Conservation of the regulated structure of folded myosin 2 in species separated by at least 600 million years of independent evolution.

ABSTRACT: The myosin 2 family of molecular motors includes isoforms regulated in different ways. Vertebrate smooth-muscle myosin is activated by phosphorylation of the regulatory light chain, whereas scallop striated adductor-muscle myosin is activated by direct calcium binding to its essential light chain. The paired heads of inhibited molecules from myosins regulated by phosphorylation have an asymmetric arrangement with motor-motor interactions. It was unknown whether such interactions were a common motif for inactivation used in other forms of myosin-linked regulation. Using electron microscopy and single-particle image processing, we show that indistinguishable structures are indeed found in myosins and heavy meromyosins isolated from scallop striated adductor muscle and turkey gizzard smooth m

SUBMITTER: Jung HS 

PROVIDER: S-EPMC2329715 | biostudies-literature | 2008 Apr

REPOSITORIES: biostudies-literature