2006年2月
Troponin is a potential regulator for actomyosin interactions
JOURNAL OF BIOCHEMISTRY
- ,
- 巻
- 139
- 号
- 2
- 開始ページ
- 289
- 終了ページ
- 293
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1093/jb/mvj030
- 出版者・発行元
- JAPANESE BIOCHEMICAL SOC
Troponin extracted from rabbit skeletal muscle directly binds to an actin filament in a molar ratio of 1:1 even in the absence of tropomyosin. An actin filament decorated with troponin did not exhibit significant difference from pure actin filaments in the maximum rate of actomyosin ATP hydrolysis and the sliding velocity of the filament examined by means of an in vitro motility assay. However, the relative number of troponin-bound actin filaments moving in the absence of calcium ions decreased to half that in their presence. The amount of HMM bound to the filaments was less than 4% of actin monomers in the presence of TNs. In addition, actin filaments could not move when Tn molecules were bound in the molar ratio of about 1:1 although they sufficiently bind to myosin heads. These results indicate that troponin can transform an actin monomer within a filament into an Off-state without sterically blocking of the myosin-binding sites with tropomyosin molecules.
- リンク情報
- ID情報
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- DOI : 10.1093/jb/mvj030
- ISSN : 0021-924X
- Web of Science ID : WOS:000235452100016