Another step ahead for myosin

Article Abstract:

Each interaction of myosin, the motor protein in muscle, with actin can include two or more sub-steps per ATP hydrolyzed. It is possible that the sub-steps seen with myr-1 from rat liver and brush-border myosin-I from chicken intestinal epithelium are linked with two intermediate steps in the ATP hydrolysis cycle. These steps could be the release of inorganic phosphate from the active site, followed by the release of ADP. It is clear that single-molecule techniques can highlight intermediate transitions in protein-protein interactions.

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Three-dimensional structural dynamics of myosin V by single-molecule fluorescence polarization

Article Abstract:

The three-dimensional measurements of the structural dynamics of the light chain domain of brain myosin V using a single molecule fluorescence polarization technique that determines the orientation of individual protein domains with 20-40-ms time resolution, is reported. The technique is applicable to the study of real-time structural changes in other biological systems.

Structural dynamics

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Drosphila Spire is an actin nucleation factor

Article Abstract:

The Drosphila protein Spire is shown to represent a third class of actin nucleation factor. In vitro, Spire nucleates new filaments at a rate that is similar to that of the formin family of proteins but slower than in the activated Arp2/3 complex.

Gene mutations, Gene mutation, Actin, Nucleation, Nucleation (Chemistry)

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