MreB

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  • Description: cell shape-determining protein, forms filaments, the polymers control/restrict the mobility of the cell wall elongation enzyme complex, required for LytE activity

Gene name mreB
Synonyms divIVB
Essential yes PubMed
Product cell shape-determining protein
Function cell shape determination
Gene expression levels in SubtiExpress: mreB
Interactions involving this protein in SubtInteract: MreB
MW, pI 35 kDa, 4.901
Gene length, protein length 1011 bp, 337 aa
Immediate neighbours mreC, radC
Sequences Protein DNA DNA_with_flanks
Genetic context
MreB context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
MreB expression.png















Categories containing this gene/protein

cell shape, membrane dynamics, cell envelope stress proteins (controlled by SigM, V, W, X, Y), essential genes, membrane proteins

This gene is a member of the following regulons

SigM regulon

The gene

Basic information

  • Locus tag: BSU28030

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
    • forms straight filaments in a heterologous system PubMed
    • polymerizes in the presence of millimolar divalent cations, binds and hydrolyzes GTP and ATP PubMed
    • involved in the organization of ϕ29 DNA replication machinery in peripheral helix-like structures PubMed
    • required for LytE activity PubMed
  • Protein family: ftsA/mreB family (according to Swiss-Prot)

Extended information on the protein

  • Kinetic information:
  • Modification:
  • 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
    • forms antiparallel double filaments 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
    • normal localization depends on the presence of glucolipids, MreB forms irregular clusters in an ugtP mutant 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:
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 1045 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 2367 PubMed

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


Localization


Other original publications

Henrik Strahl, Frank Bürmann, Leendert W Hamoen
The actin homologue MreB organizes the bacterial cell membrane.
Nat Commun: 2014, 5;3442
[PubMed:24603761] [WorldCat.org] [DOI] (I e)

Anne-Stéphanie Rueff, Arnaud Chastanet, Julia Domínguez-Escobar, Zhizhong Yao, James Yates, Maria-Victoria Prejean, Olivier Delumeau, Philippe Noirot, Roland Wedlich-Söldner, Sergio R Filipe, Rut Carballido-López
An early cytoplasmic step of peptidoglycan synthesis is associated to MreB in Bacillus subtilis.
Mol Microbiol: 2014, 91(2);348-62
[PubMed:24261876] [WorldCat.org] [DOI] (I p)

Katarína Muchová, Zuzana Chromiková, Imrich Barák
Control of Bacillus subtilis cell shape by RodZ.
Environ Microbiol: 2013, 15(12);3259-71
[PubMed:23879732] [WorldCat.org] [DOI] (I p)

Patricia Domínguez-Cuevas, Ida Porcelli, Richard A Daniel, Jeff Errington
Differentiated roles for MreB-actin isologues and autolytic enzymes in Bacillus subtilis morphogenesis.
Mol Microbiol: 2013, 89(6);1084-98
[PubMed:23869552] [WorldCat.org] [DOI] (I p)

Daniel Muñoz-Espín, Gemma Serrano-Heras, Margarita Salas
Role of host factors in bacteriophage φ29 DNA replication.
Adv Virus Res: 2012, 82;351-83
[PubMed:22420858] [WorldCat.org] [DOI] (I p)

Satoshi Matsuoka, Minako Chiba, Yu Tanimura, Michihiro Hashimoto, Hiroshi Hara, Kouji Matsumoto
Abnormal morphology of Bacillus subtilis ugtP mutant cells lacking glucolipids.
Genes Genet Syst: 2011, 86(5);295-304
[PubMed:22362028] [WorldCat.org] [DOI] (I p)

Siyuan Wang, Leon Furchtgott, Kerwyn Casey Huang, Joshua W Shaevitz
Helical insertion of peptidoglycan produces chiral ordering of the bacterial cell wall.
Proc Natl Acad Sci U S A: 2012, 109(10);E595-604
[PubMed:22343529] [WorldCat.org] [DOI] (I p)

Yoshikazu Kawai, Jon Marles-Wright, Robert M Cleverley, Robyn Emmins, Shu Ishikawa, Masayoshi Kuwano, Nadja Heinz, Nhat Khai Bui, Christopher N Hoyland, Naotake Ogasawara, Richard J Lewis, Waldemar Vollmer, Richard A Daniel, Jeff Errington
A widespread family of bacterial cell wall assembly proteins.
EMBO J: 2011, 30(24);4931-41
[PubMed:21964069] [WorldCat.org] [DOI] (I e)

Veronica Guariglia-Oropeza, John D Helmann
Bacillus subtilis σ(V) confers lysozyme resistance by activation of two cell wall modification pathways, peptidoglycan O-acetylation and D-alanylation of teichoic acids.
J Bacteriol: 2011, 193(22);6223-32
[PubMed:21926231] [WorldCat.org] [DOI] (I p)

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)

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