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
Gene expression levels in SubtiExpress: ctsR
Interactions involving this protein in SubtInteract: CtsR
Regulatory function and regulation of this protein in SubtiPathways: ctsR
Metabolic function and regulation of this protein in SubtiPathways: CtsR
MW, pI	17 kDa, 9.261
Gene length, protein length	462 bp, 154 aa
Immediate neighbours	rrnW-5S, mcsA
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

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

• BsubCyc: BSU00830

• 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
  • in addition, Arg-15 was reported to be a phosphorylation site 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

• BsubCyc: BSU00830

• 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

Additional reviews: PubMed

Original publications

Additional publications: PubMed

Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742] [WorldCat.org] [DOI] (I p)

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)