MreC is a cell shape determining protein, it couples the cytosolic MreB and MreB-like proteins to the extracellular peptidoglycan-synthesizing machinery
function
cell shape determation
product
cell shape-determining protein
Genomic Context
categories
[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)
2,859,832 -> 2,860,704
Phenotypes of a mutant
''mreC'' is essential under normal conditions [Pubmed|12682299].Depletion of MreC leads to a progressive increase in the width and a decrease in the length of the cell. This shape defect is consistent with a role for ''mreC'' in cell wall synthesis during elongation and has a similar phenotype to other genes with roles in elongation like ''[protein|search|rodA]'' and the redundant gene pair ''[protein|search|pbpA]'' and ''[protein|search|pbpH]''.Electron microscopy of cells depleted of MreC shows regions of the cell where a thick and irregular cell wall has accumulated [Pubmed|12867458,16101995].''mreC'' can be deleted provided that 0.5 M sucrose and 20 mM Mg(2 ) is provided in the media, ''mreC'' is therefore conditionally essential. The phenotype of the ''mreC'' deletion in these conditions is one characterised by extreamly fat and bloated cells that tend to grow in clusters [Pubmed|16101995].The protein
Catalyzed reaction/ biological activity
None/ structural proteinProtein family
mreC family (according to Swiss-Prot) COG1793Paralogous protein(s)
None[SW|Domains]
Intracellular N-terminus, transmembrane domain, Coiled coil domain and C-terminal beta-sheet domain.Structure
[PDB|2J5U]: MreC from ''Listeria monocytogenes'' [Pubmed|17427287][PDB|2QF4]: MreC monomer from ''Streptococcus pneumoniae'' [Pubmed|17707860][PDB|2QF5]: MreC dimer from ''Streptococcus pneumoniae'' [Pubmed|17707860][SW|Localization]
trans-membrane protein [Pubmed|21636744,16101995]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 MreC [Pubmed|16101995,20566861] seem to be misinterpretation of data [Pubmed|21636744][SW|Interactions]
part of the [SW|cell wall biosynthetic complex] [Pubmed|21636744,21636745][protein|search|MreC]-[protein|search|MreD], interacts also with a subset of the [penicillin-binding protein|search|PBPs] [Pubmed|17427287][protein|search|MreC]-[protein|search|GpsB] [Pubmed|18363795]Expression and Regulation
Operon
''[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]Regulation
expression is reduced in a [protein|search|SigV] mutant [Pubmed|21926231]Biological materials
Mutant
A non-polar inframe deletion strain named 3481 and a xylose dependent conditional mutant named 3461 is avaliable from the [SW|Errington] lab [Pubmed|16101995].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 3417 [Pubmed|16101995].Antibody
antisera raised in rabit is avaliable from the [SW|Errington] lab.Labs working on this gene/protein
[SW|Jeff Errington], Newcastle University, UK [http://www.ncl.ac.uk/camb/staff/profile/jeff.errington homepage][SW|Peter Graumann], Freiburg University, Germany [http://www.biologie.uni-freiburg.de/data/bio2/graumann/index.htm homepage]References
20566861,21636744,21636745,18363795,17427287,18179421,8459776,21926231,16101995