Difference between revisions of "CtsR"

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* '''Domains:'''  
 
* '''Domains:'''  
  
−
* '''Modification:''' phosphorylation of a tyrosine residue by [[McsB]] [http://www.ncbi.nlm.nih.gov/sites/entrez/14984053 PubMed], recently, it was reported thatCtsR is phosphorylatedby [[McsB]] on Arg-62 rather than on a tyrosine residue [http://www.ncbi.nlm.nih.gov/sites/entrez/19498169 PubMed]
+
* '''Modification:'''  
 +
** phosphorylation of a tyrosine residue by [[McsB]] [http://www.ncbi.nlm.nih.gov/sites/entrez/14984053 PubMed]
 +
** recently, it was reported that CtsR is phosphorylated by [[McsB]] on Arg-62 rather than on a tyrosine residue [http://www.ncbi.nlm.nih.gov/sites/entrez/19498169 PubMed]
  
 
* '''Cofactor(s):'''
 
* '''Cofactor(s):'''
  
−
* '''Effectors of protein activity:''' probably activated by dephosphorylation by [[McsA]] and inactivated by phosphorylation by [[McsB]] [http://www.ncbi.nlm.nih.gov/sites/entrez/14984053 PubMed1] [http://www.ncbi.nlm.nih.gov/sites/entrez/19498169 PubMed2], regulated proteolysis by [[ClpP]]/[[ClpC]] [http://www.ncbi.nlm.nih.gov/pubmed/11179229 PubMed], [http://www.ncbi.nlm.nih.gov/pubmed/16163393 PubMed], [http://www.ncbi.nlm.nih.gov/pubmed/17380125 PubMed]
+
* '''Effectors of protein activity:'''  
 +
** CtsR is inactivated by heat, heat sensing requires Gly-64 {{PubMed|20852588}}
 +
** non-phosphorylated [[McsB]] targets CtsR for degradation {{PubMed|20852588}}
 +
** regulated proteolysis by [[ClpP]]/[[ClpC]] {{PubMed|11179229,16163393,17380125}} 
  
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* '''Interactions:''' [[McsA]]-[[McsB]]-[[CtsR]]  
+
* '''Interactions:''' [[McsA]]-[[McsB]]-[[CtsR]]
 +
** [[CtsR]]-[[ClpP]]/[[ClpC]] (degradation of [[CtsR]]) {{PubMed|11179229,16163393,17380125}}
  
 
* '''Localization:'''
 
* '''Localization:'''

Revision as of 08:56, 26 October 2010

  • Description: transcription repressor of class III heat shock genes (clpC operon, clpE, clpP)

Gene name ctsR
Synonyms yacG
Essential no
Product transcription repressor
Function regulation of protein degradation
Regulatory function and regulation of this protein in SubtiPathways:
Stress, Phosphorelay
MW, pI 17 kDa, 9.261
Gene length, protein length 462 bp, 154 aa
Immediate neighbours rrnW-5S, mcsA
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
CtsR context.gif
This image was kindly provided by SubtiList







The gene

Basic information

  • Locus tag: BSU00830

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: ctsR family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
    • phosphorylation of a tyrosine residue by McsB PubMed
    • recently, it was reported that CtsR is phosphorylated by McsB on Arg-62 rather than on a tyrosine residue PubMed
  • Cofactor(s):
  • Effectors of protein activity:
    • CtsR is inactivated by heat, heat sensing requires Gly-64 PubMed
    • non-phosphorylated McsB targets CtsR for degradation PubMed
    • regulated proteolysis by ClpP/ClpC PubMed
  • Localization:

Database entries

  • Structure: 3H0D (complex with a 26bp DNA duplex, from Geobacillus stearothermophilus) PubMed
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulatory mechanism:
  • Additional information: the mRNA is very stable (half-life > 15 min) PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews

Original publications

Alexander K W Elsholz, Stephan Michalik, Daniela Zühlke, Michael Hecker, Ulf Gerth
CtsR, the Gram-positive master regulator of protein quality control, feels the heat.
EMBO J: 2010, 29(21);3621-9
[PubMed:20852588] [WorldCat.org] [DOI] (I p)

Marcus Miethke, Michael Hecker, Ulf Gerth
Involvement of Bacillus subtilis ClpE in CtsR degradation and protein quality control.
J Bacteriol: 2006, 188(13);4610-9
[PubMed:16788169] [WorldCat.org] [DOI] (P p)

Pekka Varmanen, Finn K Vogensen, Karin Hammer, Airi Palva, Hanne Ingmer
ClpE from Lactococcus lactis promotes repression of CtsR-dependent gene expression.
J Bacteriol: 2003, 185(17);5117-24
[PubMed:12923084] [WorldCat.org] [DOI] (P p)

G Hambraeus, C von Wachenfeldt, L Hederstedt
Genome-wide survey of mRNA half-lives in Bacillus subtilis identifies extremely stable mRNAs.
Mol Genet Genomics: 2003, 269(5);706-14
[PubMed:12884008] [WorldCat.org] [DOI] (P p)

J D Helmann, M F Wu, P A Kobel, F J Gamo, M Wilson, M M Morshedi, M Navre, C Paddon
Global transcriptional response of Bacillus subtilis to heat shock.
J Bacteriol: 2001, 183(24);7318-28
[PubMed:11717291] [WorldCat.org] [DOI] (P p)

A Petersohn, M Brigulla, S Haas, J D Hoheisel, U Völker, M Hecker
Global analysis of the general stress response of Bacillus subtilis.
J Bacteriol: 2001, 183(19);5617-31
[PubMed:11544224] [WorldCat.org] [DOI] (P p)

E Krüger, D Zühlke, E Witt, H Ludwig, M Hecker
Clp-mediated proteolysis in Gram-positive bacteria is autoregulated by the stability of a repressor.
EMBO J: 2001, 20(4);852-63
[PubMed:11179229] [WorldCat.org] [DOI] (P p)

I Derré, G Rapoport, T Msadek
The CtsR regulator of stress response is active as a dimer and specifically degraded in vivo at 37 degrees C.
Mol Microbiol: 2000, 38(2);335-47
[PubMed:11069659] [WorldCat.org] [DOI] (P p)

I Derré, G Rapoport, T Msadek
CtsR, a novel regulator of stress and heat shock response, controls clp and molecular chaperone gene expression in gram-positive bacteria.
Mol Microbiol: 1999, 31(1);117-31
[PubMed:9987115] [WorldCat.org] [DOI] (P p)

E Krüger, M Hecker
The first gene of the Bacillus subtilis clpC operon, ctsR, encodes a negative regulator of its own operon and other class III heat shock genes.
J Bacteriol: 1998, 180(24);6681-8
[PubMed:9852015] [WorldCat.org] [DOI] (P p)

E Krüger, T Msadek, M Hecker
Alternate promoters direct stress-induced transcription of the Bacillus subtilis clpC operon.
Mol Microbiol: 1996, 20(4);713-23
[PubMed:8793870] [WorldCat.org] [DOI] (P p)

E Krüger, U Völker, M Hecker
Stress induction of clpC in Bacillus subtilis and its involvement in stress tolerance.
J Bacteriol: 1994, 176(11);3360-7
[PubMed:8195092] [WorldCat.org] [DOI] (P p)

Additional publications: PubMed

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