Difference between revisions of "DivIVA"
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==Original Publications== | ==Original Publications== | ||
<pubmed>22582279, 19654604, 19666580,9219999,19019154,15554965, 12368265,11445541,10835369,12511520,14651647, 19478798 ,19429628, 11445541, 9219999, 9045828 20352045 20502438 11886553 21564336 22108385 22457634 22517742 22661688 </pubmed> | <pubmed>22582279, 19654604, 19666580,9219999,19019154,15554965, 12368265,11445541,10835369,12511520,14651647, 19478798 ,19429628, 11445541, 9219999, 9045828 20352045 20502438 11886553 21564336 22108385 22457634 22517742 22661688 </pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 11:13, 26 June 2012
- Description: cell-division initiation protein (septum placement), part of the Min system (with MinC, MinD, MinJ), Noc and the Min system ensure the efficient utilization of the division site at midcell in by ensuring Z ring placement
Gene name | divIVA |
Synonyms | ylmJ |
Essential | no |
Product | cell-division initiation protein |
Function | septum placement |
Interactions involving this protein in SubtInteract: DivIVA | |
MW, pI | 19 kDa, 4.846 |
Gene length, protein length | 492 bp, 164 aa |
Immediate neighbours | ylmH, ileS |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
cell division, membrane proteins, phosphoproteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU15420
Phenotypes of a mutant
Deletion of divIVA leads to filamentation and polar divisions that in turn cause a minicell phenotype. PubMed A divIVA mutant has a severe sporulation defect. PubMed
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
Filamentation is suppressed by mutations in minCD PubMed.
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: DivIVA is required for polar localisation of MinCD via MinJ. PubMed It also recruits RacA to the distal pole of the prespore PubMed.
- Protein family: gpsB family (according to Swiss-Prot)
- Paralogous protein(s): GpsB
Extended information on the protein
- Kinetic information:
- Domains: The first 60 amino acids constitute a lipid binding domain. PubMed
Multimerisation involves two coiled-coil motifs, one in the lipid binding domain, and the other one being present in the helical C-terminal domain PubMed.
- Modification:
- Cofactor(s): not known
- Effectors of protein activity: not known
Database entries
- UniProt: P71021
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon: divIVA PubMed
- Sigma factor:
- Additional information:
Biological materials
- Mutant: divIVA::tet available from the Hamoen Lab
- Expression vector:
- lacZ fusion:
- GFP fusion: divIVA-gfp fusions available from the Hamoen Lab
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Leendert Hamoen, Centre for Bacterial Cell Biology, Newcastle upon Tyne, United Kingdom [4]
Imrich Barak, Slovak Academy of Science, Bratislava, Slovakia homepage
Your additional remarks
References
Reviews
Karan Gautam Kaval, Sven Halbedel
Architecturally the same, but playing a different game: the diverse species-specific roles of DivIVA proteins.
Virulence: 2012, 3(4);406-7
[PubMed:22722244]
[WorldCat.org]
[DOI]
(I p)
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)
Jennifer R Juarez, William Margolin
Irresistible curves.
EMBO J: 2009, 28(15);2147-8
[PubMed:19654604]
[WorldCat.org]
[DOI]
(I p)
Original Publications
Joe Pogliano, Nicolas Pogliano, Jared A Silverman
Daptomycin-mediated reorganization of membrane architecture causes mislocalization of essential cell division proteins.
J Bacteriol: 2012, 194(17);4494-504
[PubMed:22661688]
[WorldCat.org]
[DOI]
(I p)
Valquiria Tiago dos Santos, Alexandre W Bisson-Filho, Frederico J Gueiros-Filho
DivIVA-mediated polar localization of ComN, a posttranscriptional regulator of Bacillus subtilis.
J Bacteriol: 2012, 194(14);3661-9
[PubMed:22582279]
[WorldCat.org]
[DOI]
(I p)
Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742]
[WorldCat.org]
[DOI]
(I p)
Christopher D A Rodrigues, Elizabeth J Harry
The Min system and nucleoid occlusion are not required for identifying the division site in Bacillus subtilis but ensure its efficient utilization.
