Movement of myosin-coated beads on oriented filaments reconstituted from purified actin

James A. Spudich, Stephen J. Kron, Michael Sheetz

Research output: Contribution to journalArticle

87 Citations (Scopus)

Abstract

Although the biochemical properties of the actin/myosin interaction have been studied extensively using actin activation of myosin ATPase as an assay1,2, until recently no well-defined assay has been available to measure the mechanical properties of ATP-dependent movement of myosin along actin filaments. The first direct measurements of the rate of myosin movement in vitro3,4 used a naturally occurring, biochemically ill-defined array of actin filaments from the alga Nitella. We report here the construction of an oriented array of filaments reconstituted from purified muscle actin and the use of this array in a biochemically defined quantitative assay for the directed movement of myosin-coated polystyrene beads. We demonstrate for the first time that actin alone, linked to a substratum by a protein anchor, is sufficient to support movement of myosin at rates consistent with the speeds of muscle contraction and other forms of cell motility.

Original languageEnglish (US)
Pages (from-to)584-586
Number of pages3
JournalNature
Volume315
Issue number6020
DOIs
StatePublished - Dec 1 1985
Externally publishedYes

Fingerprint

Myosins
Actins
Actin Cytoskeleton
Nitella
Polystyrenes
Muscle Contraction
Cell Movement
Adenosine Triphosphate
Muscles
Proteins

ASJC Scopus subject areas

  • General

Cite this

Movement of myosin-coated beads on oriented filaments reconstituted from purified actin. / Spudich, James A.; Kron, Stephen J.; Sheetz, Michael.

In: Nature, Vol. 315, No. 6020, 01.12.1985, p. 584-586.

Research output: Contribution to journalArticle

Spudich, James A. ; Kron, Stephen J. ; Sheetz, Michael. / Movement of myosin-coated beads on oriented filaments reconstituted from purified actin. In: Nature. 1985 ; Vol. 315, No. 6020. pp. 584-586.
@article{c766a0e39f424fddacdf9bb67820f69d,
title = "Movement of myosin-coated beads on oriented filaments reconstituted from purified actin",
abstract = "Although the biochemical properties of the actin/myosin interaction have been studied extensively using actin activation of myosin ATPase as an assay1,2, until recently no well-defined assay has been available to measure the mechanical properties of ATP-dependent movement of myosin along actin filaments. The first direct measurements of the rate of myosin movement in vitro3,4 used a naturally occurring, biochemically ill-defined array of actin filaments from the alga Nitella. We report here the construction of an oriented array of filaments reconstituted from purified muscle actin and the use of this array in a biochemically defined quantitative assay for the directed movement of myosin-coated polystyrene beads. We demonstrate for the first time that actin alone, linked to a substratum by a protein anchor, is sufficient to support movement of myosin at rates consistent with the speeds of muscle contraction and other forms of cell motility.",
author = "Spudich, {James A.} and Kron, {Stephen J.} and Michael Sheetz",
year = "1985",
month = "12",
day = "1",
doi = "10.1038/315584a0",
language = "English (US)",
volume = "315",
pages = "584--586",
journal = "Nature",
issn = "0028-0836",
publisher = "Nature Publishing Group",
number = "6020",

}

TY - JOUR

T1 - Movement of myosin-coated beads on oriented filaments reconstituted from purified actin

AU - Spudich, James A.

AU - Kron, Stephen J.

AU - Sheetz, Michael

PY - 1985/12/1

Y1 - 1985/12/1

N2 - Although the biochemical properties of the actin/myosin interaction have been studied extensively using actin activation of myosin ATPase as an assay1,2, until recently no well-defined assay has been available to measure the mechanical properties of ATP-dependent movement of myosin along actin filaments. The first direct measurements of the rate of myosin movement in vitro3,4 used a naturally occurring, biochemically ill-defined array of actin filaments from the alga Nitella. We report here the construction of an oriented array of filaments reconstituted from purified muscle actin and the use of this array in a biochemically defined quantitative assay for the directed movement of myosin-coated polystyrene beads. We demonstrate for the first time that actin alone, linked to a substratum by a protein anchor, is sufficient to support movement of myosin at rates consistent with the speeds of muscle contraction and other forms of cell motility.

AB - Although the biochemical properties of the actin/myosin interaction have been studied extensively using actin activation of myosin ATPase as an assay1,2, until recently no well-defined assay has been available to measure the mechanical properties of ATP-dependent movement of myosin along actin filaments. The first direct measurements of the rate of myosin movement in vitro3,4 used a naturally occurring, biochemically ill-defined array of actin filaments from the alga Nitella. We report here the construction of an oriented array of filaments reconstituted from purified muscle actin and the use of this array in a biochemically defined quantitative assay for the directed movement of myosin-coated polystyrene beads. We demonstrate for the first time that actin alone, linked to a substratum by a protein anchor, is sufficient to support movement of myosin at rates consistent with the speeds of muscle contraction and other forms of cell motility.

UR - http://www.scopus.com/inward/record.url?scp=0022263118&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0022263118&partnerID=8YFLogxK

U2 - 10.1038/315584a0

DO - 10.1038/315584a0

M3 - Article

VL - 315

SP - 584

EP - 586

JO - Nature

JF - Nature

SN - 0028-0836

IS - 6020

ER -