Difference between revisions of "RpoB"

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(Biological materials)
(Biological materials)
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* '''lacZ fusion:'''
 
* '''lacZ fusion:'''
 +
** GP2047 (aphA3) based on [[pAC7]], available in [[Jörg Stülke]]'s lab
 +
** GP2052 (cat) based on [[pAC5]], available in [[Jörg Stülke]]'s lab
  
 
* '''GFP fusion:'''
 
* '''GFP fusion:'''

Revision as of 07:55, 17 July 2015

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
RpoB context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
RpoB expression.png















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: BSU01070

Phenotypes of a mutant

essential PubMed

Database entries

  • 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:

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
    • 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:
  • 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


Original publications