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[摘要]：The production of a soluble actomyosin complex would be a significant step toward elucidating molecular interactions responsible for biological movement We took a systematic approach to producing soluble long-pitch actin dimers that are polymerization-deficient yet retain biological protein-protein interactions, including myosin binding Actin mutant proteins and chemical crosslinking were combined with different polymerization inhibition strategies, including ADP-ribosylation, or the use of a polymerization-deficient actin mutant protein. While all of the long-pitch actin dimers retained interactions reflective of F-actin activity, each displayed different interactions with myosin Myosin did not interact productively with long-pitch actin dimers capped with DNase-1, and led to filament formation of unmodified long-pitch actin dimers or dimers possessing a polymerization-deficient actin subunit However, ADP-ribosylated long-pitch actin dimers interacted with myosin, giving this dimer great potential for producing a soluble actomyosin complex, which could greatly improve our understanding of the molecular basis of movement in cells, tissues, and organisms (C) 2010 Elsevier Inc All rights reserved |
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