Calcium-dependent regulation of the motor activity of recombinant full-length Physarum myosin |
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Authors: | Zhang Ying Kawamichi Hozumi Tanaka Hideyuki Yoshiyama Shinji Kohama Kazuhiro Nakamura Akio |
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Affiliation: | Department of Molecular and Cellular Pharmacology, Gunma University Graduate School of Medicine, 3-39-22 Showa-Machi, Maebashi, Gunma, Japan. |
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Abstract: | We successfully synthesized full-length and the mutant Physarum myosin and heavy meromyosin (HMM) constructs associated with Physarum regulatory light chain and essential light chain (PhELC) using Physarum myosin heavy chain in Sf-9 cells, and examined their Ca(2+)-mediated regulation. Ca(2+) inhibited the motility and ATPase activities of Physarum myosin and HMM. The Ca(2+) effect is also reversible at the in vitro motility of Physarum myosin. We demonstrated that full-length myosin increases the Ca(2+) inhibition more effectively than HMM. Furthermore, Ca(2+) did not affect the motility and ATPase activities of the mutant Physarum myosin with PhELC that lost Ca(2+)-binding ability. Therefore, we conclude that PhELC plays a critical role in Ca(2+)-dependent regulation of Physarum myosin. |
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