The myosin catalytic domain does not rotate during the working power stroke
نویسندگان
چکیده
منابع مشابه
Direct real-time detection of the actin-activated power stroke within the myosin catalytic domain.
We have used transient kinetics, nanosecond time-resolved fluorescence resonance energy transfer (FRET), and kinetics simulations to resolve a structural transition in the Dictyostelium myosin II relay helix during the actin-activated power stroke. The relay helix plays a critical role in force generation in myosin, coupling biochemical changes in the ATPase site with the force-transducing rota...
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Myosin II generates force for the division of eukaryotic cells. The molecular basis of the spatial and temporal localization of myosin II to the cleavage furrow is unknown, although models often imply that interaction between myosin II and actin filaments is essential. We examined the localization of a chimeric protein that consists of the green fluorescent protein fused to the N terminus of tr...
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The multidomain UNC-45B chaperone is crucial for the proper folding and function of sarcomeric myosin. We recently found that UNC-45B inhibits the translocation of actin by myosin. The main functions of the UCS and TPR domains are known but the role of the central domain remains obscure. Here, we show-using in vitro myosin motility and ATPase assays-that the central domain alone acts as an inhi...
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Conventional EPR studies of muscle fibers labeled with a novel alpha-iodoketo spin label at Cys-707 of the myosin head revealed substantial internal domain reorganization on the addition of ADP to rigor fibers. The spin probes that are well-ordered in the rigor state become disordered and form two distinct populations. These orientational changes do not correspond to rotation of the myosin cata...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 1995
ISSN: 0006-3495
DOI: 10.1016/s0006-3495(95)79974-x