Diversity of Firmicutes peptidoglycan hydrolases and specificities of those involved in daughter cell separation

Res Microbiol. 2008 Sep-Oct;159(7-8):507-15. doi: 10.1016/j.resmic.2008.06.008. Epub 2008 Jul 4.

Abstract

Within Streptococcus thermophilus, Cse was identified as the major cell disconnecting peptidoglycan hydrolase (PGH) and was demonstrated to be species-specific. To identify cell disconnecting PGHs encoded by other Streptococcus genomes, we explored the diversity of domains carried by Firmicutes PGHs, and especially that of enzymes involved in daughter cell separation. This work brings to light the diversity of PGHs and reveals that each species recruits its own cell-separating enzyme distinct from that of the others. This specificity is probably correlated with the diversity of substrates found in the bacterial cell wall.

Publication types

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

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Cell Division
  • Genome, Bacterial
  • Gram-Positive Bacteria / chemistry*
  • Gram-Positive Bacteria / enzymology*
  • Gram-Positive Bacteria / genetics
  • Molecular Sequence Data
  • N-Acetylmuramoyl-L-alanine Amidase / chemistry*
  • N-Acetylmuramoyl-L-alanine Amidase / genetics
  • N-Acetylmuramoyl-L-alanine Amidase / metabolism
  • Protein Structure, Tertiary
  • Species Specificity
  • Substrate Specificity

Substances

  • Bacterial Proteins
  • N-Acetylmuramoyl-L-alanine Amidase