MreC

• Description: MreC is a cell shape determining protein and is associated with the MreB cytoskeleton in B. subtilis and other rod shaped bacteria.
  
  

Gene name	mreC
Synonyms
Essential	yes PubMed
Product	cell-shape determining protein
Function	cell-shape determation
MW, pI	32 kDa, 6.248
Gene length, protein length	870 bp, 290 aa
Immediate neighbours	mreD, mreB
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, W, X, Y), essential genes, membrane proteins

This gene is a member of the following regulons

SigH regulon

The gene

Basic information

• Locus tag: BSU28020

Phenotypes of a mutant

• mreC is essential under normal conditions PubMed.
• 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 rodA and the redundant gene pair pbpA and pbpH.
  • Electron microscopy of cells depleted of MreC shows regions of the cell where a thick and irregular cell wall has accumulated PubMed.
  • mreC can be deleted provided that 0.5 M sucrose and 20 mM Mg(2+) is provided in the media, mreC is therefore conditionally essentail. 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.

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

Additional information

Function

MreC functions in cell wall synthesis by, together with the MreB cytoskeleton, localizing the cell wall synthetic machinery to the correct part of the cell. MreC therefore ensures that the cell wall is made in the correct way to maintain the proper shape of the cell.

MreC in other organisms

MreC has been studied in other organisms where it has been shown to be important in cell shape determination.

• Escherichia coli PubMed PubMed
• Caulobacter cresentus PubMed PubMed
• Rhodobacter spheroides PubMed
• Streptomyces coelicolor PubMed

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: None/ structural protein

• Protein family: mreC family (according to Swiss-Prot) COG1793

• Paralogous protein(s): None

Extended information on the protein

• Kinetic information:

• Domains: Intracellular N-terminus, transmembrane domain, Coiled coil domain and C-terminal beta-sheet domain.

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions: MreC-MreD, interacts also with a subset of the PBPs PubMed

• Localization:
  • GFP-MreC localises to the cell membrane in a helical pattern PubMed.
  • formation of helical clusters depends on the proton motive force PubMed

Database entries

• Structure:
  • 2J5U: MreC from Listeria monocytogenes PubMed
  • 2QF4: MreC monomer from Streptococcus pneumoniae PubMed
  • 2QF5: MreC dimer from Streptococcus pneumoniae PubMed

• UniProt: Q01466

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: mreB-mreC-mreD-minC-minD PubMed

• Sigma factor: SigH PubMed

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant: A non-polar inframe deletion strain named 3481 and a xylose dependent conditional mutant named 3461 is avaliable from the Errington lab PubMed.

• Expression vector:

• lacZ fusion:

• 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.

• two-hybrid system:

• Antibody: antisera raised in rabit is avaliable from the Errington lab.

Labs working on this gene/protein

Jeff Errington, Newcastle University, UK homepage

Peter Graumann, Freiburg University, Germany homepage

Your additional remarks

mreC is an abbreviation of murein region e, gene C

References

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)