CspB

• Description: major cold-shock protein
  
  

Gene name	cspB
Synonyms
Essential	no
Product	major cold-shock protein
Function	RNA chaperone
MW, pI	7 kDa, 4.341
Gene length, protein length	201 bp, 67 aa
Immediate neighbours	yhcI, yhcJ
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU09100

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions: CshB-CspB PubMed

• Localization: cytoplasm (according to Swiss-Prot), cytoplasma, colocalizes with the ribosomes PubMed

Database entries

• Structure: 1CSQ, 1NMG (NMR)

• Swiss prot entry: P32081

• KEGG entry: [3]

• E.C. number:

Additional information

• subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

• Operon:

• Sigma factor:

• Regulation:

• 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:

• Antibody:

Labs working on this gene/protein

Mohamed Marahiel, Marburg University, Germany homepage

References

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)

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)

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 L Graumann, M A Marahiel
Cold shock proteins CspB and CspC are major stationary-phase-induced proteins in Bacillus subtilis.
Arch Microbiol: 1999, 171(2);135-8
[PubMed:9914312] [WorldCat.org] [DOI] (P p)

T Schindler, D Perl, P Graumann, V Sieber, M A Marahiel, F X Schmid
Surface-exposed phenylalanines in the RNP1/RNP2 motif stabilize the cold-shock protein CspB from Bacillus subtilis.
Proteins: 1998, 30(4);401-6
[PubMed:9533624] [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)

P Graumann, K Schröder, R Schmid, M A Marahiel
Cold shock stress-induced proteins in Bacillus subtilis.
J Bacteriol: 1996, 178(15);4611-9
[PubMed:8755892] [WorldCat.org] [DOI] (P p)

K Schröder, P Graumann, A Schnuchel, T A Holak, M A Marahiel
Mutational analysis of the putative nucleic acid-binding surface of the cold-shock domain, CspB, revealed an essential role of aromatic and basic residues in binding of single-stranded DNA containing the Y-box motif.
Mol Microbiol: 1995, 16(4);699-708
[PubMed:7476164] [WorldCat.org] [DOI] (P p)

G I Makhatadze, M A Marahiel
Effect of pH and phosphate ions on self-association properties of the major cold-shock protein from Bacillus subtilis.
Protein Sci: 1994, 3(11);2144-7
[PubMed:7703860] [WorldCat.org] [DOI] (P p)

P Graumann, M A Marahiel
The major cold shock protein of Bacillus subtilis CspB binds with high affinity to the ATTGG- and CCAAT sequences in single stranded oligonucleotides.
FEBS Lett: 1994, 338(2);157-60
[PubMed:8307174] [WorldCat.org] [DOI] (P p)

K Schröder, P Zuber, G Willimsky, B Wagner, M A Marahiel
Mapping of the Bacillus subtilis cspB gene and cloning of its homologs in thermophilic, mesophilic and psychrotrophic bacilli.
Gene: 1993, 136(1-2);277-80
[PubMed:8294017] [WorldCat.org] [DOI] (P p)

A Schnuchel, R Wiltscheck, M Czisch, M Herrler, G Willimsky, P Graumann, M A Marahiel, T A Holak
Structure in solution of the major cold-shock protein from Bacillus subtilis.
Nature: 1993, 364(6433);169-71
[PubMed:8321289] [WorldCat.org] [DOI] (P p)

H Schindelin, M A Marahiel, U Heinemann
Universal nucleic acid-binding domain revealed by crystal structure of the B. subtilis major cold-shock protein.
Nature: 1993, 364(6433);164-8
[PubMed:8321288] [WorldCat.org] [DOI] (P p)

G Willimsky, H Bang, G Fischer, M A Marahiel
Characterization of cspB, a Bacillus subtilis inducible cold shock gene affecting cell viability at low temperatures.
J Bacteriol: 1992, 174(20);6326-35
[PubMed:1400185] [WorldCat.org] [DOI] (P p)

H Schindelin, M Herrler, G Willimsky, M A Marahiel, U Heinemann
Overproduction, crystallization, and preliminary X-ray diffraction studies of the major cold shock protein from Bacillus subtilis, CspB.
Proteins: 1992, 14(1);120-4
[PubMed:1409560] [WorldCat.org] [DOI] (P p)