CspB

• Description: major cold-shock protein
  
  

Gene name	cspB
Synonyms
Essential	no
Product	major cold-shock protein
Function	RNA chaperone
Gene expression levels in SubtiExpress: cspB
Interactions involving this protein in SubtInteract: CspB
MW, pI	7 kDa, 4.341
Gene length, protein length	201 bp, 67 aa
Immediate neighbours	yhcI, yhcJ
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

RNA chaperones, cold stress proteins

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): CspC, CspD

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)
  • 3PF4 (in complex with r(GUCUUUA)) PubMed

• UniProt: P32081

• KEGG entry: [3]

• E.C. number:

Additional information

• subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

• Operon: cspB PubMed

• Expression browser: cspB PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • induced upon 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

Mohamed Marahiel, Marburg University, Germany homepage

References

Letal I Salzberg, Leagh Powell, Karsten Hokamp, Eric Botella, David Noone, Kevin M Devine
The WalRK (YycFG) and σ(I) RsgI regulators cooperate to control CwlO and LytE expression in exponentially growing and stressed Bacillus subtilis cells.
Mol Microbiol: 2013, 87(1);180-95
[PubMed:23199363] [WorldCat.org] [DOI] (I p)

Rolf Sachs, Klaas E A Max, Udo Heinemann, Jochen Balbach
RNA single strands bind to a conserved surface of the major cold shock protein in crystals and solution.
RNA: 2012, 18(1);65-76
[PubMed:22128343] [WorldCat.org] [DOI] (I p)

Anja Buttstedt, Reno Winter, Mirko Sackewitz, Gerd Hause, Franz-Xaver Schmid, Elisabeth Schwarz
Influence of the stability of a fused protein and its distance to the amyloidogenic segment on fibril formation.
PLoS One: 2010, 5(11);e15436
[PubMed:21124848] [WorldCat.org] [DOI] (I e)

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)

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)

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, 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)

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 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)