SinR

• Description: transcriptional regulator (Xre family) of post-exponential-phase responses genes
  
  

Gene name	sinR
Synonyms	sin, flaD
Essential	no
Product	transcriptional regulator (Xre family) 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: sinR
MW, pI	12 kDa, 7.177
Gene length, protein length	333 bp, 111 aa
Immediate neighbours	sinI, tasA
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

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

• BsubCyc: BSU24610

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:
  • transcription regulator of biofilm genes, acts as a true repressor of the tapA-sipW-tasA operon and as an anti-activator (prevents binding of the activator protein RemA) of the epsA-epsB-epsC-epsD-epsE-epsF-epsG-epsH-epsI-epsJ-epsK-epsL-epsM-epsN-epsO operon PubMed
  • acts as co-repressor for SlrR PubMed

• Protein family:Xre 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

• BsubCyc: BSU24610

• 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
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 699 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 425 PubMed

Biological materials

• Mutant:
  • GP923 (sinR::spec) PubMed, available in Jörg Stülke's lab
  • GP736 (sinR::tetR) PubMed, available in Jörg Stülke's lab
  • 1S97 (sinR::phleo), PubMed, available at BGSC
  • GP1672 (sinR-tasA::cat) PubMed, available in Jörg Stülke's lab
  • GP1663 (yghG-sinI-sinR-tasA), available in Jörg Stülke's lab

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

• lacZ fusion:

• GFP fusion:

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

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

• Antibody:

PubMed,

References

Reviews

Lynne S Cairns, Laura Hobley, Nicola R Stanley-Wall
Biofilm formation by Bacillus subtilis: new insights into regulatory strategies and assembly mechanisms.
Mol Microbiol: 2014, 93(4);587-98
[PubMed:24988880] [WorldCat.org] [DOI] (I p)

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)

David Dubnau
Swim or chill: lifestyles of a bacillus.
Genes Dev: 2010, 24(8);735-7
[PubMed:20395361] [WorldCat.org] [DOI] (I p)