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ID 32969
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Author
Amin, Md. Ziaul
Bando, Tetsuya
Ruksana, Razia
Anokye-Danso, Frederick
Takashima, Yasuo
Sakube, Yasuji
Kagawa, Hiroaki
Abstract
The aim of this study is to investigate the function of the C-terminal extension of three troponin I isoforms, that are unique to the body wall muscles of Caenorhabditis elegans and to understand the molecular interactions within the TN complex between troponin I with troponin C/T, and tropomyosin. We constructed several expression vectors to generate recombinant proteins of three body wall and one pharyngeal troponin I isoforms in Escherichia coli. Protein overlay assays and Western blot analyses were performed using antibodies. We demonstrated that pharyngeal TNI-4 interacted with only the pharyngeal isoforms of troponin C/T and tropomyosin. In contrast, the body wall TNI-2 bound both the body wall and pharyngeal isoforms of these components. Similar to other invertebrates, the N-terminus of troponin I contributes to interactions with troponin C. Full-length troponin I was essential for interactions with tropomyosin isoforms. Deletion of the C-terminal extension had no direct effect on the binding of the body wall troponin I to other muscle thin filament troponin C/T and tropomyosin isoforms.
Keywords
Troponin I
Caenorhabditis elegans
Troponin T
Troponin C
Tropomyosin
C-terminal extension
Note
Published with permission from the copyright holder. This is a author's copy,as published in Biochimica Biophysica et Acta, April 2007, volume 1774, issue 4, pp456-465.
Publisher URL: http://dx.doi.org/10.1016/j.bbapap.2007.01.003
Copyright © 2007 Elsevier B. V. All rights reserved.
Published Date
2007-04
Publication Title
Biochimica et Biophysica Acta. Proteins and Proteomics
Volume
volume1774
Issue
issue4
Publisher
Elsevier B.V.
Start Page
456
End Page
465
ISSN
1570-9639
NCID
AA11685085
Content Type
Journal Article
language
英語
Copyright Holders
Elsevier B.V.
File Version
author
Refereed
True
DOI
PubMed ID
Web of Sience KeyUT
Submission Path
biology_general/35