Difference between revisions of "SinI"
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| − | |colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=sinI_2552446_2552619_1 Expression at a glance]'''   {{PubMed|22383849}}<br/>[[Image:sinI_expression.png|500px]] | + | |colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=sinI_2552446_2552619_1 Expression at a glance]'''   {{PubMed|22383849}}<br/>[[Image:sinI_expression.png|500px|link=http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU24600]] | 
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Revision as of 13:54, 16 May 2013
| 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    This image was kindly provided by SubtiList | |
| Expression at a glance   PubMed   | |
Contents
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
- UniProt: P23308
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- Regulatory mechanism:
Biological materials
- Mutant:
- 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
Jennifer S Hallinan, Goksel Misirli, Anil Wipat  
Evolutionary computation for the design of a stochastic switch for synthetic genetic circuits. 
Annu Int Conf IEEE Eng Med Biol Soc: 2010, 2010;768-74 
[PubMed:21095906]
  [WorldCat.org]
 [DOI]
 (P p)
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)

