Difference between revisions of "SinI"

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(Biological materials)
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** DS91 (spc) NCIB3610 derivate, available in [[Stülke]] lab
 
** DS91 (spc) NCIB3610 derivate, available in [[Stülke]] lab
 
** 1S98 ( ''sinI''::''kan''), {{PubMed|11466285}}, available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1S98&Search=1S98 BGSC]
 
** 1S98 ( ''sinI''::''kan''), {{PubMed|11466285}}, available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1S98&Search=1S98 BGSC]
 +
** GP1663 (''yghG-sinI-sinR-tasA''), available in [[Stülke]] lab
  
 
* '''Expression vector:'''
 
* '''Expression vector:'''

Revision as of 13:26, 1 November 2013

  • Description: antagonist of SinR, drives SlrR from the SlrR(LOW) to the SlrR(HIGH) state

Gene name sinI
Synonyms
Essential no
Product antagonist of SinR
Function control of biofilm formation
Gene expression levels in SubtiExpress: sinI
Interactions involving this protein in SubtInteract: SinI
Regulation of this protein in SubtiPathways:
Biofilm
MW, pI 6 kDa, 6.333
Gene length, protein length 171 bp, 57 aa
Immediate neighbours yqhG, sinR
Sequences Protein DNA DNA_with_flanks
Genetic context
SinI context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
SinI 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 gene

Basic information

  • Locus tag: BSU24600

Phenotypes of a mutant

  • altered cell death pattern in colonies PubMed

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family:
  • Paralogous protein(s): SlrA

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
    • activated under conditions that trigger sporulation by (Spo0A) interaction PubMed,PubMed
    • repressed during exponential growth (ScoC) PubMed
    • repressed during logrithmic growth (AbrB) PubMed
    • repressed during vegetative growth (SinR) PubMed
  • Additional information:
    • the mRNA is substantially stabilized upon depletion of RNase Y PubMed

Biological materials

  • Mutant:
    • GP959 (spc), available in Stülke lab
    • DS91 (spc) NCIB3610 derivate, available in Stülke lab
    • 1S98 ( sinI::kan), PubMed, available at BGSC
    • GP1663 (yghG-sinI-sinR-tasA), 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 (C-term): GP935 (kan), available in Stülke lab
  • Antibody:

Labs working on this gene/ protein

Your additional remarks

References

Reviews

Modelling of the SinI/SinR switch

Original publications

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)

Munehiro Asally, Mark Kittisopikul, Pau Rué, Yingjie Du, Zhenxing Hu, Tolga Çağatay, Andra B Robinson, Hongbing Lu, Jordi Garcia-Ojalvo, Gürol M Süel
Localized cell death focuses mechanical forces during 3D patterning in a biofilm.
Proc Natl Acad Sci U S A: 2012, 109(46);18891-6
[PubMed:23012477] [WorldCat.org] [DOI] (I p)

Martin Lehnik-Habrink, Marc Schaffer, Ulrike Mäder, Christine Diethmaier, Christina Herzberg, Jörg Stülke
RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y.
Mol Microbiol: 2011, 81(6);1459-73
[PubMed:21815947] [WorldCat.org] [DOI] (I p)

Yunrong Chai, Thomas Norman, Roberto Kolter, Richard Losick
Evidence that metabolism and chromosome copy number control mutually exclusive cell fates in Bacillus subtilis.
EMBO J: 2011, 30(7);1402-13
[PubMed:21326214] [WorldCat.org] [DOI] (I p)

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, 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)

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 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)