Conformation and activity of smooth muscle myosin probed by various essential light chains.

Conformation and activity of smooth muscle myosin probed by various essential light chains. Research Abstract Details 

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Conformation and activity of smooth muscle myosin probed by various essential light chains. Abstract Text:

T Katoh,F Morita,

Porcine aorta smooth muscle myosin contains two essential light chain (LC17) isoforms and the light chain was replaced with one of the LC17 isoforms, rabbit skeletal muscle myosin alkali light chain 2 (A2), or scallop striated muscle myosin essential light chain (SHLC). The myosin containing either an LC17 isoform or A2 showed phosphorylation-dependent properties in the monomer conformation, filament formation, ATPase activities, and superprecipitation, behaving in essentially the same way as native myosin. On the other hand, the replacement of LC17 with SHLC destabilized the 10S conformation and the myosin was predominantly filamentous under physiological conditions, irrespective of the phosphorylation state. This myosin containing dephosphorylated regulatory light chain showed higher actin-activated ATPase activity than native dephosphorylated myosin and was further activated by Ca2+, resulting in a decrease of phosphorylation-dependent regulation. Superprecipitation for the myosin was observed only when the regulatory light chain was phosphorylated. Superprecipitation for myosin containing SHLC was significantly slow in the absence of Ca2+ in comparison with that for myosin containing LC17, and was further activated by the presence of Ca2+. On the basis of the differences in amino acid sequences of these essential light chains, it appears that the N-terminal domain of LC17 may be implicated in these phosphorylation-dependent properties of smooth muscle myosin.

Conformation and activity of smooth muscle myosin probed by various essential light chains. Publishing Authors By Initials

T Katoh,F Morita,

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

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Conformation and activity of smooth muscle myosin probed by various essential light chains. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 121

Page Numbers: 56-62

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Jan

YEAR: 1997

Conformation and activity of smooth muscle myosin probed by various essential light chains. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Conformation and activity of smooth muscle myosin probed by various essential light chains. Keywords Mesh Terms:

KEYWORDS: Swine

MESH TERMS: metabolism

Chemical & Substance for Abstract: Conformation and activity of smooth muscle myosin probed by various essential light chains. Information

Substance Name: Myosins

Registry Number: EC 3.6.1.4

Grant and Affiliation Information for Conformation and activity of smooth muscle myosin probed by various essential light chains.

AFFILIATION: Division of Chemistry, Graduate School of Science, Hokkaido University, Sapporo.

Country: JAPAN

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MEDLINETA: J Biochem

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