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

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)