A functional recombinant myosin II lacking a regulatory light chain-binding site

Taro Q.P. Uyeda, James A. Spudich

Research output: Contribution to journalArticlepeer-review

102 Citations (Scopus)

Abstract

Myosin II, which converts the energy of adenosine triphosphate hydrolysis into the movement of actin filaments, is a hexamer of two heavy chains, two essential light chains, and two regulatory light chains (RLCs). Dictyostelium myosin II is known to be regulated in vitro by phosphorylation of the RLC. Cells in which the wild-type myosin II heavy chain was replaced with a recombinant form that lacks the binding site for RLC carried out cytokinesis and almost normal development, processes known to be dependent on functional myosin II. Characterization of the purified recombinant protein suggests that a complex of RLC and the RLC binding site of the heavy chain plays an inhibitory role for adenosine triphosphatase activity and a structural role for the movement of myosin along actin.

Original languageEnglish
Pages (from-to)1867-1870
Number of pages4
JournalScience
Volume262
Issue number5141
DOIs
Publication statusPublished - 1993
Externally publishedYes

ASJC Scopus subject areas

  • General

Fingerprint Dive into the research topics of 'A functional recombinant myosin II lacking a regulatory light chain-binding site'. Together they form a unique fingerprint.

Cite this