MreB
- Description: cell shape-determining protein, forms filaments, the polymers control/restrict the mobility of the cell wall elongation enzyme complex
Gene name | mreB |
Synonyms | divIVB |
Essential | yes PubMed |
Product | cell shape-determining protein |
Function | cell shape determination |
MW, pI | 35 kDa, 4.901 |
Gene length, protein length | 1011 bp, 337 aa |
Immediate neighbours | mreC, radC |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
Categories containing this gene/protein
cell shape, cell envelope stress proteins (controlled by SigM, W, X, Y), essential genes, membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU28030
Phenotypes of a mutant
- essential PubMed
- the mutation can be suppressed by inactivation of ponA, ptsI, ccpA PubMed, by overexpression of YvcK PubMed, or by addition of 5 mM magnesium to the growth medium PubMed
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: ftsA/mreB family (according to Swiss-Prot)
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization:
- during logarithmic growth, MreB forms discrete patches thst move processively along peripheral tracks perpendicular to the cell axis PubMed
- forms transverse bands as cells enter the stationary phase PubMed
- close to the inner surface of the cytoplasmic membrane PubMed
- reports on helical structures formed by MreB PubMed seem to be misinterpretation of data PubMed
Database entries
- UniProt: Q01465
- 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: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in the labs of Jeff Errington and Boris Görke
- Antibody: available in the Jeff Errington and Peter Graumann labs
Labs working on this gene/protein
Jeff Errington, Newcastle University, UK homepage
Peter Graumann, Freiburg University, Germany homepage
Your additional remarks
References
Reviews
Additional reviews: PubMed
Andrew Jermy
Bacterial physiology: MreB takes a back seat.
Nat Rev Microbiol: 2011, 9(8);560-1
[PubMed:21725336]
[WorldCat.org]
[DOI]
(I e)
Kevin D Young
Bacterial shape: two-dimensional questions and possibilities.
Annu Rev Microbiol: 2010, 64;223-40
[PubMed:20825347]
[WorldCat.org]
[DOI]
(I p)
Peter L Graumann
Cytoskeletal elements in bacteria.
Annu Rev Microbiol: 2007, 61;589-618
[PubMed:17506674]
[WorldCat.org]
[DOI]
(P p)
Rut Carballido-López
The bacterial actin-like cytoskeleton.
Microbiol Mol Biol Rev: 2006, 70(4);888-909
[PubMed:17158703]
[WorldCat.org]
[DOI]
(P p)
Linda A Amos, Fusinita van den Ent, Jan Löwe
Structural/functional homology between the bacterial and eukaryotic cytoskeletons.
Curr Opin Cell Biol: 2004, 16(1);24-31
[PubMed:15037301]
[WorldCat.org]
[DOI]
(P p)
Localization
Ethan C Garner, Remi Bernard, Wenqin Wang, Xiaowei Zhuang, David Z Rudner, Tim Mitchison
Coupled, circumferential motions of the cell wall synthesis machinery and MreB filaments in B. subtilis.
Science: 2011, 333(6039);222-5
[PubMed:21636745]
[WorldCat.org]
[DOI]
(I p)
Julia Domínguez-Escobar, Arnaud Chastanet, Alvaro H Crevenna, Vincent Fromion, Roland Wedlich-Söldner, Rut Carballido-López
Processive movement of MreB-associated cell wall biosynthetic complexes in bacteria.
Science: 2011, 333(6039);225-8
[PubMed:21636744]
[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)
Hervé Joël Defeu Soufo, Peter L Graumann
Dynamic localization and interaction with other Bacillus subtilis actin-like proteins are important for the function of MreB.
Mol Microbiol: 2006, 62(5);1340-56
[PubMed:17064365]
[WorldCat.org]
[DOI]
(P p)
Other original publications
Elodie Foulquier, Frédérique Pompeo, Alain Bernadac, Leon Espinosa, Anne Galinier
The YvcK protein is required for morphogenesis via localization of PBP1 under gluconeogenic growth conditions in Bacillus subtilis.
