Difference between revisions of "RpmE"

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(Expression and regulation)
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=Expression and regulation=
 
=Expression and regulation=
  
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* '''Operon:''' ''rpmE'' {{PubMed|9353933}}
  
 
* '''Sigma factor:'''  
 
* '''Sigma factor:'''  
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* '''Regulatory mechanism:'''  
 
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=Biological materials =
 
=Biological materials =

Revision as of 20:11, 2 February 2010

Gene name rpmE
Synonyms
Essential yes PubMed
Product ribosomal protein L31
Function translation
MW, pI 7 kDa, 9.157
Gene length, protein length 198 bp, 66 aa
Immediate neighbours tdk, rho
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
RpmE context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU37070

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:
  • Protein family: Type A subfamily (according to Swiss-Prot)
  • Paralogous protein(s): YtiA

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity: Zn(2+) PubMed
  • Interactions:
  • Localization:

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Under conditions of zinc starvation, RpmE is replaced by its paralog YtiA, that does not require zinc PubMed


Expression and regulation

  • Sigma factor:
  • Regulation:
    • RelA dependent downregulation (Class I) during stringent response PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Matthew A Lauber, William E Running, James P Reilly
B. subtilis ribosomal proteins: structural homology and post-translational modifications.
J Proteome Res: 2009, 8(9);4193-206
[PubMed:19653700] [WorldCat.org] [DOI] (P p)

Scott E Gabriel, John D Helmann
Contributions of Zur-controlled ribosomal proteins to growth under zinc starvation conditions.
J Bacteriol: 2009, 191(19);6116-22
[PubMed:19648245] [WorldCat.org] [DOI] (I p)

Yousuke Natori, Hideaki Nanamiya, Genki Akanuma, Saori Kosono, Toshiaki Kudo, Kozo Ochi, Fujio Kawamura
A fail-safe system for the ribosome under zinc-limiting conditions in Bacillus subtilis.
Mol Microbiol: 2007, 63(1);294-307
[PubMed:17163968] [WorldCat.org] [DOI] (P p)

Hideaki Nanamiya, Genki Akanuma, Yousuke Natori, Rikinori Murayama, Saori Kosono, Toshiaki Kudo, Kazuo Kobayashi, Naotake Ogasawara, Seung-Moon Park, Kozo Ochi, Fujio Kawamura
Zinc is a key factor in controlling alternation of two types of L31 protein in the Bacillus subtilis ribosome.
Mol Microbiol: 2004, 52(1);273-83
[PubMed:15049826] [WorldCat.org] [DOI] (P p)