2011年5月
Interaction Sites of Tropomyosin in Muscle Thin Filament as Identified by Site-Directed Spin-Labeling
BIOPHYSICAL JOURNAL
- ,
- ,
- ,
- ,
- 巻
- 100
- 号
- 10
- 開始ページ
- 2432
- 終了ページ
- 2439
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1016/j.bpj.2011.03.021
- 出版者・発行元
- CELL PRESS
To identify interaction sites we measured the rotational motion of a spin label covalently bound to the side chain of a cysteine genetically incorporated into rabbit skeletal muscle tropomyosin (Tm) at positions 13, 36, 146, 160, 174, 190, 209, 230, 271, and 279. Upon the addition of F-actin, the mobility of all the spin labels, especially at position 13, 271, or 279, of Tm was inhibited significantly. Slow spin-label motion at the C-terminus (at the 230th and 271st residues) was observed upon addition of troponin. The binding of myosin-head Si fragments without troponin immobilized Tm residues at 146, 160, 190, 209, 230, 271, and 279, suggesting that these residues are involved in a direct interaction between Tm and actin in its open state. As immobilization occurred at substoichiometric amounts of Si binding to actin (a 1:7 molar ratio), the structural changes induced by Si binding to one actin subunit must have propagated and influenced interaction sites over seven actin subunits.
- リンク情報
-
- DOI
- https://doi.org/10.1016/j.bpj.2011.03.021
- CiNii Articles
- http://ci.nii.ac.jp/naid/120003726649
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/21575577
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000290830900014&DestApp=WOS_CPL
- ID情報
-
- DOI : 10.1016/j.bpj.2011.03.021
- ISSN : 0006-3495
- CiNii Articles ID : 120003726649
- PubMed ID : 21575577
- Web of Science ID : WOS:000290830900014