Cell growth and cell division in the rod-shaped actinomycete Corynebacterium glutamicum

Antonie Van Leeuwenhoek. 2008 Jun;94(1):99-109. doi: 10.1007/s10482-008-9224-4. Epub 2008 Feb 19.

Abstract

Bacterial cell growth and cell division are highly complicated and diversified biological processes. In most rod-shaped bacteria, actin-like MreB homologues produce helicoidal structures along the cell that support elongation of the lateral cell wall. An exception to this rule is peptidoglycan synthesis in the rod-shaped actinomycete Corynebacterium glutamicum, which is MreB-independent. Instead, during cell elongation this bacterium synthesizes new cell-wall material at the cell poles whereas the lateral wall remains inert. Thus, the strategy employed by C. glutamicum to acquire a rod-shaped morphology is completely different from that of Escherichia coli or Bacillus subtilis. Cell division in C. glutamicum also differs profoundly by the apparent absence in its genome of homologues of spatial or temporal regulators of cell division, and its cell division apparatus seems to be simpler than those of other bacteria. Here we review recent advances in our knowledge of the C. glutamicum cell cycle in order to further understand this very different model of rod-shape acquisition.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Bacillus subtilis / cytology
  • Bacillus subtilis / genetics
  • Bacillus subtilis / growth & development
  • Bacillus subtilis / metabolism
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Cell Division*
  • Corynebacterium glutamicum / cytology*
  • Corynebacterium glutamicum / genetics
  • Corynebacterium glutamicum / growth & development*
  • Corynebacterium glutamicum / metabolism
  • Escherichia coli / cytology
  • Escherichia coli / genetics
  • Escherichia coli / growth & development
  • Escherichia coli / metabolism
  • Gene Expression Regulation, Bacterial
  • Genome, Bacterial
  • Penicillin-Binding Proteins / genetics
  • Penicillin-Binding Proteins / metabolism

Substances

  • Bacterial Proteins
  • Penicillin-Binding Proteins