LytG of Bacillus subtilis is a novel peptidoglycan hydrolase: the major active glucosaminidase

Biochemistry. 2003 Jan 21;42(2):257-64. doi: 10.1021/bi020498c.

Abstract

LytG (YubE) of Bacillus subtilis is a novel 32 kDa autolysin produced during vegetative growth under the control of Esigma(A) RNA polymerase. Muropeptide analysis of vegetative cells of B. subtilis revealed LytG to be the major glucosaminidase responsible for peptidoglycan structural determination during vegetative growth. Overexpression and purification of LytG allowed its biochemical characterization. Despite sequence homology suggesting muramidase activity, LytG is a novel glucosaminidase with exoenzyme activity and may form part of a novel family of autolysins. It is involved in cell division, lysis, and motility on swarm plates.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacillus subtilis / cytology
  • Bacillus subtilis / enzymology*
  • Bacillus subtilis / genetics
  • Bacillus subtilis / growth & development
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / physiology
  • Bacteriolysis / physiology
  • Base Sequence
  • Cell Division / physiology
  • Cell Wall / enzymology
  • Cell Wall / metabolism
  • Chromatography, High Pressure Liquid
  • Endopeptidases / physiology
  • Gene Expression Regulation, Bacterial
  • Hexosaminidases / chemistry*
  • Hexosaminidases / physiology
  • Hydrolysis
  • Molecular Sequence Data
  • Movement / physiology
  • N-Acetylmuramoyl-L-alanine Amidase / chemistry*
  • N-Acetylmuramoyl-L-alanine Amidase / genetics
  • N-Acetylmuramoyl-L-alanine Amidase / physiology
  • Nuclear Magnetic Resonance, Biomolecular
  • Peptides / analysis
  • Peptidoglycan / chemistry
  • Protein Binding

Substances

  • Bacterial Proteins
  • Peptides
  • Peptidoglycan
  • Hexosaminidases
  • Endopeptidases
  • gamma-D-glutamyl-meso-diaminopimelate peptidase I
  • N-Acetylmuramoyl-L-alanine Amidase