CshA

• 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
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 This image was kindly provided by SubtiList
[None Expression at a glance]   PubMed

Categories containing this gene/protein

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

The gene

Basic information

• Locus tag: BSU04580

Phenotypes of a mutant

• poor growth at low temperatures (16 to 20°C) PubMed
• reduced number of ribosomes PubMed
• no expression of the frlB-frlO-frlN-frlM-frlD operon PubMed
• strongly increased expression of the ysbA-ysbB operon PubMed
• transcription profile resulting from rny depletion: GEO PubMed

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

• GEO entry: [2] (cshA deletion vs. wild type) PubMed

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:
  • RNA helicase
  • required for ribosome assembly (biogenesis of the large subunit) PubMed

• Protein family: helicase C-terminal domain (according to Swiss-Prot) DEAD-box RNA helicase

• Paralogous protein(s): CshB, DeaD, YfmL

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:
  • CshA interacts with the RNA polymerase PubMed
  • part of the RNA degradosome PubMed
  • CshA-CshA PubMed
  • CshA-CspB PubMed
  • CshA-PnpA PubMed
  • CshA-Rny PubMed
  • CshA-RnjA PubMed
  • CshA-Eno PubMed
  • CshA-PfkA PubMed
  • DeaD-CshA PubMed
  • RnpA-CshA PubMed
  • RplA-CshA PubMed
  • RplC-CshA PubMed

• Localization: cytoplasma, colocalizes with the ribosomes PubMed, cell membrane PubMed

Database entries

• Structure:

• UniProt: P96614

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon:

• Expression browser: cshA PubMed

• 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 Jörg Stülke's lab
  • GP1083 (cat), available in Jörg Stülke's lab

• 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

• FLAG-tag construct:
  • GP1010 (spc, based on pGP1331), available in Jörg Stülke's lab
  • GP1074 (tet), available in Jörg Stülke's lab

• Antibody:

Labs working on this gene/protein

Mohamed Marahiel, Marburg University, Germany homepage

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)

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)