MreB

• 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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

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

• 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

• BsubCyc: BSU28030

• DBTBS entry: [1]

• SubtiList entry: [2]

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)

• Paralogous protein(s): Mbl, MreBH

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactors:

• Effectors of protein activity:

• Interactions:
  • part of the cell wall biosynthetic complex PubMed
  • forms antiparallel double filaments PubMed
  • MreB-TufA PubMed
  • MreB-Mbl PubMed
  • MreB-MreBH PubMed
  • MreB-TagT PubMed
  • MreB-TagU PubMed
  • RodZ-MreB PubMed
  • DapI-MreB PubMed
  • MreB-PonA PubMed

• 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

• BsubCyc: BSU28030

• Structure: 1JCE (from Thermotoga maritima) PubMed

• UniProt: Q01465

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon:
  • radC-mreB-mreC-mreD-minC-minD PubMed
  • mreB-mreC-mreD-minC-minD PubMed

• Expression browser: mreB PubMed

• Sigma factor:
  • radC: SigM PubMed

• Regulation:
  • expression is reduced in a SigV mutant PubMed
  • expression is increased in an ugtP mutant PubMed

• 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:

• 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

References

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)