Location of the calmodulin- and actin-binding domains at the C-terminus of caldesmon.
Digestion of caldesmon with carboxypeptidase Y is accompanied by loss of its ability to inhibit actomyosin ATPase activity and to bind actin and calmodulin. Similarly, carboxypeptidase Y digestion of a terminal 40 kDa chymotryptic fragment of caldesmon abolishes its inhibition of the actomyosin ATPase and binding to actin and calmodulin. This represents the first direct demonstration that these functional domains of caldesmon are located close to the carboxy-terminus of the molecule.
Makuch
R
R
Department of Muscle Biochemistry, Nencki Institute of Experimental Biology, Warsaw, Poland.
Walsh
M P
MP
Dabrowska
R
R
D000199:Actins / Q000378:metabolism*; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001665:Binding Sites; D002147:Calmodulin / Q000378:metabolism*; D002148:Calmodulin-Binding Proteins / Q000378:metabolism* / Q000494:pharmacology; D002268:Carboxypeptidases / Q000378:metabolism; D002645:Chickens; D002918:Chymotrypsin / Q000378:metabolism; D005895:Gizzard, Avian / Q000032:analysis; D008970:Molecular Weight; D009218:Myosins / Q000037:antagonists & inhibitors; D010446:Peptide Fragments / Q000378:metabolism; D011817:Rabbits
D000199:Actins; D000596:Amino Acids; D002147:Calmodulin; D002148:Calmodulin-Binding Proteins; D010446:Peptide Fragments; D002268:Carboxypeptidases; C022633:serine carboxypeptidase; D002918:Chymotrypsin; D009218:Myosins