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

Reviews

Arnaud Chastanet, Rut Carballido-Lopez
The actin-like MreB proteins in Bacillus subtilis: a new turn.
Front Biosci (Schol Ed): 2012, 4(4);1582-606
[PubMed:22652894] [WorldCat.org] [DOI] (I e)

Sven van Teeffelen, Zemer Gitai
Rotate into shape: MreB and bacterial morphogenesis.
EMBO J: 2011, 30(24);4856-7
[PubMed:22166997] [WorldCat.org] [DOI] (I e)

Courtney L White, James W Gober
MreB: pilot or passenger of cell wall synthesis?
Trends Microbiol: 2012, 20(2);74-9
[PubMed:22154164] [WorldCat.org] [DOI] (I p)

Andrew Jermy
Bacterial physiology: MreB takes a back seat.
Nat Rev Microbiol: 2011, 9(8);560-1
[PubMed:21725336] [WorldCat.org] [DOI] (I e)

Johann Mignolet, Patrick H Viollier
A sweet twist gets Bacillus into shape.
Mol Microbiol: 2011, 80(2);283-5
[PubMed:21371139] [WorldCat.org] [DOI] (I p)

Matthew T Cabeen, Christine Jacobs-Wagner
The bacterial cytoskeleton.
Annu Rev Genet: 2010, 44;365-92
[PubMed:21047262] [WorldCat.org] [DOI] (I p)

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)