MreB

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  • Description: cell-shape determining protein

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
MreB context.gif
This image was kindly provided by SubtiList



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 or 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:
    • forms helical structures close to the inner surface of the cytoplasmic membrane PubMed
    • formation of helical clusters depends on the proton motive force PubMed

Database entries

  • Structure: 1JCE (from Thermotoga maritima) PubMed
  • 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:

Labs working on this gene/protein

Jeff Errington, Newcastle University, UK homepage

Peter Graumann, Freiburg University, Germany homepage

Your additional remarks

References

Reviews

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)

Loclization

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)

Original publications

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)

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)

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)

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