CtsR

• 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
Interactions involving this protein in SubtInteract: CtsR
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 This image was kindly provided by SubtiList

Categories containing this gene/protein

proteolysis, transcription factors and their control, general stress proteins (controlled by SigB), heat shock proteins, phosphoproteins

This gene is a member of the following regulons

CtsR regulon, SigB regulon

The gene

Basic information

• Locus tag: BSU00830

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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

• Interactions:
  • McsA-McsB-CtsR
  • CtsR-ClpP/ClpC (degradation of CtsR) PubMed

• Localization:

Database entries

• Structure: 3H0D (complex with a 26bp DNA duplex, from Geobacillus stearothermophilus) PubMed

• UniProt: P37568

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: ctsR-mcsA-mcsB-clpC-radA-disA PubMed

• Expression browser: ctsR PubMed

• Sigma factor: SigA PubMed, SigB PubMed1 PubMed2

• Regulation:
  • induced by stress (SigB) PubMed
  • repressed at low temperatures (CtsR) PubMed

• Regulatory mechanism:
  • CtsR: transcription repression PubMed

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

Biological materials

• Mutant: ctsR::aphA3 availbale from the Gerth lab

ctsRG65P::spec available from the Gerth lab

• Expression vector: for expression, purification in E. coli with N-terminal His-tag, pRSETA available in Gerth lab

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody: available in Gerth lab

References

Reviews

Alexander K W Elsholz, Ulf Gerth, Michael Hecker
Regulation of CtsR activity in low GC, Gram+ bacteria.
Adv Microb Physiol: 2010, 57;119-44
[PubMed:21078442] [WorldCat.org] [DOI] (I p)

Wolfgang Schumann
The Bacillus subtilis heat shock stimulon.
Cell Stress Chaperones: 2003, 8(3);207-17
[PubMed:14984053] [WorldCat.org] [DOI] (P p)

Original publications

Additional publications: PubMed

Liang Tao, Partho Chattoraj, Indranil Biswas
CtsR regulation in mcsAB-deficient Gram-positive bacteria.
J Bacteriol: 2012, 194(6);1361-8
[PubMed:22247503] [WorldCat.org] [DOI] (I p)

Alexander K W Elsholz, Kristina Hempel, Dierk-Christoph Pöther, Dörte Becher, Michael Hecker, Ulf Gerth
CtsR inactivation during thiol-specific stress in low GC, Gram+ bacteria.
Mol Microbiol: 2011, 79(3);772-85
[PubMed:21208299] [WorldCat.org] [DOI] (I p)

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)