Difference between revisions of "CspD"

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Revision as of 11:46, 19 April 2012

  • Description: cold shock protein

Gene name cspD
Synonyms
Essential no
Product cold shock protein
Function RNA chaperone
MW, pI 7 kDa, 4.31
Gene length, protein length 198 bp, 66 aa
Immediate neighbours ugtP, degR
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
CspD context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
CspD expression.png
























Categories containing this gene/protein

RNA chaperones, cold stress proteins

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU21930

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family:

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

  • subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

  • Operon:
  • Sigma factor:
  • Regulation:
    • weakly induced by cold shock PubMed
  • Regulatory mechanism:
  • Additional information: subject to Clp-dependent proteolysis upon glucose starvation PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews

Michael H Weber, Mohamed A Marahiel
Bacterial cold shock responses.
Sci Prog: 2003, 86(Pt 1-2);9-75
[PubMed:12838604] [WorldCat.org] [DOI] (P p)

Michael H W Weber, Mohamed A Marahiel
Coping with the cold: the cold shock response in the Gram-positive soil bacterium Bacillus subtilis.
Philos Trans R Soc Lond B Biol Sci: 2002, 357(1423);895-907
[PubMed:12171653] [WorldCat.org] [DOI] (P p)

Original publications

Ulf Gerth, Holger Kock, Ilja Kusters, Stephan Michalik, Robert L Switzer, Michael Hecker
Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis.
J Bacteriol: 2008, 190(1);321-31
[PubMed:17981983] [WorldCat.org] [DOI] (I p)

Tanja Kaan, Georg Homuth, Ulrike Mäder, Julia Bandow, Thomas Schweder
Genome-wide transcriptional profiling of the Bacillus subtilis cold-shock response.
Microbiology (Reading): 2002, 148(Pt 11);3441-3455
[PubMed:12427936] [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)

Michael H W Weber, Ingo Fricke, Niclas Doll, Mohamed A Marahiel
CSDBase: an interactive database for cold shock domain-containing proteins and the bacterial cold shock response.
Nucleic Acids Res: 2002, 30(1);375-8
[PubMed:11752341] [WorldCat.org] [DOI] (I p)

M H Weber, C L Beckering, M A Marahiel
Complementation of cold shock proteins by translation initiation factor IF1 in vivo.
J Bacteriol: 2001, 183(24);7381-6
[PubMed:11717297] [WorldCat.org] [DOI] (P p)

M H Weber, A V Volkov, I Fricke, M A Marahiel, P L Graumann
Localization of cold shock proteins to cytosolic spaces surrounding nucleoids in Bacillus subtilis depends on active transcription.
J Bacteriol: 2001, 183(21);6435-43
[PubMed:11591689] [WorldCat.org] [DOI] (P p)

T Schindler, P L Graumann, D Perl, S Ma, F X Schmid, M A Marahiel
The family of cold shock proteins of Bacillus subtilis. Stability and dynamics in vitro and in vivo.
J Biol Chem: 1999, 274(6);3407-13
[PubMed:9920884] [WorldCat.org] [DOI] (P p)

P Graumann, T M Wendrich, M H Weber, K Schröder, M A Marahiel
A family of cold shock proteins in Bacillus subtilis is essential for cellular growth and for efficient protein synthesis at optimal and low temperatures.
Mol Microbiol: 1997, 25(4);741-56
[PubMed:9379903] [WorldCat.org] [DOI] (P p)