2005 Fiscal Year Final Research Report Summary
Detailed analysis of the ATPase activity of Chara myosin
| Project/Area Number |
16570153
|
|---|
| Research Category |
Grant-in-Aid for Scientific Research (C)
|
| Allocation Type | Single-year Grants |
|---|
| Section | 一般 |
|---|
| Research Field |
Cell biology
|
|---|
| Research Institution | Chiba University |
|---|
Principal Investigator |
YAMAMOTO Keiichi Chiba University, Faculty of Science, Professor, 理学部, 教授 (70053361)
|
|---|
| Co-Investigator(Kenkyū-buntansha) |
ITO Kohji Chiba University, Faculty of Science, Research Associate, 理学部, 助手 (50302526)
|
|---|
| Project Period (FY) |
2004 – 2005
|
| Keywords | myosin / motor protein / ATP hydrolysis / stopped flow / cytoplasmic streaming |
|---|
| Research Abstract |
Chara corallina myosin is the fastest molecular motor protein known so far. To investigate the molecular mechanism of the fast movement, we determined the time of the strongly bound state with actin by measuring transient kinetic parameters of a recombinant motor domain construct of Chara myosin. The rate constant of ADP dissociation from acto-motor domain was 1,920 s^<-1>. The rate constant of ATP-induced dissociation of the motor domain from actin was 4.0 μM^<-1> s^<-1> at 25℃, which leads to an estimate of the rate constant of 6,000 s^<-1> at physiological ATP concentration. From these data, the time spent in the strongly bound state with actin was estimated to be 0.69 ms. This value is the shortest among known values for various myosins. This short strongly bound state most likely accounts for the fast motility.
|
-
-
-
-
-
[Book] 分子細胞生物学 第5版2005
Author(s)
石浦章一, 石川 統, 須藤和夫, 野田春彦, 丸山工作, 山本啓一共訳
Total Pages
918
Publisher
東京化学同人
Description
「研究成果報告書概要(和文)」より
