Filamentous Aggregates of Native Titin and Binding of C-protein and AMP-deaminase

Jane F. Koretz, Thomas C. Irving, Kuan Wang

Research output: Contribution to journalArticle

37 Citations (Scopus)

Abstract

In solutions of high ionic strength, native titin-2, a large extractable fragment of the sarcomere matrix protein titin, appears as extremely long, flexible, and slender beaded strings. We report here that in solutions of lower ionic strength near neutral pH, titin-2 assembles into higher-order aggregates with surface projections. Solid phase binding assays show that two myosin-binding proteins, C-protein and AMP-deaminase, are also titin-binding proteins. Both proteins decorate titin aggregates, producing filaments of more uniform appearance. Numerical Fourier transforms of these decorated aggregates show ˜ 12-nm periodicities. The interaction of titin with myosin-associated proteins such as C-protein may take part in the anchoring mechanism that prevents the stretching and extension of titin filaments in the A band.

Original languageEnglish
Pages (from-to)305-309
Number of pages5
JournalArchives of Biochemistry and Biophysics
Volume304
Issue number2
DOIs
Publication statusPublished - 1993
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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