Mapping myosin-binding sites on actin probed by peptides that inhibit actomyosin interaction.

Mapping myosin-binding sites on actin probed by peptides that inhibit actomyosin interaction. Research Abstract Details 

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Mapping myosin-binding sites on actin probed by peptides that inhibit actomyosin interaction. Abstract Text:

T Katoh,F Morita,

A 2-kDa peptide (2K peptide) which was derived from the neck region of porcine aorta smooth muscle myosin heavy chain binds to actin competitively with skeletal myosin subfragment 1 (S1) in the absence of ATP and inhibits acto-S1 ATPase activity [Katoh, T. and Morita, F. (1993) J. Biol. Chem. 268, 2380-2388]. Using this and other peptides, myosin-binding sites on actin were mapped and their functions were studied. The 2K peptide inhibited the acto-S1 ATPase activity without inhibiting the binding of S1 to actin in the presence of ATP. On the other hand, the dansylated 2K peptide (DNS-2K peptide) inhibited not only the acto-S1 ATPase activity but also the binding of S1 to actin in the presence of ATP. Then, DNS-2K peptide was crosslinked to actin with 1-ethyl-3[3-(dimethylamino)propyl] carbodiimide. Amino acid composition and sequencing analyses of the fluorescent lysylendopeptidase-peptides of the crosslinked product indicated that DNS-2K peptide was crosslinked to acidic residues within residues 1-18 (Asp1, Glu2, Asp3, Glu4, and/or Asp11), 19-50 (Asp25), and 85-113 (Glu99 or Glu100) of actin. A competition experiment for the crosslinking with unlabeled 2K peptide showed that the crosslinking to residues 85-113 of actin was specific for DNS-2K peptide. In addition, isolated actin peptide 85-113 was found to show the competitive inhibition of actin-activated ATPase activity of S1 with respect to actin. These results suggest that the site within residues 1-28 of actin participates in the actin-activation of myosin ATPase activity, and the site within residues 85-113 of actin participates in the weak binding of myosin to actin in the presence of ATP.

Mapping myosin-binding sites on actin probed by peptides that inhibit actomyosin interaction. Publishing Authors By Initials

T Katoh,F Morita,

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

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Mapping myosin-binding sites on actin probed by peptides that inhibit actomyosin interaction. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 120

Page Numbers: 580-6

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Sep

YEAR: 1996

Mapping myosin-binding sites on actin probed by peptides that inhibit actomyosin interaction. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Mapping myosin-binding sites on actin probed by peptides that inhibit actomyosin interaction. Keywords Mesh Terms:

KEYWORDS: Rabbits

MESH TERMS: chemistry

Chemical & Substance for Abstract: Mapping myosin-binding sites on actin probed by peptides that inhibit actomyosin interaction. Information

Substance Name: Myosins

Registry Number: EC 3.6.1.4

Grant and Affiliation Information for Mapping myosin-binding sites on actin probed by peptides that inhibit actomyosin interaction.

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

Country: JAPAN

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MEDLINETA: J Biochem

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