MreB

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

Gene name	mreB
Synonyms	divIVB
Essential	yes PubMed
Product	cell shape-determining protein
Function	cell shape determination
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
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

cell shape, 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

• 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

• Protein family: ftsA/mreB family (according to Swiss-Prot)

• Paralogous protein(s): Mbl, MreBH

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:
  • part of the cell wall biosynthetic complex PubMed
  • MreB-TufA PubMed
  • MreB-Mbl PubMed
  • MreB-MreBH PubMed
  • MreB-TagT PubMed
  • MreB-TagU 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
  • 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

• 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:

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

Additional reviews: PubMed

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)

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

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)

Localization

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

Additional publications: PubMed