Degradation of proteins with blocked amino groups by cytoplasmic proteases.
The effect of blocking amino groups on the susceptibility of BSA and calmodulin to high molecular weight protease (HMP) and calpain, the two major cytosolic proteases, was studied. Both proteases hydrolyzed methylated vs. unmodified BSA more slowly. Methylation of BSA resulted in the accumulation of proteolytic intermediates, especially of larger sizes. However, similar fragments were generated from unmodified BSA indicating that rates of hydrolysis rather that sites of proteolytic cleavage were altered. Calmodulin from Dictyostelium discoideum was hydrolyzed rapidly by HMP whereas brain and muscle calmodulins which have a epsilon-N-trimethyl residue on the single surface lysine were relatively stable.
D000818:Animals; D002147:Calmodulin / Q000378:metabolism*; D002154:Calpain / Q000378:metabolism*; D003600:Cytosol / Q000201:enzymology; D006868:Hydrolysis; D007700:Kinetics; D009132:Muscles / Q000201:enzymology; D010447:Peptide Hydrolases / Q000097:blood*; D011817:Rabbits; D051381:Rats; D012156:Reticulocytes / Q000201:enzymology; D012710:Serum Albumin, Bovine / Q000378:metabolism*
D002147:Calmodulin; D012710:Serum Albumin, Bovine; D010447:Peptide Hydrolases; D002154:Calpain