Difference between revisions of "CshA"

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===Phenotypes of a mutant ===
 
===Phenotypes of a mutant ===
 
* poor growth at low temperatures (16 to 20°C) {{PubMed|23175651}}
 
* poor growth at low temperatures (16 to 20°C) {{PubMed|23175651}}
* reduced number of ribosomes {{PubMed|23175651}}
+
* reduced number of [[ribosome]]s {{PubMed|23175651}}
  
 
=== Database entries ===
 
=== Database entries ===
Line 70: Line 70:
 
=== Basic information/ Evolution ===
 
=== Basic information/ Evolution ===
  
* '''Catalyzed reaction/ biological activity:''' RNA helicase
+
* '''Catalyzed reaction/ biological activity:'''  
 +
** RNA helicase
 +
** required for [[ribosome]] assembly (biogenesis of the large subunit) {{PubMed|23175651}}
  
 
* '''Protein family:''' helicase C-terminal domain (according to Swiss-Prot) [[DEAD-box RNA helicases|DEAD-box RNA helicase]]
 
* '''Protein family:''' helicase C-terminal domain (according to Swiss-Prot) [[DEAD-box RNA helicases|DEAD-box RNA helicase]]
Line 100: Line 102:
 
** [[DeaD]]-[[CshA]] {{PubMed|20572937}}
 
** [[DeaD]]-[[CshA]] {{PubMed|20572937}}
 
** [[RnpA]]-[[CshA]] {{PubMed|21764917}}
 
** [[RnpA]]-[[CshA]] {{PubMed|21764917}}
 +
** [[RplA]]-[[CshA]] {{PubMed|23175651}}
 +
** [[RplC]]-[[CshA]] {{PubMed|23175651}}
  
 
* '''[[Localization]]:''' cytoplasma, colocalizes with the ribosomes [http://www.ncbi.nlm.nih.gov/sites/entrez/16352840 PubMed], cell membrane {{PubMed|20572937}}
 
* '''[[Localization]]:''' cytoplasma, colocalizes with the ribosomes [http://www.ncbi.nlm.nih.gov/sites/entrez/16352840 PubMed], cell membrane {{PubMed|20572937}}

Revision as of 16:48, 26 November 2012

Gene name cshA
Synonyms ydbR
Essential no
Product DEAD-box RNA helicase
Function RNA helicase
Gene expression levels in SubtiExpress: cshA
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
[None Expression at a glance]   PubMed
CshA expression.png















Categories containing this gene/protein

DEAD-box RNA helicases, translation, 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
    • required for ribosome assembly (biogenesis of the large subunit) PubMed

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:
  • 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

  • Expression vector:
    • for expression/ purification from B. subtilis with C-terminal Strep-tag, for SPINE, in pGP382: pGP1387, available in Jörg Stülke's lab
    • for expression/ purification from B. subtilis with C-terminal Strep-tag, for SPINE, expression from the native chromomsomal site: GP1026 (aphA3), available in Jörg Stülke's lab
    • for expression/ purification from E. coli with N-terminal His-tag, in pWH844: pGP1386, available in Jörg Stülke's lab
  • lacZ fusion:
  • GFP fusion:
    • pGP1369 for chromosomal expression of CshA-YFP, available in Jörg Stülke's lab
    • B. subtilis GP1081 cshA-gfp spc, available in Jörg Stülke's lab,
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jörg Stülke's lab
  • Antibody:

Labs working on this gene/protein

Mohamed Marahiel, Marburg University, Germany homepage

Your additional remarks

References

Additional publications: PubMed

Martin Lehnik-Habrink, Leonie Rempeters, Ákos T Kovács, Christoph Wrede, Claudia Baierlein, Heike Krebber, Oscar P Kuipers, Jörg Stülke
DEAD-Box RNA helicases in Bacillus subtilis have multiple functions and act independently from each other.
J Bacteriol: 2013, 195(3);534-44
[PubMed:23175651] [WorldCat.org] [DOI] (I p)

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)