Regulatory light-chain Cys-55 sites on the two heads of myosin can come within 2A of each other.
The di-thiol reagent, 5,5'-dithiobis (2-nitrobenzoic acid) is shown to induce disulfide bond formation between Mercenaria regulatory light-chain Cys-55 sites on either head of scallop hybrid myosin. This indicates that these two sites on opposite heads of myosin can come within 2A of each other and this confirms a prediction based on earlier data [Chantler, Tao and Stafford (1991) Biophys. J. 59, 1242-1250]. Results demonstrate that myosin heads in solution show a considerable mutual freedom of movement which can be monitored by probes in the vicinity of regulatory light-chain residue 55. Implications for light-chain movement on the myosin head are discussed.
Bower
S M
SM
Department of Anatomy and Neurobiology, Medical College of Pennsylvania, Philadelphia 19129.
Wang
Y
Y
Chantler
P D
PD
D000818:Animals; D003545:Cysteine / Q000737:chemistry*; D004228:Dithionitrobenzoic Acid / Q000737:chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D008974:Mollusca / Q000737:chemistry; D009218:Myosins / Q000737:chemistry*; D011487:Protein Conformation
D004228:Dithionitrobenzoic Acid; D009218:Myosins; D003545:Cysteine