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

Jeff Errington
Bacterial morphogenesis and the enigmatic MreB helix.
Nat Rev Microbiol: 2015, 13(4);241-8
[PubMed:25578957] [WorldCat.org] [DOI] (I p)

Kathrin Schirner, Ye-Jin Eun, Mike Dion, Yun Luo, John D Helmann, Ethan C Garner, Suzanne Walker
Lipid-linked cell wall precursors regulate membrane association of bacterial actin MreB.
Nat Chem Biol: 2015, 11(1);38-45
[PubMed:25402772] [WorldCat.org] [DOI] (I p)

Fusinita van den Ent, Thierry Izoré, Tanmay Am Bharat, Christopher M Johnson, Jan Löwe
Bacterial actin MreB forms antiparallel double filaments.
Elife: 2014, 3;e02634
[PubMed:24843005] [WorldCat.org] [DOI] (I e)

Philipp V Olshausen, Hervé Joël Defeu Soufo, Kai Wicker, Rainer Heintzmann, Peter L Graumann, Alexander Rohrbach
Superresolution imaging of dynamic MreB filaments in B. subtilis--a multiple-motor-driven transport?
Biophys J: 2013, 105(5);1171-81
[PubMed:24010660] [WorldCat.org] [DOI] (I p)

Christian Reimold, Herve Joel Defeu Soufo, Felix Dempwolff, Peter L Graumann
Motion of variable-length MreB filaments at the bacterial cell membrane influences cell morphology.
Mol Biol Cell: 2013, 24(15);2340-9
[PubMed:23783036] [WorldCat.org] [DOI] (I p)

Felix Dempwolff, Christian Reimold, Michael Reth, Peter L Graumann
Bacillus subtilis MreB orthologs self-organize into filamentous structures underneath the cell membrane in a heterologous cell system.
PLoS One: 2011, 6(11);e27035
[PubMed:22069484] [WorldCat.org] [DOI] (I p)

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

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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