A Three-Dimensional FRET Analysis to Construct an Atomic Model of the Actin–Tropomyosin–Troponin Core Domain Complex on a Muscle Thin Filament

Material type: 文書・図像類

Author: MIKI, Masaoほか

Publisher: ELSEVIR

Publication date: 2012-03

Material Format: Digital

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Note (General)：: It is essential to knowthe detailed structure of the thin filament to understand the regulation mechanism of striated muscle contraction. Fluorescence...

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Material Type: 文書・図像類
Title: A Three-Dimensional FRET Analysis to Construct an Atomic Model of the Actin–Tropomyosin–Troponin Core Domain Complex on a Muscle Thin Filament
Author/Editor: MIKI, Masao
MAKIMURA, Satoshi
SUGAHARA, Yasuyuki
YAMADA, Ryuta
BUNYA, Masashi
SAITOH, Takahiro
TOBITA, Hidetaka
Author Heading: MIKI, Masao
MAKIMURA, Satoshi
SUGAHARA, Yasuyuki
YAMADA, Ryuta
BUNYA, Masashi
SAITOH, Takahiro
TOBITA, Hidetaka
Publication, Distribution, etc.: ELSEVIR
Publication Date: 2012-03
Publication Date (W3CDTF): 2012-03
Periodical title: Journal of Molecular Biology
No. or year of volume/issue: 420 1-2
Volume: 420
Issue: 1-2
Pages: 40-55
Text Language Code: eng
Target Audience: 一般
Note (General): It is essential to knowthe detailed structure of the thin filament to understand the regulation mechanism of striated muscle contraction. Fluorescence resonance energy transfer (FRET) was used to construct an atomic model of the actin–tropomyosin (Tm)–troponin (Tn) core domain complex. We generated single-cysteine mutants in the 167–195 region of Tm and in TnC, TnI, and the β-TnT 25-kDa fragment, and each was attached with an energy donor probe. An energy acceptor probe was located at actin Gln41, actin Cys374, or the actin nucleotide-binding site. From these donor–acceptor pairs, FRET efficiencies were determined with and without Ca2+. Using the atomic coordinates for F-actin, Tm, and the Tn core domain, we searched all possible arrangements for Tm or the Tn core domain on F-actin to calculate the FRET efficiency for each donor–acceptor pair in each arrangement. By minimizing the squared sum of deviations for the calculated FRET efficiencies from the observed FRET efficiencies, we determined the location of Tm segment 167– 195 and the Tn core domain on F-actin with andwithout Ca2+. The bulk of the Tn core domain is located near actin subdomains 3 and 4. The central helix of TnC is nearly perpendicular to the F-actin axis, directing the N-terminal domain of TnC toward the actin outer domain. The C-terminal region in the I–T arm forms a four-helix-bundle structure with the Tm 175–185 region. After Ca2+ release, the Tn core domainmoves toward the actin outer domain and closer to the center of the F-actin axis.
Access Restrictions: 限定公開
Data Provider (Database): 国立情報学研究所 : 学術機関リポジトリデータベース（IRDB）（機関リポジトリ）
https://irdb.nii.ac.jp
Original Data Provider (Database): 福井大学 : 福井大学学術機関リポジトリ