Conformation, filament assembly, and activity of single-headed smooth muscle myosin.

Conformation, filament assembly, and activity of single-headed smooth muscle myosin. Research Abstract Details 

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Conformation, filament assembly, and activity of single-headed smooth muscle myosin. Abstract Text:

K Konishi,T Katoh,F Morita,M Yazawa,

Single-headed myosin was prepared by digestion of porcine aorta smooth muscle myosin with Staphylococcus aureus V8 protease in the presence of actin. The single-headed myosin preparation contained intact light chains, a rod fragment of a heavy chain, and a heavy chain of which only a minor fraction contained a nick in the head segment. Below 0.2 M NaCl, the single-headed myosin showed a decrease in Ca2+-ATPase activity and an increase in the elution time on gel filtration HPLC in a phosphorylation-dependent manner, indicating a phosphorylation-dependent conformational transition between the extended and folded forms. These conformations were confirmed by electron microscopic observation of rotary-shadowed samples of single-headed myosin. However, the conformational transition of single-headed myosin occurred in a narrower range with lower salt concentrations than that of double-headed myosin. The filament assembly of single-headed myosin was thus facilitated and phosphorylation-independent. The single-headed myosin also showed high actin-activated ATPase activity independent of phosphorylation. These results indicate that the two-headed structure of smooth muscle myosin is not essential for the conformational transition, but is required for the phosphorylation-dependent regulation of enzymatic activity and filament assembly.

Conformation, filament assembly, and activity of single-headed smooth muscle myosin. Publishing Authors By Initials

K Konishi,T Katoh,F Morita,M Yazawa,

For similar animals: chordata: vertebrates: mammals: artiodactyla: swine research abstracts see: animals: chordata: vertebrates: mammals: artiodactyla: swine research

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Conformation, filament assembly, and activity of single-headed smooth muscle myosin. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 124

Page Numbers: 163-70

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Jul

YEAR: 1998

Conformation, filament assembly, and activity of single-headed smooth muscle myosin. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Conformation, filament assembly, and activity of single-headed smooth muscle myosin. Keywords Mesh Terms:

KEYWORDS: Swine

MESH TERMS: metabolism

Chemical & Substance for Abstract: Conformation, filament assembly, and activity of single-headed smooth muscle myosin. Information

Substance Name: Myosins

Registry Number: EC 3.6.1.4

Grant and Affiliation Information for Conformation, filament assembly, and activity of single-headed smooth muscle myosin.

AFFILIATION: Division of Chemistry, Graduate School of Science, Hokkaido University, Kita-ku, Sapporo, 060-0810, Japan.

Country: JAPAN

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MEDLINETA: J Biochem

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