Difference between revisions of "MinC"

From SubtiWiki
Jump to: navigation, search
Line 107: Line 107:
 
* '''[[Sigma factor]]:'''  
 
* '''[[Sigma factor]]:'''  
 
** ''[[radC]]'': [[SigM]] {{PubMed|18179421}}
 
** ''[[radC]]'': [[SigM]] {{PubMed|18179421}}
** ''[[mreB]]'': [[SigH]] [http://www.ncbi.nlm.nih.gov/sites/entrez/8459776 PubMed]
 
 
** ''[[minC]]'': [[SigH]] {{PubMed|8459776}}
 
** ''[[minC]]'': [[SigH]] {{PubMed|8459776}}
  
Line 139: Line 138:
 
<pubmed> 19680248 19884039 </pubmed>
 
<pubmed> 19680248 19884039 </pubmed>
 
==Original Publications==
 
==Original Publications==
<pubmed>8459776,19019154,1400224,10411726,15317782, 20352045,18588879, 19141479 20566861 20711458 </pubmed>
+
<pubmed>8459776,19019154,1400224,10411726,15317782, 20352045,18588879, 19141479 20566861 20711458 18179421</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 16:10, 17 May 2011

  • Description: cell-division inhibitor (septum placement), destabilizes FtsZ-rings at new cell poles

Gene name minC
Synonyms
Essential no
Product cell-division inhibitor
Function septum placement
MW, pI 24 kDa, 6.262
Gene length, protein length 678 bp, 226 aa
Immediate neighbours minD, mreD
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
MinC context.gif
This image was kindly provided by SubtiList



Categories containing this gene/protein

cell division, cell envelope stress proteins (controlled by SigM, W, X, Y), membrane proteins

This gene is a member of the following regulons

SigH regulon, SigM regulon

The gene

Basic information

  • Locus tag: BSU28000

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: The Min system prevents minicell formation adjacent to recently completed division sites by promoting the disassembly of the cytokinetic ring, thereby ensuring that cell division occurs only once per cell cycle PubMed
  • Protein family: minC family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization:
    • polar/ septal at the cell membrane PubMed
    • membrane binding/ polar localization depends on the proton motive force PubMed

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews

Marc Bramkamp, Suey van Baarle
Division site selection in rod-shaped bacteria.
Curr Opin Microbiol: 2009, 12(6);683-8
[PubMed:19884039] [WorldCat.org] [DOI] (I p)

David W Adams, Jeff Errington
Bacterial cell division: assembly, maintenance and disassembly of the Z ring.
Nat Rev Microbiol: 2009, 7(9);642-53
[PubMed:19680248] [WorldCat.org] [DOI] (I p)

Original Publications

Inês Filipa Fernandes de Oliveira, Anabela de Sousa Borges, Viola Kooij, Jeremy Bartosiak-Jentys, Joen Luirink, Dirk-Jan Scheffers
Characterization of ftsZ mutations that render Bacillus subtilis resistant to MinC.
PLoS One: 2010, 5(8);e12048
[PubMed:20711458] [WorldCat.org] [DOI] (I e)

Henrik Strahl, Leendert W Hamoen
Membrane potential is important for bacterial cell division.
Proc Natl Acad Sci U S A: 2010, 107(27);12281-6
[PubMed:20566861] [WorldCat.org] [DOI] (I p)

Suey van Baarle, Marc Bramkamp
The MinCDJ system in Bacillus subtilis prevents minicell formation by promoting divisome disassembly.
PLoS One: 2010, 5(3);e9850
[PubMed:20352045] [WorldCat.org] [DOI] (I e)

James A Gregory, Eric C Becker, Kit Pogliano
Bacillus subtilis MinC destabilizes FtsZ-rings at new cell poles and contributes to the timing of cell division.
Genes Dev: 2008, 22(24);3475-88
[PubMed:19141479] [WorldCat.org] [DOI] (P p)

Marc Bramkamp, Robyn Emmins, Louise Weston, Catriona Donovan, Richard A Daniel, Jeff Errington
A novel component of the division-site selection system of Bacillus subtilis and a new mode of action for the division inhibitor MinCD.
Mol Microbiol: 2008, 70(6);1556-69
[PubMed:19019154] [WorldCat.org] [DOI] (I p)

Dirk-Jan Scheffers
The effect of MinC on FtsZ polymerization is pH dependent and can be counteracted by ZapA.
FEBS Lett: 2008, 582(17);2601-8
[PubMed:18588879] [WorldCat.org] [DOI] (P p)

Warawan Eiamphungporn, John D Helmann
The Bacillus subtilis sigma(M) regulon and its contribution to cell envelope stress responses.
Mol Microbiol: 2008, 67(4);830-48
[PubMed:18179421] [WorldCat.org] [DOI] (P p)

David E Anderson, Frederico J Gueiros-Filho, Harold P Erickson
Assembly dynamics of FtsZ rings in Bacillus subtilis and Escherichia coli and effects of FtsZ-regulating proteins.
J Bacteriol: 2004, 186(17);5775-81
[PubMed:15317782] [WorldCat.org] [DOI] (P p)

A L Marston, J Errington
Selection of the midcell division site in Bacillus subtilis through MinD-dependent polar localization and activation of MinC.
Mol Microbiol: 1999, 33(1);84-96
[PubMed:10411726] [WorldCat.org] [DOI] (P p)

S Lee, C W Price
The minCD locus of Bacillus subtilis lacks the minE determinant that provides topological specificity to cell division.
Mol Microbiol: 1993, 7(4);601-10
[PubMed:8459776] [WorldCat.org] [DOI] (P p)

P A Levin, P S Margolis, P Setlow, R Losick, D Sun
Identification of Bacillus subtilis genes for septum placement and shape determination.
J Bacteriol: 1992, 174(21);6717-28
[PubMed:1400224] [WorldCat.org] [DOI] (P p)