Difference between revisions of "CspB"

From SubtiWiki
Jump to: navigation, search
Line 15: Line 15:
 
|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU09100 cspB]
 
|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU09100 cspB]
 
|-
 
|-
|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/CspB CspB]
+
|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://subtiwiki.uni-goettingen.de/interact/ ''Subt''Interact]''': [http://subtiwiki.uni-goettingen.de/interact/index.php?protein=CspB CspB]
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 7 kDa, 4.341   
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 7 kDa, 4.341   

Revision as of 15:30, 11 November 2013

  • 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
CspB context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
CspB 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: BSU09100

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

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

Database entries

  • KEGG entry: [3]
  • E.C. number:

Additional information

  • subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

  • 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

Your additional remarks

References

Additional publications: PubMed

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)

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)