCat.org] [DOI] (I p)

Allen Chi-Shing Yu, Aldrin Kay-Yuen Yim, Wai-Kin Mat, Amy Hin-Yan Tong, Si Lok, Hong Xue, Stephen Kwok-Wing Tsui, J Tze-Fei Wong, Ting-Fung Chan
Mutations enabling displacement of tryptophan by 4-fluorotryptophan as a canonical amino acid of the genetic code.
Genome Biol Evol: 2014, 6(3);629-41
[PubMed:24572018] [WorldCat.org] [DOI] (I p)

Yong Heon Lee, Ki Hyun Nam, John D Helmann
A mutation of the RNA polymerase β' subunit (rpoC) confers cephalosporin resistance in Bacillus subtilis.
Antimicrob Agents Chemother: 2013, 57(1);56-65
[PubMed:23070162] [WorldCat.org] [DOI] (I p)

Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742] [WorldCat.org] [DOI] (I p)

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)

Elecia B Johnston, Peter J Lewis, Renate Griffith
The interaction of Bacillus subtilis sigmaA with RNA polymerase.
Protein Sci: 2009, 18(11);2287-97
[PubMed:19735077] [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)

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)

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)