Persisting in vitro motility of actin filaments at nanomolar ATP concentrations after ATP pretreatment

M. Kellermayer, Thomas R. Hinds, Gerald H. Pollack

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Muscle contraction is driven by the relative sliding of actin- and myosin-containing filaments. This process can be reconstituted in in vitro motility assays, where fluorescent actin filaments travel over a lawn of myosin heads. The velocity of the traveling actin filaments has been shown to depend strongly on the free adenosine triphosphate (ATP) concentration, but below 2-4 μM ATP, filament movement is consistently abolished. Here we report that after a brief exposure of actomyosin to 1 mM ATP, actin filament motility persists down to nanomolar ATP concentrations.

Original languageEnglish
Pages (from-to)89-95
Number of pages7
JournalBBA - Bioenergetics
Volume1229
Issue number1
DOIs
Publication statusPublished - Apr 4 1995

Fingerprint

Actin Cytoskeleton
Actins
Adenosine Triphosphate
Myosins
Actomyosin
Muscle Contraction
Muscle
Assays
In Vitro Techniques

Keywords

  • Actin filament
  • ATP
  • Energy production, unexplained
  • Heavy meromyosin
  • Motility assay, in vitro

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology

Cite this

Persisting in vitro motility of actin filaments at nanomolar ATP concentrations after ATP pretreatment. / Kellermayer, M.; Hinds, Thomas R.; Pollack, Gerald H.

In: BBA - Bioenergetics, Vol. 1229, No. 1, 04.04.1995, p. 89-95.

Research output: Contribution to journalArticle

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