CshA

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Gene name cshA
Synonyms ydbR
Essential no
Product DEAD-box RNA helicase
Function RNA helicase
Interactions involving this protein in SubtInteract: CshA
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



Categories containing this gene/protein

DEAD-box RNA helicases, cold stress proteins, membrane proteins

This gene is a member of the following regulons

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

Extended information on the protein

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

Database entries

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

Additional information

Expression and regulation

  • Operon:
  • Sigma factor:
  • Regulation:
    • induced by cold shock PubMed
    • constitutive, similar expression at high and low temperatures, throughout growth and in both minimal and complex medium PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant: GP1035 (aphA3), available in Stülke lab
    • GP1083 (cat), 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: pGP1369 for chromosomal expression of CshA-YFP, available in Stülke lab
    • B. subtilis GP1081 cshA-gfp spc, available in Stülke lab,
  • 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

Additional publications: PubMed

Martin Lehnik-Habrink, Joseph Newman, Fabian M Rothe, Alexandra S Solovyova, Cecilia Rodrigues, Christina Herzberg, Fabian M Commichau, Richard J Lewis, Jörg Stülke
RNase Y in Bacillus subtilis: a Natively disordered protein that is the functional equivalent of RNase E from Escherichia coli.
J Bacteriol: 2011, 193(19);5431-41
[PubMed:21803996] [WorldCat.org] [DOI] (I p)

Christelle M Roux, Jonathon P DeMuth, Paul M Dunman
Characterization of components of the Staphylococcus aureus mRNA degradosome holoenzyme-like complex.
J Bacteriol: 2011, 193(19);5520-6
[PubMed:21764917] [WorldCat.org] [DOI] (I p)

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)