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Myosin VI dimerization triggers an unfolding of a three-helix bundle in order to extend its reach.
Mukherjea, Monalisa; Llinas, Paola; Kim, HyeongJun; Travaglia, Mirko; Safer, Daniel; Ménétrey, Julie; Franzini-Armstrong, Clara; Selvin, Paul R; Houdusse, Anne; Sweeney, H Lee.
Afiliação
  • Mukherjea M; Department of Physiology, University of Pennsylvania School of Medicine, Philadelphia, 19104, USA.
Mol Cell ; 35(3): 305-15, 2009 Aug 14.
Article em En | MEDLINE | ID: mdl-19664948
ABSTRACT
Myosin VI challenges the prevailing theory of how myosin motors move on actin the lever arm hypothesis. While the reverse directionality and large powerstroke of myosin VI can be attributed to unusual properties of a subdomain of the motor (converter with a unique insert), these adaptations cannot account for the large step size on actin. Either the lever arm hypothesis needs modification, or myosin VI has some unique form of extension of its lever arm. We determined the structure of the region immediately distal to the lever arm of the motor and show that it is a three-helix bundle. Based on C-terminal truncations that display the normal range of step sizes on actin, CD, fluorescence studies, and a partial deletion of the bundle, we demonstrate that this bundle unfolds upon dimerization of two myosin VI monomers. This unconventional mechanism generates an extension of the lever arm of myosin VI.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Cadeias Pesadas de Miosina Limite: Animals Idioma: En Revista: Mol Cell Assunto da revista: BIOLOGIA MOLECULAR Ano de publicação: 2009 Tipo de documento: Article País de afiliação: Estados Unidos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Cadeias Pesadas de Miosina Limite: Animals Idioma: En Revista: Mol Cell Assunto da revista: BIOLOGIA MOLECULAR Ano de publicação: 2009 Tipo de documento: Article País de afiliação: Estados Unidos