Two heads of myosin are better than one for generating force and motion
AUTOR(ES)
Tyska, M. J.
FONTE
The National Academy of Sciences
RESUMO
Several classes of the myosin superfamily are distinguished by their “double-headed” structure, where each head is a molecular motor capable of hydrolyzing ATP and interacting with actin to generate force and motion. The functional significance of this dimeric structure, however, has eluded investigators since its discovery in the late 1960s. Using an optical-trap transducer, we have measured the unitary displacement and force produced by double-headed and single-headed smooth- and skeletal-muscle myosins. Single-headed myosin produces approximately half the displacement and force (≈6 nm; 0.7 pN) of double-headed myosin (≈10 nm; 1.4 pN) during a unitary interaction with actin. These data suggest that muscle myosins require both heads to generate maximal force and motion.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=16344Documentos Relacionados
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