Structure-Function Studies of Myosin Motor Domains
نویسندگان
چکیده
منابع مشابه
Structure-function studies of the myosin motor domain: importance of the 50-kDa cleft.
We used random mutagenesis to create 21 point mutations in a highly conserved region of the motor domain of Dictyostelium myosin and classified them into three distinct groups based on the ability to complement myosin null cell phenotypes: wild type, intermediate, and null. Biochemical analysis of the mutated myosins also revealed three classes of mutants that correlated well with the phenotypi...
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B idirectional, or saltatory, motion is the back-and-forth movement of organelles as they are transported on their filamentous tracks (1, 2). It occurs when plus-end– and minus-end–directed motor proteins colocate on a cargo and there is an alternation in which motor dominates. Bidirectional transport has been observed for many organelles—exosomes, endosomes, mitochondria, melanosomes, neural a...
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Dictyostelium provides a powerful environment for characterization of myosin II function. It provides well-established biochemical methods for in vitro analysis of myosin's properties as well as an array of molecular genetic tools. The absence of myosin function results in an array of phenotypes that can be used to genetically manipulate myosin function. We have previously reported methods for ...
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Myosin filaments interact with actin to generate muscle contraction and many forms of cell motility. X-ray and electron microscopy (EM) studies have revealed the general organization of myosin molecules in relaxed filaments, but technical difficulties have prevented a detailed description. Recent studies using improved ultrastructural and image analysis techniques are overcoming these problems....
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Myosin 1C, the first mammalian single-headed myosin to be purified, cloned, and sequenced, has been implicated in the translocation of plasma membrane channels and transporters. Like other forms of myosin I (of which eight exist in humans) myosin 1C consists of motor, neck, and tail domains. The neck domain binds calmodulins more tightly in the absence than in the presence of Ca(2+). Release of...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2009
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2008.12.3637