Studies on the F-actin · tropomyosin · troponin complex II. Partial reconstitution of thin filament by F-actin, tropomyosin and the tropomyosin binding component of troponin (TN-T)

Shin'ichi Ishiwata, Hiroshi Kondo

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

It was found that thin filaments are reconstituted from F-actin, tropomyosin and the tropomyosin binding component of troponin (TN-T) in vitro according to a self-assembly mechanism. Although a gel structure is formed when the three proteins are mixed in the order F-actin, TN-T and tropomyosin, it is in a metastable state and spontaneously transforms to dispersed filaments in an equilibrium state. The rate of the transformation is largely dependent on temperature. When the mixing order of TN-T and tropomyosin is reversed, large amounts of the complex appear immediately in the dispersed filament form. Dependence on the order of mixing is observed only when the molar ratio of TN-T to tropomyosin is about one, i.e. at the physiological ratio. When the molar ratio of TN-T to tropomyosin is either above or below one, a stable gel form or a stable dispersed filament form was, respectively, obtained independently of the mixing order of the three proteins.

Original languageEnglish
Pages (from-to)341-349
Number of pages9
JournalBBA - Protein Structure
Volume534
Issue number2
DOIs
Publication statusPublished - 1978 Jun 21
Externally publishedYes

Fingerprint

Tropomyosin
Troponin T
Troponin
Actins
Gels
Self assembly
troponin-tropomyosin complex
Proteins
Temperature

ASJC Scopus subject areas

  • Medicine(all)

Cite this

Studies on the F-actin · tropomyosin · troponin complex II. Partial reconstitution of thin filament by F-actin, tropomyosin and the tropomyosin binding component of troponin (TN-T). / Ishiwata, Shin'ichi; Kondo, Hiroshi.

In: BBA - Protein Structure, Vol. 534, No. 2, 21.06.1978, p. 341-349.

Research output: Contribution to journalArticle

@article{d32e66c6d2284d54af7bcee1b38603e5,
title = "Studies on the F-actin · tropomyosin · troponin complex II. Partial reconstitution of thin filament by F-actin, tropomyosin and the tropomyosin binding component of troponin (TN-T)",
abstract = "It was found that thin filaments are reconstituted from F-actin, tropomyosin and the tropomyosin binding component of troponin (TN-T) in vitro according to a self-assembly mechanism. Although a gel structure is formed when the three proteins are mixed in the order F-actin, TN-T and tropomyosin, it is in a metastable state and spontaneously transforms to dispersed filaments in an equilibrium state. The rate of the transformation is largely dependent on temperature. When the mixing order of TN-T and tropomyosin is reversed, large amounts of the complex appear immediately in the dispersed filament form. Dependence on the order of mixing is observed only when the molar ratio of TN-T to tropomyosin is about one, i.e. at the physiological ratio. When the molar ratio of TN-T to tropomyosin is either above or below one, a stable gel form or a stable dispersed filament form was, respectively, obtained independently of the mixing order of the three proteins.",
author = "Shin'ichi Ishiwata and Hiroshi Kondo",
year = "1978",
month = "6",
day = "21",
doi = "10.1016/0005-2795(78)90017-X",
language = "English",
volume = "534",
pages = "341--349",
journal = "Biochimica et Biophysica Acta - Proteins and Proteomics",
issn = "1570-9639",
publisher = "Elsevier",
number = "2",

}

TY - JOUR

T1 - Studies on the F-actin · tropomyosin · troponin complex II. Partial reconstitution of thin filament by F-actin, tropomyosin and the tropomyosin binding component of troponin (TN-T)

AU - Ishiwata, Shin'ichi

AU - Kondo, Hiroshi

PY - 1978/6/21

Y1 - 1978/6/21

N2 - It was found that thin filaments are reconstituted from F-actin, tropomyosin and the tropomyosin binding component of troponin (TN-T) in vitro according to a self-assembly mechanism. Although a gel structure is formed when the three proteins are mixed in the order F-actin, TN-T and tropomyosin, it is in a metastable state and spontaneously transforms to dispersed filaments in an equilibrium state. The rate of the transformation is largely dependent on temperature. When the mixing order of TN-T and tropomyosin is reversed, large amounts of the complex appear immediately in the dispersed filament form. Dependence on the order of mixing is observed only when the molar ratio of TN-T to tropomyosin is about one, i.e. at the physiological ratio. When the molar ratio of TN-T to tropomyosin is either above or below one, a stable gel form or a stable dispersed filament form was, respectively, obtained independently of the mixing order of the three proteins.

AB - It was found that thin filaments are reconstituted from F-actin, tropomyosin and the tropomyosin binding component of troponin (TN-T) in vitro according to a self-assembly mechanism. Although a gel structure is formed when the three proteins are mixed in the order F-actin, TN-T and tropomyosin, it is in a metastable state and spontaneously transforms to dispersed filaments in an equilibrium state. The rate of the transformation is largely dependent on temperature. When the mixing order of TN-T and tropomyosin is reversed, large amounts of the complex appear immediately in the dispersed filament form. Dependence on the order of mixing is observed only when the molar ratio of TN-T to tropomyosin is about one, i.e. at the physiological ratio. When the molar ratio of TN-T to tropomyosin is either above or below one, a stable gel form or a stable dispersed filament form was, respectively, obtained independently of the mixing order of the three proteins.

UR - http://www.scopus.com/inward/record.url?scp=0017805766&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0017805766&partnerID=8YFLogxK

U2 - 10.1016/0005-2795(78)90017-X

DO - 10.1016/0005-2795(78)90017-X

M3 - Article

VL - 534

SP - 341

EP - 349

JO - Biochimica et Biophysica Acta - Proteins and Proteomics

JF - Biochimica et Biophysica Acta - Proteins and Proteomics

SN - 1570-9639

IS - 2

ER -