Difference between revisions of "SinR"

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* '''Kinetic information:'''
 
* '''Kinetic information:'''
  
−
* '''Domains:'''  
+
* '''Domains:'''
 +
** DNA-binding N-terminal domain (aa 1-69) {{PubMed|21708175}}
 +
** [[SinI]]-binding C-terminal domain (aa 74-111) {{PubMed|21708175}}
  
 
* '''Modification:'''
 
* '''Modification:'''
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* '''Cofactor(s):'''
 
* '''Cofactor(s):'''
  
−
* '''Effectors of protein activity:''' [[SinI]] and [[SlrA]] are antagonists to [[SinR]]  {{PubMed|19788541}}, [[SlrR]] is also antagonist of [[SinR]] {{PubMed|20351052}}
+
* '''Effectors of protein activity:'''
 +
** [[SinI]] and [[SlrA]] are antagonists to [[SinR]]  {{PubMed|19788541}}
 +
** [[SlrR]] is also antagonist of [[SinR]] {{PubMed|20351052}}
  
−
* '''Interactions:''' [[SlrA]]-[[SinR]] {{PubMed|19788541}}, [[SlrR]]-[[SinR]] {{PubMed|20351052}}, [[SinR]]-[[ScoC]],  [[SinR]]-[[SinI]]
+
* '''Interactions:'''  
 +
** [[SlrA]]-[[SinR]] {{PubMed|19788541}}
 +
** [[SlrR]]-[[SinR]] {{PubMed|20351052}}
 +
** [[SinR]]-[[ScoC]]
 +
** [[SinR]]-[[SinI]] {{PubMed|9799632}}
  
 
* '''Localization:'''
 
* '''Localization:'''
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=== Database entries ===
 
=== Database entries ===
  
−
* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=1B0N 1B0N] (complex [[SinR]]-[[SinI]])
+
* '''Structure:'''  
 +
** [http://www.rcsb.org/pdb/explore.do?structureId=3QQ6 3QQ6] (N-terminal domain, aa 1-69) {{PubMed|21708175}}
 +
** [http://www.rcsb.org/pdb/explore.do?structureId=2YAL 2YAL] (C-terminal domain, aa 74-111) {{PubMed|21708175}}
 +
** [http://www.rcsb.org/pdb/explore.do?structureId=1B0N 1B0N] (complex [[SinR]]-[[SinI]]) {{PubMed|9799632}}
  
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P06533 P06533]
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P06533 P06533]

Revision as of 20:23, 29 June 2011

  • 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
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





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

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):
  • Localization:

Database entries

  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Additional information:

Biological materials

  • Mutant: TMB079 sinR::spec, GP736 (tetR), available in Stülke lab
  • Expression vector:
  • 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

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)

Prashant Kodgire, K Krishnamurthy Rao
A dual mode of regulation of flgM by ScoC in Bacillus subtilis.
Can J Microbiol: 2009, 55(8);983-9
[PubMed:19898538] [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)

Yunrong Chai, Roberto Kolter, Richard Losick
A widely conserved gene cluster required for lactate utilization in Bacillus subtilis and its involvement in biofilm formation.
J Bacteriol: 2009, 191(8);2423-30
[PubMed:19201793] [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)

Yunrong Chai, Frances Chu, Roberto Kolter, Richard Losick
Bistability and biofilm formation in Bacillus subtilis.
Mol Microbiol: 2008, 67(2);254-63
[PubMed:18047568] [WorldCat.org] [DOI] (P p)

Prashant Kodgire, Madhulika Dixit, K Krishnamurthy Rao
ScoC and SinR negatively regulate epr by corepression in Bacillus subtilis.
J Bacteriol: 2006, 188(17);6425-8
[PubMed:16923912] [WorldCat.org] [DOI] (P p)

Steven S Branda, Frances Chu, Daniel B Kearns, Richard Losick, Roberto Kolter
A major protein component of the Bacillus subtilis biofilm matrix.
Mol Microbiol: 2006, 59(4);1229-38
[PubMed:16430696] [WorldCat.org] [DOI] (P p)

