A further study on the regulation of microbial proteases.
Various agents were tested for their effects on microbial proteases, which activity was monitored by the analysis of cleaved peptide bands in SDS-polyacrylamide gel electrophoresis. Using casein as a substrate, fungal protease (type XIX) was inhibited by the phenyl methyl sulphonyl fluoride, chymostatin, antipain and leupeptin, while bacterial protease (type XXVI) was inhibited by phosphatidyl glycerol, phosphatidyl inositol and sphingosine. MS2 RNA exerted minor inhibition on the bacterial proteolysis of regulatory subunits of cyclic AMP-dependent protein kinase (A-PK). The cleavage of DNA binding protein by both proteases was inhibited, in the presence of MS2 RNA and lambda DNA. In comparison, phosphatidyl serine slightly stimulated the fungal protease on the cleavage of ribonuclease T1. RNA polymerase is a good substrate of the bacterial protease as indicated by the generation of multiple cleaved peptide fragments, whereas alkaline phosphatase is not susceptible to proteolysis.
Kuo
W N
WN
Division of Science and Mathematics, Bethune-Cookman College, Daytona Beach, Florida 32115.
Ganesan
U
U
Robinson
A D
AD
Fausti
M E
ME
Jean
M N
MN
Flanders
J R
JR
Johnson
G K
GK
D001230:Aspergillus / Q000201:enzymology; D001419:Bacteria / Q000201:enzymology; D002364:Caseins / Q000378:metabolism*; D010450:Endopeptidases / Q000187:drug effects / Q000378:metabolism*; D008055:Lipids / Q000494:pharmacology; D009711:Nucleotides / Q000494:pharmacology; D010455:Peptides / Q000494:pharmacology; D011480:Protease Inhibitors; D013379:Substrate Specificity
D002364:Caseins; D008055:Lipids; D009711:Nucleotides; D010455:Peptides; D011480:Protease Inhibitors; D010450:Endopeptidases