Conformational distributions and proximity relationships in the rigor complex of actin and myosin subfragment-1

M. Nyitrai, G. Hild, András Lukács, Emöke Bódis, B. Somogyi

Research output: Contribution to journalArticle

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Abstract

Cyclic conformational changes in the myosin head are considered essential for muscle contraction. We hereby show that the extension of the fluorescence resonance energy transfer method described originally by Taylor et al. (Taylor, D. L., Reidler, J,, Spudich, J. A., and Stryer, L. (1981) J. Cell Biol. 89, 362-367) allows determination of the position of a labeled point outside the actin filament in supramolecular complexes and also characterization of the conformational heterogeneity of an actin-binding protein while considering donor-acceptor distance distributions. Using this method we analyzed proximity relationships between two labeled points of S1 and the actin filament in the acto-S1 rigor complex. The donor (N- [[(iodoacetyl)amino]ethyl]-5-naphthylamine-1-sulfonate) was attached to either the catalytic domain (Cys-707) or the essential light chain (Cys-177) of S1, whereas the acceptor (5-(iodoacetamido)fluorescein) was attached to the actin filament (Cys-374). In contrast to the narrow positional distribution (assumed as being Gaussian) of Cys-707 (5 ± 3 Å), the positional distribution of Cys-177 was found to be broad (102 ± 4 Å). Such a broad positional distribution of the label on the essential light chain of S1 may be important in accommodating the helically arranged acto-myosin binding relative to the filament axis.

Original languageEnglish
Pages (from-to)2404-2409
Number of pages6
JournalJournal of Biological Chemistry
Volume275
Issue number4
DOIs
Publication statusPublished - Jan 28 2000

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pioglitazone
Myosin Subfragments
Myosins
Actin Cytoskeleton
Actins
1-Naphthylamine
Microfilament Proteins
Muscle
Light
Labels
Fluorescence Resonance Energy Transfer
Muscle Contraction
Catalytic Domain
actin subfragments

ASJC Scopus subject areas

  • Biochemistry

Cite this

Conformational distributions and proximity relationships in the rigor complex of actin and myosin subfragment-1. / Nyitrai, M.; Hild, G.; Lukács, András; Bódis, Emöke; Somogyi, B.

In: Journal of Biological Chemistry, Vol. 275, No. 4, 28.01.2000, p. 2404-2409.

Research output: Contribution to journalArticle

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