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mreD [Tue Dec 08 2015 12:51:32 GMT+0100 (CET)]
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mreD [Tue Dec 08 2015 12:51:32 GMT+0100 (CET)]

MreD is a cell shape determining protein, it couples the cytosolic MreB and MreB-like proteins to the extracellular peptidoglycan-synthesizing machinery
19.00 kDa
cell shape determation
cell shape-determining protein

Genomic Context



  • [category|SW 1|Cellular processes] → [category|SW 1.1|Cell envelope and cell division] → [category|SW 1.1.2|Cell shape]
  • [category|SW 4|Lifestyles] → [category|SW 4.3|Coping with stress] → [category|SW 4.3.2|Cell envelope stress proteins (controlled by SigM, V, W, X, Y)]
  • [category|SW 6|Groups of genes] → [category|SW 6.1|Essential genes]
  • [category|SW 6|Groups of genes] → [category|SW 6.2|Membrane proteins]
  • [SW|Categories] containing this gene/protein

  • [SW|cell shape], [SW|cell envelope stress proteins (controlled by SigM, V, W, X, Y)], [SW|essential genes], [SW|membrane proteins]
  • This gene is a member of the following [SW|regulons]

  • [SW|SigM regulon]
  • Gene

    Coordinates on the chromosome (coding sequence)
    2,859,317 -> 2,859,835

    Phenotypes of a mutant

  • the phenotype of ''mreD'' is similar to that of ''[protein|search|mreC]
  • ''mreD'' is essential under normal conditions [Pubmed|12682299]
  • Depletion of MreD leads to a progressive increase in the width and a decrease in the length of the cell and cells become lytic. In the depletion strain, lysis can be prevented and cell growth, but not cell shape, can be recovered by inculaion of Magnesium in the media. This shape defect is consistent with a role for ''mreD'' in cell wall synthesis during elongation and has a similar phenotype to other genes with roles in elongation.
  • The protein

    Catalyzed reaction/ biological activity

  • None/ structural
  • Protein family

  • mreD family (according to Swiss-Prot) COG2891
  • Paralogous protein(s)

  • None
  • Structure

  • None
  • [SW|Localization]

  • trans-membrane protein [Pubmed|21636744]
  • during logarithmic growth, [protein|search|MreD] forms discrete patches thst move processively along peripheral tracks perpendicular to the cell axis [Pubmed|21636744]
  • forms transverse bands as cells enter the stationary phase [Pubmed|21636744]
  • reports on helical structures formed by MreD [Pubmed|20566861] seem to be misinterpretation of data [Pubmed|21636744]
  • [SW|Interactions]

  • part of the [SW|cell wall biosynthetic complex] [Pubmed|21636744,21636745]
  • [protein|search|MreD] is a member of a suspected group of hubs proteins that were suggested to be involved in a large number of [SW|interactions] [Pubmed|21630458]
  • [protein|search|RodZ]-[protein|search|MreD] [Pubmed|23879732]
  • Expression and Regulation


  • ''[protein|search|radC]-[protein|search|mreB]-[protein|search|mreC]-[protein|search|mreD]-[protein|search|minC]-[protein|search|minD]'' [Pubmed|18179421]
  • ''[protein|search|mreB]-[protein|search|mreC]-[protein|search|mreD]-[protein|search|minC]-[protein|search|minD]'' [Pubmed|8459776]
  • [SW|Sigma factor]

  • ''[protein|search|radC]'': [protein|search|SigM] [Pubmed|18179421]
  • Biological materials


  • A conditional mutant with an inframe deletion of ''mreD'' complemented by a xylose inducible copy at an ectopic locus (strain named 4352) is avaliable from the Errington Group.
  • GFP fusion

  • A functional N-terminal GFP fusion has been made where the fusion protein is the only copy of the gene in the cell: strain 3416 [Pubmed|16101995].
  • Labs working on this gene/protein

  • [SW|Peter Graumann], Freiburg University, Germany [ homepage]
  • References


  • 20566861,21636744,21636745
  • Other original publications

  • 1400224,18156271,16101995,19643765,8459776,18179421,21630458,23879732