Difference between revisions of "SinR"

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* '''[[SubtInteract|Interactions]]:'''
 
* '''[[SubtInteract|Interactions]]:'''
** [[SlrA]]-[[SinR]] {{PubMed|19788541}}
+
** [[SlrA]]-[[SinR]] {{PubMed|19788541}}, K(D) 10.6 nM  {{PubMed|23430750}}
** [[SlrR]]-[[SinR]] {{PubMed|20351052}}, [[Veg]] may inhibit this interaction {{PubMed|23378512}}
+
** [[SlrR]]-[[SinR]] {{PubMed|20351052}}, K(D) 47.5 nM  {{PubMed|23430750}}, [[Veg]] may inhibit this interaction {{PubMed|23378512}}
 
+
** [[SinR]]-[[SinI]] {{PubMed|9799632}}, K(D) 1.8 nM  {{PubMed|23430750}}
 
** [[SinR]]-[[ScoC]]
 
** [[SinR]]-[[ScoC]]
** [[SinR]]-[[SinI]] {{PubMed|9799632}}
 
  
 
* '''[[Localization]]:'''
 
* '''[[Localization]]:'''
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==Original publications==
 
==Original publications==
 
'''Additonal publications:''' {{PubMed|22329926,21326214,21708175}}
 
'''Additonal publications:''' {{PubMed|22329926,21326214,21708175}}
<pubmed> 22893383 23378512</pubmed>
+
<pubmed> 22893383 23378512 23430750</pubmed>
 
  <big>''Diethmaier C, Pietack N, Gunka K, Wrede C, Lehnik-Habrink M, Herzberg C, Hübner S, Stülke J''  </big>
 
  <big>''Diethmaier C, Pietack N, Gunka K, Wrede C, Lehnik-Habrink M, Herzberg C, Hübner S, Stülke J''  </big>
 
  <big>'''A Novel Factor Controlling Bistability in ''Bacillus subtilis'': The YmdB Protein Affects</big>
 
  <big>'''A Novel Factor Controlling Bistability in ''Bacillus subtilis'': The YmdB Protein Affects</big>

Revision as of 16:04, 24 February 2013

  • 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
SinR context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
SinR expression.png















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 SinR 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]

Additional information

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):

Database entries

  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • 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
  • 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:

Labs working on this gene/protein

Your additional remarks

References

Reviews

Modelling of the SinI/SinR switch

Original publications

Additonal publications: PubMed

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