Inhibition of acto-myosin subfragment-1 ATPase activity by peptides corresponding to various segments of the 20-kDa domain of myosin heavy chain.

Inhibition of acto-myosin subfragment-1 ATPase activity by peptides corresponding to various segments of the 20-kDa domain of myosin heavy chain. Research Abstract Details 

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Inhibition of acto-myosin subfragment-1 ATPase activity by peptides corresponding to various segments of the 20-kDa domain of myosin heavy chain. Abstract Text:

M Eto,K Isonishi,Y Fukui,F Morita,N Nishi,S Tokura,

As reported previously, the synthetic heptapeptide having the amino acid sequence around the reactive Cys (SH1) of myosin heavy chain, IRICRKG-NH2, inhibited acto-myosin subfragment-1 (S-1) ATPase activity and half inhibition (K1/2) was observed at a peptide concentration of 0.06 mM. The inhibitory ability of the peptide was found to be decreased to one-fifth by acetylation of its N-terminal alpha-amino group. A similar effect of N-acetylation was observed with a nonapeptide, EGIRICRKG-NH2, and an undecapeptide, VLEGIRICRKG-NH2. These results indicate that N-terminal-free synthetic peptides do not act as proper analogs of the corresponding segment of S-1 heavy chain against F-actin. We isolated a longer peptide extending from Thr682 to Lys709 in S-1 heavy chain, with two Cys residues corresponding to SH1 and SH2. This peptide, having 28 residues (28peptide), inhibited acto-S-1 ATPase activity with a K1/2 of 0.23 mM. A cosedimentation binding assay indicated that the 28peptide completely dissociated acto-S-1 in the presence of ATP. This behavior is different from that observed with the N-terminal-free synthetic heptapeptide, and thus the 28peptide might be an analog of the corresponding segment. There is a possibility that the region corresponding to the 28peptide in S-1 heavy chain may bind directly with F-actin and may be involved in determining the acto-S-1 link during the steady state of the acto-S-1 ATPase reaction.

Inhibition of acto-myosin subfragment-1 ATPase activity by peptides corresponding to various segments of the 20-kDa domain of myosin heavy chain. Publishing Authors By Initials

M Eto,K Isonishi,Y Fukui,F Morita,N Nishi,S Tokura,

For similar animals: chordata: vertebrates: mammals: lagomorpha: rabbits research abstracts see: animals: chordata: vertebrates: mammals: lagomorpha: rabbits research

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Inhibition of acto-myosin subfragment-1 ATPase activity by peptides corresponding to various segments of the 20-kDa domain of myosin heavy chain. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 115

Page Numbers: 701-7

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Apr

YEAR: 1994

Inhibition of acto-myosin subfragment-1 ATPase activity by peptides corresponding to various segments of the 20-kDa domain of myosin heavy chain. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Inhibition of acto-myosin subfragment-1 ATPase activity by peptides corresponding to various segments of the 20-kDa domain of myosin heavy chain. Keywords Mesh Terms:

KEYWORDS: Rabbits

MESH TERMS: chemistry

Chemical & Substance for Abstract: Inhibition of acto-myosin subfragment-1 ATPase activity by peptides corresponding to various segments of the 20-kDa domain of myosin heavy chain. Information

Substance Name: Myosins

Registry Number: EC 3.6.1.4

Grant and Affiliation Information for Inhibition of acto-myosin subfragment-1 ATPase activity by peptides corresponding to various segments of the 20-kDa domain of myosin heavy chain.

AFFILIATION: Department of Chemistry, Faculty of Science, Hokkaido University.

Country: JAPAN

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MEDLINETA: J Biochem

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