PLoS Genet: 2012, 8(3);e1002561
[PubMed:22457634]
[WorldCat.org]
[DOI]
(I p)
Prahathees Eswaramoorthy, Marcella L Erb, James A Gregory, Jared Silverman, Kit Pogliano, Joe Pogliano, Kumaran S Ramamurthi
Cellular architecture mediates DivIVA ultrastructure and regulates min activity in Bacillus subtilis.
mBio: 2011, 2(6);
[PubMed:22108385]
[WorldCat.org]
[DOI]
(I e)
Kenneth Briley, Peter Prepiak, Miguel J Dias, Jeanette Hahn, David Dubnau
Maf acts downstream of ComGA to arrest cell division in competent cells of B. subtilis.
Mol Microbiol: 2011, 81(1);23-39
[PubMed:21564336]
[WorldCat.org]
[DOI]
(I p)
Maria A Oliva, Sven Halbedel, Stefan M Freund, Pavel Dutow, Thomas A Leonard, Dmitry B Veprintsev, Leendert W Hamoen, Jan Löwe
Features critical for membrane binding revealed by DivIVA crystal structure.
EMBO J: 2010, 29(12);1988-2001
[PubMed:20502438]
[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)
Kumaran S Ramamurthi, Richard Losick
Negative membrane curvature as a cue for subcellular localization of a bacterial protein.
Proc Natl Acad Sci U S A: 2009, 106(32);13541-5
[PubMed:19666580]
[WorldCat.org]
[DOI]
(I p)
Jennifer R Juarez, William Margolin
Irresistible curves.
EMBO J: 2009, 28(15);2147-8
[PubMed:19654604]
[WorldCat.org]
[DOI]
(I p)
Rok Lenarcic, Sven Halbedel, Loek Visser, Michael Shaw, Ling Juan Wu, Jeff Errington, Davide Marenduzzo, Leendert W Hamoen
Localisation of DivIVA by targeting to negatively curved membranes.
EMBO J: 2009, 28(15);2272-82
[PubMed:19478798]
[WorldCat.org]
[DOI]
(I p)
Pamela Gamba, Jan-Willem Veening, Nigel J Saunders, Leendert W Hamoen, Richard A Daniel
Two-step assembly dynamics of the Bacillus subtilis divisome.
J Bacteriol: 2009, 191(13);4186-94
[PubMed:19429628]
[WorldCat.org]
[DOI]
(I 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)
S E Perry, D H Edwards
Identification of a polar targeting determinant for Bacillus subtilis DivIVA.
Mol Microbiol: 2004, 54(5);1237-49
[PubMed:15554965]
[WorldCat.org]
[DOI]
(P p)
Virginie Molle, Masaya Fujita, Shane T Jensen, Patrick Eichenberger, José E González-Pastor, Jun S Liu, Richard Losick
The Spo0A regulon of Bacillus subtilis.
Mol Microbiol: 2003, 50(5);1683-701
[PubMed:14651647]
[WorldCat.org]
[DOI]
(P p)
Leendert W Hamoen, Jeffery Errington
Polar targeting of DivIVA in Bacillus subtilis is not directly dependent on FtsZ or PBP 2B.
J Bacteriol: 2003, 185(2);693-7
[PubMed:12511520]
[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)
H B Thomaides, M Freeman, M El Karoui, J Errington
Division site selection protein DivIVA of Bacillus subtilis has a second distinct function in chromosome segregation during sporulation.
Genes Dev: 2001, 15(13);1662-73
[PubMed:11445541]
[WorldCat.org]
[DOI]
(P p)
D H Edwards, H B Thomaides, J Errington
Promiscuous targeting of Bacillus subtilis cell division protein DivIVA to division sites in Escherichia coli and fission yeast.
EMBO J: 2000, 19(11);2719-27
[PubMed:10835369]
[WorldCat.org]
[DOI]
(P p)
D H Edwards, J Errington
The Bacillus subtilis DivIVA protein targets to the division septum and controls the site specificity of cell division.
Mol Microbiol: 1997, 24(5);905-15
[PubMed:9219999]
[WorldCat.org]
[DOI]
(P p)
J H Cha, G C Stewart
The divIVA minicell locus of Bacillus subtilis.
J Bacteriol: 1997, 179(5);1671-83
[PubMed:9045828]
[WorldCat.org]
[DOI]
(P p)