Mol Microbiol: 2011, 80(2);309-18
[PubMed:21320184]
[WorldCat.org]
[DOI]
(I p)
Hervé Joël Defeu Soufo, Peter L Graumann
Bacillus subtilis MreB paralogues have different filament architectures and lead to shape remodelling of a heterologous cell system.
Mol Microbiol: 2010, 78(5);1145-58
[PubMed:21091501]
[WorldCat.org]
[DOI]
(I p)
Hervé Joël Defeu Soufo, Christian Reimold, Uwe Linne, Tobias Knust, Johannes Gescher, Peter L Graumann
Bacterial translation elongation factor EF-Tu interacts and colocalizes with actin-like MreB protein.
Proc Natl Acad Sci U S A: 2010, 107(7);3163-8
[PubMed:20133608]
[WorldCat.org]
[DOI]
(I p)
Yoshikazu Kawai, Kei Asai, Jeffery Errington
Partial functional redundancy of MreB isoforms, MreB, Mbl and MreBH, in cell morphogenesis of Bacillus subtilis.
Mol Microbiol: 2009, 73(4);719-31
[PubMed:19659933]
[WorldCat.org]
[DOI]
(I p)
Daniel Muñoz-Espín, Richard Daniel, Yoshikazu Kawai, Rut Carballido-López, Virginia Castilla-Llorente, Jeff Errington, Wilfried J J Meijer, Margarita Salas
The actin-like MreB cytoskeleton organizes viral DNA replication in bacteria.
Proc Natl Acad Sci U S A: 2009, 106(32);13347-52
[PubMed:19654094]
[WorldCat.org]
[DOI]
(I p)
Kathrin Schirner, Jeff Errington
Influence of heterologous MreB proteins on cell morphology of Bacillus subtilis.
Microbiology (Reading): 2009, 155(Pt 11);3611-3621
[PubMed:19643765]
[WorldCat.org]
[DOI]
(I p)
Yoshikazu Kawai, Richard A Daniel, Jeffery Errington
Regulation of cell wall morphogenesis in Bacillus subtilis by recruitment of PBP1 to the MreB helix.
Mol Microbiol: 2009, 71(5);1131-44
[PubMed:19192185]
[WorldCat.org]
[DOI]
(I p)
Joshua A Mayer, Kurt J Amann
Assembly properties of the Bacillus subtilis actin, MreB.
Cell Motil Cytoskeleton: 2009, 66(2);109-18
[PubMed:19117023]
[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)
Rut Carballido-López, Alex Formstone, Ying Li, S Dusko Ehrlich, Philippe Noirot, Jeff Errington
Actin homolog MreBH governs cell morphogenesis by localization of the cell wall hydrolase LytE.
Dev Cell: 2006, 11(3);399-409
[PubMed:16950129]
[WorldCat.org]
[DOI]
(P p)
Alex Formstone, Jeffery Errington
A magnesium-dependent mreB null mutant: implications for the role of mreB in Bacillus subtilis.
Mol Microbiol: 2005, 55(6);1646-57
[PubMed:15752190]
[WorldCat.org]
[DOI]
(P p)
Richard A Daniel, Jeff Errington
Control of cell morphogenesis in bacteria: two distinct ways to make a rod-shaped cell.
Cell: 2003, 113(6);767-76
[PubMed:12809607]
[WorldCat.org]
[DOI]
(P p)
F van den Ent, L A Amos, J Löwe
Prokaryotic origin of the actin cytoskeleton.
Nature: 2001, 413(6851);39-44
[PubMed:11544518]
[WorldCat.org]
[DOI]
(P p)
L J Jones, R Carballido-López, J Errington
Control of cell shape in bacteria: helical, actin-like filaments in Bacillus subtilis.
Cell: 2001, 104(6);913-22
[PubMed:11290328]
[WorldCat.org]
[DOI]
(P p)
Y Abhayawardhane, G C Stewart
Bacillus subtilis possesses a second determinant with extensive sequence similarity to the Escherichia coli mreB morphogene.
J Bacteriol: 1995, 177(3);765-73
[PubMed:7836311]
[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)