| Literature DB >> 20633559 |
Ying Zhang1, Akio Nakamura, Hozumi Kawamichi, Shinji Yoshiyama, Takeshi Katayama, Kazuhiro Kohama.
Abstract
To examine the role of two light chains (LCs) of the myosin II on Ca2+ regulation, we produced hybrid heavy meromyosin (HMM) having LCs from Physarum and/or scallop myosin using the smooth muscle myosin heavy chain. Ca2+ inhibited motility and ATPase activity of hybrid HMMs with LCs from Physarum myosin but activated those of hybrid HMM with LCs from scallop myosin, indicating an active role of LCs. ATPase activity of hybrid HMMs with LCs from different species showed the same effect by Ca2+ even though they did not support motility. Our results suggest that communication between the original combinations of LC is important for the motor function. Copyright (c) 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.Entities:
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Year: 2010 PMID: 20633559 DOI: 10.1016/j.febslet.2010.07.011
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124