Difference between revisions of "MreB"

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(Extended information on the protein)
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=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU28030&redirect=T BSU28030]
  
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/mreBCD-minCD.html]
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/mreBCD-minCD.html]
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=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU28030&redirect=T BSU28030]
  
 
* '''Structure:''' [http://www.rcsb.org/pdb/explore/explore.do?pdbId=1JCE 1JCE] (from ''Thermotoga maritima'') {{PubMed|11544518}}  
 
* '''Structure:''' [http://www.rcsb.org/pdb/explore/explore.do?pdbId=1JCE 1JCE] (from ''Thermotoga maritima'') {{PubMed|11544518}}  

Revision as of 14:24, 2 April 2014

  • 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, 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
    • 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:

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

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