The importance of C-terminal amino acid residues of actin to the inhibition of actomyosin ATPase activity by caldesmon and troponin I.
Proteolytic elimination of three C-terminal amino acid residues from actin weakens its interaction with caldesmon and troponin I and, in consequence, lowers the inhibitory effects of both proteins on actomyosin ATPase activity. These results prove the importance of C-terminal extremity of actin to the overall interaction of this protein with caldesmon and troponin I.
Makuch
R
R
Department of Muscle Biochemistry, Nencki Institute of Experimental Biology, Warsaw, Poland.
Kołakowski
J
J
Dabrowska
R
R
D000199:Actins / Q000737:chemistry* / Q000502:physiology; D000818:Animals; D017301:Ca(2+) Mg(2+)-ATPase / Q000378:metabolism; D002148:Calmodulin-Binding Proteins / Q000502:physiology*; D002645:Chickens; D004789:Enzyme Activation; D009218:Myosins / Q000037:antagonists & inhibitors*; D014336:Troponin / Q000502:physiology*; D019210:Troponin I
D000199:Actins; D002148:Calmodulin-Binding Proteins; D014336:Troponin; D019210:Troponin I; D017301:Ca(2+) Mg(2+)-ATPase; D009218:Myosins