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

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dc.contributor.authorJung, Hyun Suken_US
dc.contributor.authorBurgess, Stan A.en_US
dc.contributor.authorBillington, Neilen_US
dc.contributor.authorColegrave, Melanieen_US
dc.contributor.authorPatel, Hiteshen_US
dc.contributor.authorChalovich, Josephen_US
dc.contributor.authorChantler, Peter D.en_US
dc.contributor.authorKnight, Peter J.en_US
dc.date.accessioned2011-04-13T20:56:10Zen_US
dc.date.accessioned2011-05-17T01:27:02Z
dc.date.available2011-04-13T20:56:10Zen_US
dc.date.available2011-05-17T01:27:02Z
dc.date.issued2008-04-22en_US
dc.description.abstractThe 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 muscle. The similarities extend beyond the shapes of the heads and interactions between them: In both myosins, the tail folds into three segments, apparently at identical sites; all three segments are in close association outside the head region; and two segments are associated in the same way with one head in the asymmetric arrangement. Thus, these organisms, which have different regulatory mechanisms and diverged from a common ancestor >600 Myr ago, have the same quaternary structure. Conservation across such a large evolutionary distance suggests that this conformation is of fundamental functional importance. Proceedings of the National Academy of Science, Vol. 105, No. 16, Apr 2008en_US
dc.identifier.citationProceedings of the National Academy of Science; 105:16 p. 6022-6026en_US
dc.identifier.doi10.1073/pnas.0707846105
dc.identifier.pmidPMC2329715en_US
dc.identifier.urihttp://hdl.handle.net/10342/3317en_US
dc.language.isoen_USen_US
dc.publisherEast Carolina Universityen_US
dc.relation.urihttp://www.pnas.org/content/105/16/6022en_US
dc.rightsAuthor notified of opt-out rights by Cammie Jennings prior to upload of this article.en_US
dc.subjectElectron microscopyen_US
dc.subjectMolluscan muscleen_US
dc.subjectRegulationen_US
dc.subjectSmooth muscleen_US
dc.subjectImage processingen_US
dc.titleConservation of the regulated structure of folded myosin 2 in species separated by at least 600 million years of independent evolutionen_US
dc.typeArticleen_US
ecu.journal.issue16
ecu.journal.nameProceedings of the National Academy of Science
ecu.journal.pages6022-6026
ecu.journal.volume105

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