Difference between revisions of "RpmI"

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|colspan="2" | '''Genetic context''' <br/> [[Image:rpmI_context.gif]]
 
|colspan="2" | '''Genetic context''' <br/> [[Image:rpmI_context.gif]]
 
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|colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=rpmI_2952615_2952815_-1 Expression at a glance]'''&#160;&#160;&#160;{{PubMed|22383849}}<br/>[[Image:rpmI_expression.png|500px]]
 
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Revision as of 10:42, 20 April 2012

Gene name rpmI
Synonyms
Essential yes PubMed
Product ribosomal protein L35
Function translation
Interactions involving this protein in SubtInteract: RpmI
MW, pI 7 kDa, 12.525
Gene length, protein length 198 bp, 66 aa
Immediate neighbours rplT, infC
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
RpmI context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
RpmI expression.png
























Categories containing this gene/protein

translation, essential genes

This gene is a member of the following regulons

RplT regulon, stringent response

The gene

Basic information

  • Locus tag: BSU28860

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:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

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

Additional information

Expression and regulation

  • 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

Patrice Bruscella, Karen Shahbabian, Soumaya Laalami, Harald Putzer
RNase Y is responsible for uncoupling the expression of translation factor IF3 from that of the ribosomal proteins L35 and L20 in Bacillus subtilis.
Mol Microbiol: 2011, 81(6);1526-41
[PubMed:21843271] [WorldCat.org] [DOI] (I p)

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)

Nasslie Choonee, Sergine Even, Lena Zig, Harald Putzer
Ribosomal protein L20 controls expression of the Bacillus subtilis infC operon via a transcription attenuation mechanism.
Nucleic Acids Res: 2007, 35(5);1578-88
[PubMed:17289755] [WorldCat.org] [DOI] (I p)

Christine Eymann, Georg Homuth, Christian Scharf, Michael Hecker
Bacillus subtilis functional genomics: global characterization of the stringent response by proteome and transcriptome analysis.
J Bacteriol: 2002, 184(9);2500-20
[PubMed:11948165] [WorldCat.org] [DOI] (P p)