TY - JOUR
T1 - Light chain phosphorylation alters the conformation of skeletal muscle myosin
AU - Ritz-Gold, Carolyn J.
AU - Cooke, Roger
AU - Blumenthal, Donald K.
AU - Stull, James T.
N1 - Funding Information:
ACKNOWLEDGEMENTS: This work was supported by grants from the USPHS (HL-16683 for R.C.) and from the Muscular Dystrophy Association (J.T.S.), and by Training Grant/Awards (NIH HL 07192-01 for C.J.R.-G., and GM 02267 for D.K.B.). The authors wish to acknowledge the expert technical assistance of Ms. Kathleen Franks.
PY - 1980/3/13
Y1 - 1980/3/13
N2 - Using limited proteolysis by chymotrypsin or papain, we examined the effects of phosphorylation on the conformation of skeletal muscle myosin. In the absence of MgCl2, phosphorylation of the 19,000 dalton light chain (LC2) inhibited digestion of LC2 by chymotrypsin or papain. Phosphorylation also suppressed chymotryptic conversion of the heavy chain to subfragment 1 and increased its conversion to heavy meromyosin. These results indicate that phosphorylation alters the conformation of the N-terminal segment of LC2 and suggest that it also affects the heavy chain. In the presence of MgCl2, phosphorylation inhibited the chymotryptic digestion of LC2 but an effect on digestion of the heavy chain was not apparent. Thus, phosphorylation of LC2 alters LC2 conformation under physiological conditions.
AB - Using limited proteolysis by chymotrypsin or papain, we examined the effects of phosphorylation on the conformation of skeletal muscle myosin. In the absence of MgCl2, phosphorylation of the 19,000 dalton light chain (LC2) inhibited digestion of LC2 by chymotrypsin or papain. Phosphorylation also suppressed chymotryptic conversion of the heavy chain to subfragment 1 and increased its conversion to heavy meromyosin. These results indicate that phosphorylation alters the conformation of the N-terminal segment of LC2 and suggest that it also affects the heavy chain. In the presence of MgCl2, phosphorylation inhibited the chymotryptic digestion of LC2 but an effect on digestion of the heavy chain was not apparent. Thus, phosphorylation of LC2 alters LC2 conformation under physiological conditions.
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U2 - 10.1016/S0006-291X(80)80267-1
DO - 10.1016/S0006-291X(80)80267-1
M3 - Article
C2 - 6990926
AN - SCOPUS:0019153164
SN - 0006-291X
VL - 93
SP - 209
EP - 214
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 1
ER -