SinR

• Description: transcriptional regulator of post-exponential-phase responses genes
  
  

Gene name	sinR
Synonyms	sin, flaD
Essential	no
Product	transcriptional regulator of post-exponential-phase responses genes
Function	control of biofilm formation
Gene expression levels in SubtiExpress: sinR
Interactions involving this protein in SubtInteract: SinR
Metabolic function and regulation of this protein in SubtiPathways: Biofilm, Central C-metabolism, Protein secretion
MW, pI	12 kDa, 7.177
Gene length, protein length	333 bp, 111 aa
Immediate neighbours	sinI, tasA
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

AbrB regulon, ScoC regulon, Spo0A regulon

The gene

Basic information

• Locus tag: BSU24610

Phenotypes of a mutant

• the mutation suppresses the galactose toxicity to a galE mutant PubMed

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: transcription repressor of biofilm genes, acts as co-repressor for SlrR PubMed

• Protein family:

• Paralogous protein(s): SlrR

Extended information on the protein

• Kinetic information:

• Domains:
  • DNA-binding N-terminal domain (aa 1-69) PubMed
  • SinI-binding C-terminal domain (aa 74-111) PubMed

• Modification:

• Cofactor(s):

• Effectors of protein activity:
  • SinI and SlrA are antagonists to SinR PubMed
  • SlrR is also antagonist of SinR PubMed

• Interactions:
  • SlrA-SinR PubMed, K(D) 10.6 nM PubMed
  • SlrR-SinR PubMed, K(D) 47.5 nM PubMed, Veg may inhibit this interaction PubMed
  • SinR-SinI PubMed, K(D) 1.8 nM PubMed
  • SinR-ScoC

• Localization:

Database entries

• Structure:
  • 3QQ6 (N-terminal domain, aa 1-69) PubMed
  • 2YAL (C-terminal domain, aa 74-111) PubMed
  • 1B0N (complex SinR-SinI) PubMed

• UniProt: P06533

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon:
  • sinI-sinR PubMed
  • sinR PubMed

• Expression browser: sinR PubMed

• Sigma factor:
  • sinI: SigA PubMed
  • sinR: SigA PubMed

• Regulation:
  • sinI: repressed under conditions that trigger sporulation (Spo0A) PubMed
  • sinI: repressed during exponential growth (ScoC) PubMed
  • sinI: repressed during logrithmic growth (AbrB) PubMed
  • sinI: repressed during vegetative growth (SinR) PubMed

• Regulatory mechanism:
  • Spo0A: transcription repression PubMed
  • ScoC: transcription repression PubMed
  • AbrB: transcription repression PubMed
  • SinR: transcription repression PubMed

• Additional information:
  • the mRNA is substantially stabilized upon depletion of RNase Y (the half-life of the mRNA increases from 3.5 to 13 min) PubMed

Biological materials

• Mutant: TMB079 sinR::spec, GP736 (tetR), available in Stülke lab
  • 1S97 ( sinR::phleo), PubMed, available at BGSC

• Expression vector:
  • N-terminal Strep-tag, for SPINE, expression in B. subtilis, in pGP380: pGP1083 , available in Stülke lab

• lacZ fusion:

• GFP fusion:

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

• FLAG-tag construct: GP960 (spc, based on pGP1331), available in the Stülke lab

• Antibody:

References

Original publications

Additonal 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)

Yunrong Chai, Pascale B Beauregard, Hera Vlamakis, Richard Losick, Roberto Kolter
Galactose metabolism plays a crucial role in biofilm formation by Bacillus subtilis.
mBio: 2012, 3(4);e00184-12
[PubMed:22893383] [WorldCat.org] [DOI] (I e)

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

Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J  
RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y. 
Mol Microbiol. 2011 81(6): 1459-1473. 
PubMed:21815947