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J Biol Chem, Vol. 273, Issue 28, 17702-17707, July 10, 1998
From the Department of Physiology, University of Massachusetts
Medical Center, Worcester, Massachusetts 01655, the
§ Muscle Research Group, Boston Biomedical Research
Institute, Boston, Massachusetts 02114, and the ¶ Institute of
Medical Sciences, University of Tokyo, Minato-ku, Tokyo 108, Japan
The motor function of smooth muscle myosin is
activated by phosphorylation of the regulatory light chain (RLC) at
Ser19. However, the molecular mechanism by which the
phosphorylation activates the motor function is not yet understood. In
the present study, we focused our attention on the role of the central
helix of RLC for regulation. The flexible region at the middle of the central helix (Gly95-Pro98) was substituted or
deleted to various extents, and the effects of the deletion or
substitution on the regulation of the motor activity of myosin were
examined. Deletion of Gly95-Asp97,
Gly95-Thr96, or
Thr96-Asp97 decreased the actin-translocating
activity of myosin a little, but the
phosphorylation-dependent regulation of the motor activity was not disrupted. In contrast, the deletion of
Gly95-Pro98 of RLC completely abolished the
actin translocating activity of phosphorylated myosin. However, the
unregulated myosin long subfragment 1 containing this RLC mutant showed
motor activity the same as that containing the wild type RLC. Since
long subfragment 1 motor activity is unregulated by phosphorylation,
i.e. constitutively active, these results suggest that the
deletion of these residues at the central helix of RLC disrupts the
phosphorylation-mediated activation mechanism but not the motor
function of myosin itself. On the other hand, the elimination of
Pro98 or substitution of
Gly95-Pro98 by Ala resulted in the activation
of actin translocating activity of dephosphorylated myosin, whereas it
did not affect the motor activity of phosphorylated myosin. Together,
these results clearly indicate the importance of the hinge at the
central helix of RLC on the phosphorylation-mediated regulation of
smooth muscle myosin.
A Hinge at the Central Helix of the Regulatory Light Chain of
Myosin Is Critical for Phosphorylation-dependent
Regulation of Smooth Muscle Myosin Motor Activity
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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