Tissue-specific interactions of TNI isoforms with other TN subunits and tropomyosins in C. elegans: The role of the C- and N-terminal extensions

Md Ziaul Amin, Tetsuya Bando, Razia Ruksana, Frederick Anokye-Danso, Yasuo Takashima, Yasuji Sakube, Hiroaki Kagawa

Research output: Contribution to journalArticle

5 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)456-465
Number of pages10
JournalBiochimica et Biophysica Acta - Proteins and Proteomics
Volume1774
Issue number4
DOIs
Publication statusPublished - Apr 2007

Keywords

  • C-terminal extension
  • Caenorhabditis elegans
  • Tropomyosin
  • Troponin C
  • Troponin I
  • Troponin T

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biophysics
  • Biochemistry
  • Molecular Biology

Fingerprint Dive into the research topics of 'Tissue-specific interactions of TNI isoforms with other TN subunits and tropomyosins in C. elegans: The role of the C- and N-terminal extensions'. Together they form a unique fingerprint.

  • Cite this