Probes bound to myosin Cys-707 rotate during length transients in contraction.
It is widely conjectured that muscle shortens because portions of myosin molecules (the "cross-bridges") impel the actin filament to which they transiently attach and that the impulses result from rotation of the cross-bridges. Crystallography indicates that a cross-bridge is articulated-consisting of a globular catalytic/actin-binding domain and a long lever arm that may rotate. Conveniently, a rhodamine probe with detectable attitude can be attached between the globular domain and the lever arm, enabling the observer to tell whether the anchoring region rotates. Well-established signature effects observed in shortening are tension changes resulting from the sudden release or quick stretch of active muscle fibers. In this investigation we found that closely correlated with such tension changes are changes in the attitude of the rhodamine probes. This correlation strongly supports the conjecture about how shortening is achieved.
Burghardt
T P
TP
Department of Biochemistry and Molecular Biology, Mayo Foundation, 200 First Street South West, Rochester, MN 55905, USA. burghardt@mayo.edu
Garamszegi
S P
SP
Ajtai
K
K
D000199:Actins / Q000737:chemistry; D000818:Animals; D001665:Binding Sites; D018360:Crystallography, X-Ray; D003545:Cysteine; D005456:Fluorescent Dyes; D009119:Muscle Contraction; D009218:Myosins / Q000737:chemistry*; D011487:Protein Conformation; D011817:Rabbits; D012235:Rhodamines
D000199:Actins; D005456:Fluorescent Dyes; D012235:Rhodamines; D009218:Myosins; D003545:Cysteine