Difference between revisions of "CshA"

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=References=
 
=References=
'''Additional publications:''' {{PubMed|20709848,21710567}}
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<pubmed>16352840,20572937 , 12399512 16861794, 23175651,21803996 20709848,21710567</pubmed>
<pubmed>16352840,20572937 , 12399512 16861794, 23175651,21803996</pubmed>
 
 
==  CshA in other organisms ==
 
==  CshA in other organisms ==
 
<pubmed> 23229022  21764917</pubmed>
 
<pubmed> 23229022  21764917</pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 18:54, 17 November 2013

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
Sequences Protein DNA DNA_with_flanks
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: [3]
  • 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

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)

Olivier Delumeau, François Lecointe, Jan Muntel, Alain Guillot, Eric Guédon, Véronique Monnet, Michael Hecker, Dörte Becher, Patrice Polard, Philippe Noirot
The dynamic protein partnership of RNA polymerase in Bacillus subtilis.
Proteomics: 2011, 11(15);2992-3001
[PubMed:21710567] [WorldCat.org] [DOI] (I p)

Franck Pandiani, Julien Brillard, Isabelle Bornard, Caroline Michaud, Stéphanie Chamot, Christophe Nguyen-the, Véronique Broussolle
Differential involvement of the five RNA helicases in adaptation of Bacillus cereus ATCC 14579 to low growth temperatures.
Appl Environ Microbiol: 2010, 76(19);6692-7
[PubMed:20709848] [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)

CshA in other organisms

Stella Oun, Peter Redder, Jean-Philippe Didier, Patrice François, Anna-Rita Corvaglia, Elena Buttazzoni, Caroline Giraud, Myriam Girard, Jacques Schrenzel, Patrick Linder
The CshA DEAD-box RNA helicase is important for quorum sensing control in Staphylococcus aureus.
RNA Biol: 2013, 10(1);157-65
[PubMed:23229022] [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)