Difference between revisions of "CshA"

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(References)
(Extended information on the protein)
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* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
  
* '''Interactions:''' [[CshA]]-[[CspB]] [http://www.ncbi.nlm.nih.gov/sites/entrez/16352840 PubMed]
+
* '''Interactions:''' [[CshA]]-[[CshA]] {{PubMed|20572937}}, [[CshA]]-[[CspB]] [http://www.ncbi.nlm.nih.gov/sites/entrez/16352840 PubMed], [[CshA]]-[[PnpA]] {{PubMed|20572937}}, [[CshA]]-[[Rny]] {{PubMed|20572937}}, [[CshA]]-[[RnjA]] {{PubMed|20572937}}, [[CshA]]-[[Eno]] {{PubMed|20572937}}, [[CshA]]-[[PfkA]] {{PubMed|20572937}}
  
* '''Localization:''' cytoplasma, colocalizes with the ribosomes [http://www.ncbi.nlm.nih.gov/sites/entrez/16352840 PubMed]
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* '''Localization:''' cytoplasma, colocalizes with the ribosomes [http://www.ncbi.nlm.nih.gov/sites/entrez/16352840 PubMed], cell membrane {{PubMed|20572937}}
  
 
=== Database entries ===
 
=== Database entries ===

Revision as of 09:10, 25 June 2010

  • Description: DEAD-box RNA helicase, important for adaptation to low temperatures

Gene name cshA
Synonyms ydbR
Essential no
Product DEAD-box RNA helicase
Function RNA helicase
MW, pI 57 kDa, 9.89
Gene length, protein length 1533 bp, 511 aa
Immediate neighbours murF, ydbS
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YdbR context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU04580

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: RNA helicase
  • Protein family: helicase C-terminal domain (according to Swiss-Prot) DEAD-box RNA helicase

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization: cytoplasma, colocalizes with the ribosomes PubMed, cell membrane PubMed

Database entries

  • Structure:
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Operon:
  • Sigma factor:
  • Regulation:
    • induced by cold shock PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant: GP1035 (aphA3), available in Stülke lab
  • Expression vector:
    • for expression/ purification from B. subtilis with C-terminal Strep-tag, for SPINE, in pGP382: pGP1387, available in Stülke lab
    • for expression/ purification from B. subtilis with C-terminal Strep-tag, for SPINE, expression from the native chromomsomal site: GP1026, available in Stülke lab
    • for expression/ purification from E. coli with N-terminal His-tag, in pWH844: pGP1386, available in Stülke lab
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab
  • FLAG-tag construct: GP1010 (spc, based on pGP1331), available in the Stülke labs
  • Antibody:

Labs working on this gene/protein

Mohamed Marahiel, Marburg University, Germany homepage

Your additional remarks

References

Martin Lehnik-Habrink, Henrike Pförtner, Leonie Rempeters, Nico Pietack, Christina Herzberg, Jörg Stülke
The RNA degradosome in Bacillus subtilis: identification of CshA as the major RNA helicase in the multiprotein complex.
Mol Microbiol: 2010, 77(4);958-71
[PubMed:20572937] [WorldCat.org] [DOI] (I p)

Yoshinari Ando, Kouji Nakamura
Bacillus subtilis DEAD protein YdbR possesses ATPase, RNA binding, and RNA unwinding activities.
Biosci Biotechnol Biochem: 2006, 70(7);1606-15
[PubMed:16861794] [WorldCat.org] [DOI] (P p)

Karen Hunger, Carsten L Beckering, Frank Wiegeshoff, Peter L Graumann, Mohamed A Marahiel
Cold-induced putative DEAD box RNA helicases CshA and CshB are essential for cold adaptation and interact with cold shock protein B in Bacillus subtilis.
J Bacteriol: 2006, 188(1);240-8
[PubMed:16352840] [WorldCat.org] [DOI] (P p)

Carsten L Beckering, Leif Steil, Michael H W Weber, Uwe Völker, Mohamed A Marahiel
Genomewide transcriptional analysis of the cold shock response in Bacillus subtilis.
J Bacteriol: 2002, 184(22);6395-402
[PubMed:12399512] [WorldCat.org] [DOI] (P p)