Limited proteolysis of actin by a specific bacterial protease.
A 36 kDa fragment of rabbit skeletal muscle actin resistant to further proteolytic breakdown was obtained with a new bacterial protease. This fragment was the only cleavage product obtained from native actin whereas proteolysis of heat-inactivated actin was unlimited. The 36 kDa fragment failed to polymerize and to inhibit DNase I activity. Binding to DNase I protects actin against proteolysis by protease. The results on actin proteolysis by different proteases are compared.
Khaitlina SYu
Institute of Cytology, USSR Academy of Sciences, Leningrad.
Smirnova
T D
TD
Usmanova
A M
AM
D000199:Actins / Q000378:metabolism*; D000818:Animals; D003850:Deoxyribonuclease I / Q000378:metabolism; D004351:Drug Resistance; D004926:Escherichia coli / Q000201:enzymology*; D006868:Hydrolysis; D009132:Muscles / Q000378:metabolism; D010447:Peptide Hydrolases / Q000378:metabolism*; D011817:Rabbits
D000199:Actins; D003850:Deoxyribonuclease I; D010447:Peptide Hydrolases