Difference between revisions of "MreB"

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==Reviews==
 
==Reviews==
 
<pubmed>17506674 17158703 15037301  </pubmed>
 
<pubmed>17506674 17158703 15037301  </pubmed>
==Loclization==
+
==Localization==
 
<pubmed> 17064365,  20566861  </pubmed>
 
<pubmed> 17064365,  20566861  </pubmed>
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==Other original publications==
 
==Other original publications==
 
<pubmed>15752190,11290328,12809607,1400224,19192185,7836311, 16950129, 19192185, 19117023 19643765 19654094 19659933 8459776 11544518 20133608</pubmed>
 
<pubmed>15752190,11290328,12809607,1400224,19192185,7836311, 16950129, 19192185, 19117023 19643765 19654094 19659933 8459776 11544518 20133608</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 13:01, 19 July 2010

  • Description: cell-shape determining protein

Gene name mreB
Synonyms divIVB
Essential yes PubMed
Product cell-shape determining protein
Function cell-shape determination
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
MreB context.gif
This image was kindly provided by SubtiList



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 or addition of 5 mM Magnesium to the growth medium PubMed

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: ftsA/mreB family (according to Swiss-Prot)

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization:
    • forms helical structures close to the inner surface of the cytoplasmic membrane PubMed
    • formation of helical clusters depends on the proton motive force 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

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

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