mreB [2017-12-20 16:36:21]

cell shape-determining protein, forms filaments, the polymers control/restrict the mobility of the cell wall elongation enzyme complex, required for LytE activity

Locus: BSU28030

Isoelectric point: 4.90

Molecular weight: 35.79 kDa

Protein length: 337 aa

Gene length: 1011 bp

Function: cell shape determination

Product: cell shape-determining protein

Essential: yes

Synonyms: divIVB

Genomic Context

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Categories containing this gene/protein

• Cellular processes → Cell envelope and cell division → Cell shape
• Cellular processes → Cell envelope and cell division → Membrane dynamics
• Lifestyles → Coping with stress → Cell envelope stress proteins (controlled by SigM, V, W, X, Y)
• Groups of genes → Essential genes
• Groups of genes → Membrane proteins

Gene

Coordinates: 2,860,735 → 2,861,748

Phenotypes of a mutant

• essential PubMed
• the mutation can be suppressed by inactivation of ponA, ptsI, ccpA PubMed, by overexpression of GlmR PubMed, or by addition of 5 mM magnesium to the growth medium PubMed

The protein

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)

Paralogous protein(s)

• Mbl, MreBH

Modification

• acetylated at Lys-240, this is important for restricting cell wall growth and cell diameter PubMed

Structure

• 1JCF (from Thermotoga maritima, 57% identity) PubMed

Localization

• during logarithmic growth, MreB forms discrete patches that move processively along peripheral tracks perpendicular to the cell axis PubMed
• forms transverse bands as cells enter the stationary phase PubMed
• forms antiparallel double filaments 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
• during stationary phase: delocalized in the cytoplasm PubMed
• during development of genetic competence: co-localizes with polar clusters of the late competence protein ComGA (ComGA sequesters MreB) PubMed
• MreB patch speed depends on the growth rate, the faster growth, the higher the patch speed PubMed

Expression and Regulation

Operons

• Genes: mreB-mreC-mreD-minC-minD
  Description: PubMed

  Sigma factors

  • SigA: sigma factor, promoter p1, upstream of Maf PubMed, in SigA regulon
  • SigM: sigma factor, promoter p2, within Maf PubMed, in SigM regulon
  • SigH: sigma factor, promoter p4, upstream of MinC PubMed, in SigH regulon

  Regulatory mechanism

  • ComK: activation, PubMed, in ComK regulon

  Regulation

  • constitutively expressed PubMed

• Genes: maf-radC-mreB-mreC-mreD-minC-minD
  Description: PubMed

  Sigma factors

  • SigM: sigma factor, promoter p2 within Maf PubMed, in SigM regulon
  • SigA: sigma factor, promoter p1, upstream of Maf PubMed, in SigA regulon

  Regulatory mechanism

  • ComK: activation, PubMed, in ComK regulon

  Regulation

  • constitutively expressed PubMed

Biological materials

Two-hybrid system

• B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in the labs of Jeff Errington and Boris Görke

Antibody

• available in the Jeff Errington and Peter Graumann labs

Labs working on this gene/protein

• Jeff Errington, Newcastle University, UK homepage
• Peter Graumann, Freiburg University, Germany homepage

References

Reviews

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Localization

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Other original publications

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