Tropomyosin Inhibits the Rate of Actin Polymerization by Stabilizing Actin Filaments

Sarah E. Hitchcock-DeGregori; Prakash Sampath; Thomas D. Pollard

doi:10.1021/bi00426a016

Tropomyosin Inhibits the Rate of Actin Polymerization by Stabilizing Actin Filaments

Sarah E. Hitchcock-DeGregori, Prakash Sampath, Thomas D. Pollard

Robert Wood Johnson Medical School (RWJMS), Pathology

Research output: Contribution to journal › Article › peer-review

60 Scopus citations

Abstract

Tropomyosin inhibition of the rate of spontaneous polymerization of actin is associated with binding of tropomyosin to actin filaments. Rate constants determined by using a direct electron microscopic assay of elongation showed that αα- and αβ-tropomyosin have a small or no effect on the rate of elongation at either end of the filaments. The most likely explanation for the inhibition of the rate of polymerization of actin in bulk samples is that tropomyosin reduces the number of filament ends by mechanical stabilization of the filaments.

Original language	English (US)
Pages (from-to)	9182-9185
Number of pages	4
Journal	Biochemistry
Volume	27
Issue number	26
DOIs	https://doi.org/10.1021/bi00426a016
State	Published - Dec 1 1988

All Science Journal Classification (ASJC) codes

Biochemistry

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10.1021/bi00426a016

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abstract = "Tropomyosin inhibition of the rate of spontaneous polymerization of actin is associated with binding of tropomyosin to actin filaments. Rate constants determined by using a direct electron microscopic assay of elongation showed that αα- and αβ-tropomyosin have a small or no effect on the rate of elongation at either end of the filaments. The most likely explanation for the inhibition of the rate of polymerization of actin in bulk samples is that tropomyosin reduces the number of filament ends by mechanical stabilization of the filaments.",

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year = "1988",

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T1 - Tropomyosin Inhibits the Rate of Actin Polymerization by Stabilizing Actin Filaments

AU - Hitchcock-DeGregori, Sarah E.

AU - Sampath, Prakash

AU - Pollard, Thomas D.

PY - 1988/12/1

Y1 - 1988/12/1

N2 - Tropomyosin inhibition of the rate of spontaneous polymerization of actin is associated with binding of tropomyosin to actin filaments. Rate constants determined by using a direct electron microscopic assay of elongation showed that αα- and αβ-tropomyosin have a small or no effect on the rate of elongation at either end of the filaments. The most likely explanation for the inhibition of the rate of polymerization of actin in bulk samples is that tropomyosin reduces the number of filament ends by mechanical stabilization of the filaments.

AB - Tropomyosin inhibition of the rate of spontaneous polymerization of actin is associated with binding of tropomyosin to actin filaments. Rate constants determined by using a direct electron microscopic assay of elongation showed that αα- and αβ-tropomyosin have a small or no effect on the rate of elongation at either end of the filaments. The most likely explanation for the inhibition of the rate of polymerization of actin in bulk samples is that tropomyosin reduces the number of filament ends by mechanical stabilization of the filaments.

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JO - Biochemistry

JF - Biochemistry

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ER -

Tropomyosin Inhibits the Rate of Actin Polymerization by Stabilizing Actin Filaments

Abstract

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