Journal of Bacteriology · 1998 · 97 citations · 23 references
Life SciencesMicrobiologyMolecular BiologyBacteriologyEnzymologyMicrobial GeneticsCell Wall BiochemistryMicrobial Cell StructureProtein StructureBacterial Cell Wall PhysiologyCatalytic ActivityCell Wall HydrolasesCell Wall ProteinsExponential GrowthLytic EnzymesPeptidoglycan Cell WallPeptidoglycan Degradation
Bacillus subtilis cell wall-bound protein CWBP33 is encoded by lytE, a gene expressed during the exponential growth phase. Sequence analysis of LytE, a 33-kDa protein, reveals two domains. The N-terminal domain contains a threefold-repeated motif common to several peptidoglycan binding proteins, while the C-terminal domain, probably carrying the catalytic activity, has homology with certain exoproteins. Zymographs unambiguously reveal that the absence of CWBP33, due to inactivation of lytE, is accompanied by the loss of a lytic activity. In lytE mutants, the cell autolysis rate is significantly decreased, although autolysis of corresponding, purified cell walls does not seem to be affected.
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