Troponin is a potential regulator for actomyosin interactions

Hiroaki Mizuno, Hajime Honda

    Research output: Contribution to journalArticlepeer-review

    3 Citations (Scopus)

    Abstract

    Troponin extracted from rabbit skeletal muscle directly binds to an actin filament in a molar ratio of 1:1 even in the absence of tropomyosin. An actin filament decorated with troponin did not exhibit significant difference from pure actin filaments in the maximum rate of actomyosin ATP hydrolysis and the sliding velocity of the filament examined by means of an in vitro motility assay. However, the relative number of troponin-bound actin filaments moving in the absence of calcium ions decreased to half that in their presence. The amount of HMM bound to the filaments was less than 4% of actin monomers in the presence of TNs. In addition, actin filaments could not move when Tn molecules were bound in the molar ratio of about 1:1 although they sufficiently bind to myosin heads. These results indicate that troponin can transform an actin monomer within a filament into an Off-state without sterically blocking of the myosin-binding sites with tropomyosin molecules.

    Original languageEnglish
    Pages (from-to)289-293
    Number of pages5
    JournalJournal of biochemistry
    Volume139
    Issue number2
    DOIs
    Publication statusPublished - 2006 Feb

    Keywords

    • ATPase
    • Actin filament
    • Motility
    • Sliding
    • Troponin

    ASJC Scopus subject areas

    • Biochemistry
    • Molecular Biology

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