Frances Chu, Daniel B Kearns, Steven S Branda, Roberto Kolter, Richard Losick
Targets of the master regulator of biofilm formation in Bacillus subtilis.
Mol Microbiol: 2006, 59(4);1216-28
[PubMed:16430695] [WorldCat.org] [DOI] (P p)

Daniel B Kearns, Frances Chu, Steven S Branda, Roberto Kolter, Richard Losick
A master regulator for biofilm formation by Bacillus subtilis.
Mol Microbiol: 2005, 55(3);739-49
[PubMed:15661000] [WorldCat.org] [DOI] (P p)

Alejandro Sánchez, Jorge Olmos
Bacillus subtilis transcriptional regulators interaction.
Biotechnol Lett: 2004, 26(5);403-7
[PubMed:15104138] [WorldCat.org] [DOI] (P p)

Sasha H Shafikhani, Ines Mandic-Mulec, Mark A Strauch, Issar Smith, Terrance Leighton
Postexponential regulation of sin operon expression in Bacillus subtilis.
J Bacteriol: 2002, 184(2);564-71
[PubMed:11751836] [WorldCat.org] [DOI] (P p)

D J Scott, S Leejeerajumnean, J A Brannigan, R J Lewis, A J Wilkinson, J G Hoggett
Quaternary re-arrangement analysed by spectral enhancement: the interaction of a sporulation repressor with its antagonist.
J Mol Biol: 1999, 293(5);997-1004
[PubMed:10547280] [WorldCat.org] [DOI] (P p)

R J Lewis, J A Brannigan, W A Offen, I Smith, A J Wilkinson
An evolutionary link between sporulation and prophage induction in the structure of a repressor:anti-repressor complex.
J Mol Biol: 1998, 283(5);907-12
[PubMed:9799632] [WorldCat.org] [DOI] (P p)

M A Cervin, R J Lewis, J A Brannigan, G B Spiegelman
The Bacillus subtilis regulator SinR inhibits spoIIG promoter transcription in vitro without displacing RNA polymerase.
Nucleic Acids Res: 1998, 26(16);3806-12
[PubMed:9685500] [WorldCat.org] [DOI] (P p)

K Fredrick, J D Helmann
FlgM is a primary regulator of sigmaD activity, and its absence restores motility to a sinR mutant.
J Bacteriol: 1996, 178(23);7010-3
[PubMed:8955328] [WorldCat.org] [DOI] (P p)

M H Rashid, J Sekiguchi
flaD (sinR) mutations affect SigD-dependent functions at multiple points in Bacillus subtilis.
J Bacteriol: 1996, 178(22);6640-3
[PubMed:8932324] [WorldCat.org] [DOI] (P p)

J Hahn, A Luttinger, D Dubnau
Regulatory inputs for the synthesis of ComK, the competence transcription factor of Bacillus subtilis.
Mol Microbiol: 1996, 21(4);763-75
[PubMed:8878039] [WorldCat.org] [DOI] (P p)

P Margot, V Lazarevic, D Karamata
Effect of the SinR protein on the expression of the Bacillus subtilis 168 lytABC operon.
Microb Drug Resist: 1996, 2(1);119-21
[PubMed:9158733] [WorldCat.org] [DOI] (P p)

M A Strauch
In vitro binding affinity of the Bacillus subtilis AbrB protein to six different DNA target regions.
J Bacteriol: 1995, 177(15);4532-6
[PubMed:7635837] [WorldCat.org] [DOI] (P p)

U Bai, I Mandic-Mulec, I Smith
SinI modulates the activity of SinR, a developmental switch protein of Bacillus subtilis, by protein-protein interaction.
Genes Dev: 1993, 7(1);139-48
[PubMed:8422983] [WorldCat.org] [DOI] (P p)

P T Kallio, J E Fagelson, J A Hoch, M A Strauch
The transition state regulator Hpr of Bacillus subtilis is a DNA-binding protein.
J Biol Chem: 1991, 266(20);13411-7
[PubMed:1906467] [WorldCat.org] (P p)

N K Gaur, K Cabane, I Smith
Structure and expression of the Bacillus subtilis sin operon.
J Bacteriol: 1988, 170(3);1046-53
[PubMed:3125149] [WorldCat.org] [DOI] (P p)

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