Extracellular proteolytic activation of bacteriolytic peptidoglycan hydrolases of Staphylococcus simulans biovar staphylolyticus.
Staphylococcus simulans biovar staphylolyticus secreted two bacteriolytic peptidoglycan hydrolases as proproteins that were activated as they were processed by an extracellular sulphydryl protease. This processing resulted in the production of multiple molecular-mass forms of each enzyme. Cells from early exponential phase cultures were susceptible to lysis by the mature forms of each of the peptidoglycan hydrolases whereas stationary phase cells were resistant. Thus secretion of these bacteriolytic enzymes during early exponential growth as precursors that are activated later by the protease would provide time for the cells to become resistant.
Neumann
V C
VC
Department of Biological Sciences, University of Alabama, Tuscaloosa 35487.
Heath
H E
HE
LeBlanc
P A
PA
Sloan
G L
GL
D001426:Bacterial Proteins / Q000378:metabolism*; D001433:Bacteriolysis; D003546:Cysteine Endopeptidases / Q000378:metabolism*; D010450:Endopeptidases / Q000378:metabolism*; D004789:Enzyme Activation; D004792:Enzyme Precursors / Q000378:metabolism*; D005110:Extracellular Space; D008837:Micrococcus; D008970:Molecular Weight; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000378:metabolism*; D013210:Staphylococcus / Q000201:enzymology* / Q000502:physiology; D013211:Staphylococcus aureus; D001619:beta-N-Acetylhexosaminidases / Q000378:metabolism*
D001426:Bacterial Proteins; D004792:Enzyme Precursors; D001619:beta-N-Acetylhexosaminidases; D010450:Endopeptidases; D003546:Cysteine Endopeptidases; D009238:N-Acetylmuramoyl-L-alanine Amidase