SlrR

• Description: transcriptional activator of competence development and sporulation genes, represses SigD-dependent flagellar genes, antagonist of SlrA and SinR, has LexA-like autocleavage activity
  
  

Gene name	slrR
Synonyms	yveJ, slr
Essential	no
Product	transcription regulator, SlrA antagonist
Function	regulation of initiation of biofilm formation and of autolysis
Gene expression levels in SubtiExpress: slrR
Interactions involving this protein in SubtInteract: SlrR
Regulation of this protein in SubtiPathways: Biofilm
MW, pI	17 kDa, 9.63
Gene length, protein length	456 bp, 152 aa
Immediate neighbours	epsA, pnbA
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

transcription factors and their control, transition state regulators, biofilm formation

This gene is a member of the following regulons

Abh regulon, AbrB regulon, SinR regulon

The SlrR regulon:

• lytA-lytB-lytC, lytF

The gene

Basic information

• Locus tag: BSU34380

Phenotypes of a mutant

• • smooth colonies on MsGG medium, no biofilm formation PubMed

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

Additional information

• overexpression of slrR suppresses the phenotype of a ymdB mutant PubMed

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:
  • SlrR binds to and inhibits the activity of SlrA, SlrA indirectly stimulates the synthesis of SlrR by interacting with SinR. SlrR can bind to SinR and SinR directly represses the transcription of SlrR. SlrR indirectly derepresses its own gene. The heterocomplex of SlrR-SinR is a repressor of autolysin and motility genes and inhibits the repressor function of SinR. PubMed
  • repression of transcription of lytA-lytB-lytC and lytF PubMed
  • autocleavage PubMed

• Protein family:

• Paralogous protein(s): SinR

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:
  • subject to self-cleavage via a LexA-like autopeptidase, this involves ClpC PubMed

• Cofactor(s):

• Effectors of protein activity: interaction with SinR triggers binding of SlrR to the promoters of lytA-lytB-lytC and lytF, resulting in their repression PubMed

• Interactions:
  • SlrA-SlrR PubMed
  • SlrR-SinR PubMed, K(D) 47.5 nM PubMed, Veg may inhibit this interaction PubMed

• Localization:

Database entries

• Structure:

• UniProt: P71049

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon: slrR PubMed

• Expression browser: slrR PubMed

• Sigma factor:

• Regulation:

• Regulatory mechanism:
  • Abh: transcription activation PubMed
  • SinR: transcription repression PubMed
  • AbrB: transcription repression PubMed

• Additional information:
  • induction by sequestration of SinR by SinI, SlrA PubMed or by SlrR itself PubMed
  • the slrR gene is not expressed in a ymdB mutant PubMed
  • the amount of the mRNA is substantially decreased upon depletion of RNase Y (this is likely due to the increased stability of the sinR mRNA) PubMed

Biological materials

• Mutant:
  • GP955 (slrR-pnbA::cat), available in Jörg Stülke's lab

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab

• Antibody:

References

Reviews

Hera Vlamakis, Yunrong Chai, Pascale Beauregard, Richard Losick, Roberto Kolter
Sticking together: building a biofilm the Bacillus subtilis way.
Nat Rev Microbiol: 2013, 11(3);157-68
[PubMed:23353768] [WorldCat.org] [DOI] (I p)

Patrick Piggot
Epigenetic switching: bacteria hedge bets about staying or moving.
Curr Biol: 2010, 20(11);R480-2
[PubMed:20541494] [WorldCat.org] [DOI] (I p)

Original publications

Additional publications: PubMed

Joseph A Newman, Cecilia Rodrigues, Richard J Lewis
Molecular basis of the activity of SinR protein, the master regulator of biofilm formation in Bacillus subtilis.
J Biol Chem: 2013, 288(15);10766-78
[PubMed:23430750] [WorldCat.org] [DOI] (I p)

Ying Lei, Taku Oshima, Naotake Ogasawara, Shu Ishikawa
Functional analysis of the protein Veg, which stimulates biofilm formation in Bacillus subtilis.
J Bacteriol: 2013, 195(8);1697-705
[PubMed:23378512] [WorldCat.org] [DOI] (I p)

Diethmaier C, Pietack N, Gunka K, Wrede C, Lehnik-Habrink M, Herzberg C, Hübner S, Stülke J  
A Novel Factor Controlling Bistability in Bacillus subtilis: The YmdB Protein Affects
Flagellin Expression and Biofilm Formation. 
J Bacteriol.: 2011, 193(21):5997-6007. 
PubMed:21856853

Yunrong Chai, Roberto Kolter, Richard Losick
Reversal of an epigenetic switch governing cell chaining in Bacillus subtilis by protein instability.
Mol Microbiol: 2010, 78(1);218-29
[PubMed:20923420] [WorldCat.org] [DOI] (I p)

Yunrong Chai, Thomas Norman, Roberto Kolter, Richard Losick
An epigenetic switch governing daughter cell separation in Bacillus subtilis.
Genes Dev: 2010, 24(8);754-65
[PubMed:20351052] [WorldCat.org] [DOI] (I p)

Yunrong Chai, Roberto Kolter, Richard Losick
Paralogous antirepressors acting on the master regulator for biofilm formation in Bacillus subtilis.
Mol Microbiol: 2009, 74(4);876-87
[PubMed:19788541] [WorldCat.org] [DOI] (I p)

Ewan J Murray, Mark A Strauch, Nicola R Stanley-Wall
SigmaX is involved in controlling Bacillus subtilis biofilm architecture through the AbrB homologue Abh.
J Bacteriol: 2009, 191(22);6822-32
[PubMed:19767430] [WorldCat.org] [DOI] (I p)

Kazuo Kobayashi
SlrR/SlrA controls the initiation of biofilm formation in Bacillus subtilis.
Mol Microbiol: 2008, 69(6);1399-410
[PubMed:18647168] [WorldCat.org] [DOI] (I p)

Frances Chu, Daniel B Kearns, Anna McLoon, Yunrong Chai, Roberto Kolter, Richard Losick
A novel regulatory protein governing biofilm formation in Bacillus subtilis.
Mol Microbiol: 2008, 68(5);1117-27
[PubMed:18430133] [WorldCat.org] [DOI] (I p)