Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2049068 | FEBS Letters | 2010 | 6 Pages |
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.
Related Topics
Life Sciences
Agricultural and Biological Sciences
Plant Science
Authors
Ying Zhang, Akio Nakamura, Hozumi Kawamichi, Shinji Yoshiyama, Takeshi Katayama, Kazuhiro Kohama,