Difference between revisions of "MinD"

From SubtiWiki
Jump to: navigation, search
(Additional information)
(Categories containing this gene/protein)
Line 35: Line 35:
 
= [[Categories]] containing this gene/protein =
 
= [[Categories]] containing this gene/protein =
 
{{SubtiWiki category|[[cell division]]}},
 
{{SubtiWiki category|[[cell division]]}},
{{SubtiWiki category|[[cell envelope stress proteins (controlled by SigM, W, X, Y)]]}},
+
{{SubtiWiki category|[[cell envelope stress proteins (controlled by SigM, V, W, X, Y)]]}},
 
{{SubtiWiki category|[[membrane proteins]]}}
 
{{SubtiWiki category|[[membrane proteins]]}}
  

Revision as of 22:06, 24 August 2011

  • Description: cell-division inhibitor (septum placement)

Gene name minD
Synonyms divIVB1
Essential no
Product cell-division inhibitor
Function septum placement
Interactions involving this protein in SubtInteract: MinD
MW, pI 29 kDa, 4.984
Gene length, protein length 804 bp, 268 aa
Immediate neighbours spoIVFA, minC
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
MinD context.gif
This image was kindly provided by SubtiList



Categories containing this gene/protein

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

This gene is a member of the following regulons

SigH regulon, SigM regulon

The gene

Basic information

  • Locus tag: BSU27990

Phenotypes of a mutant

Database entries

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

Additional information

  • A mutation was found in this gene after evolution under relaxed selection for sporulation PubMed

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: MinD subfamily (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)

Original Publications

Christopher T Brown, Laura K Fishwick, Binna M Chokshi, Marissa A Cuff, Jay M Jackson, Travis Oglesby, Alison T Rioux, Enrique Rodriguez, Gregory S Stupp, Austin H Trupp, James S Woollcombe-Clarke, Tracy N Wright, William J Zaragoza, Jennifer C Drew, Eric W Triplett, Wayne L Nicholson
Whole-genome sequencing and phenotypic analysis of Bacillus subtilis mutants following evolution under conditions of relaxed selection for sporulation.
Appl Environ Microbiol: 2011, 77(19);6867-77
[PubMed:21821766] [WorldCat.org] [DOI] (I p)

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)

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)

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)

Sabine Autret, Jeffery Errington
A role for division-site-selection protein MinD in regulation of internucleoid jumping of Soj (ParA) protein in Bacillus subtilis.
Mol Microbiol: 2003, 47(1);159-69
[PubMed:12492861] [WorldCat.org] [DOI] (P p)

Frederico J Gueiros-Filho, Richard Losick
A widely conserved bacterial cell division protein that promotes assembly of the tubulin-like protein FtsZ.
Genes Dev: 2002, 16(19);2544-56
[PubMed:12368265] [WorldCat.org] [DOI] (P p)

M E Karoui, J Errington
Isolation and characterization of topological specificity mutants of minD in Bacillus subtilis.
Mol Microbiol: 2001, 42(5);1211-21
[PubMed:11886553] [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)

A L Marston, H B Thomaides, D H Edwards, M E Sharpe, J Errington
Polar localization of the MinD protein of Bacillus subtilis and its role in selection of the mid-cell division site.
Genes Dev: 1998, 12(21);3419-30
[PubMed:9808628] [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)