SinI

• Description: antagonist of SinR
  
  

Gene name	sinI
Synonyms
Essential	no
Product	antagonist of SinR
Function	control of SinR activity
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
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU24600

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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:

• Interactions: SinR-SinI

• Localization:

Database entries

• Structure:

• UniProt: P23308

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: sinI-sinR PubMed

• Sigma factor: SigA PubMed

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

• Regulatory mechanism:
  • Spo0A: transcription activation, in a portion of cells PubMed
  • ScoC: transcription repression PubMed
  • AbrB: transcription repression PubMed

• Additional information:

Biological materials

• Mutant:
  • GP959 (spc), available in Stülke lab
  • DS91 (spc) NCIB3610 derivate, 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

• Antibody:

References

Original publications

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)

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)