Key result
Recombinant rat alpha-actin demonstrated a sliding velocity of 6.25 mm/s in an in vitro motility assay, consistent with the 6.31 mm/s velocity of wild-type rabbit skeletal muscle actin.
Absolute Event Rate: 6.25% vs 6.31%
The development of fully active recombinant alpha-actin with specific fluorescent labeling sites enables advanced single-molecule studies of actin dynamics during muscle contraction.
Facilitates single-molecule studies of actin dynamics in contraction; leaves open clinical translation pending human validation.
Until recently, actin was thought to act merely as a passive track for its motility partner, myosin, during actomyosin interactions. Yet a recent report having observed dynamical conformational changes in labeled skeletal muscle alpha-actin suggests that actin has a more active role. Because the labeling technique was still immature, however, conclusions regarding the significance of the different conformations are difficult to make. Here, we describe the preparation of fully active alpha-actin obtained from a baculovirus expression system. We developed alpha-actin recombinants, of which subdomains 1 and 2 have specific sites for fluorescent probes. This specific labeling technique offers to significantly expand the information acquired from actin studies.
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Iwane et al. (2009) studied this question. Recombinant alpha-actin vs. Rabbit skeletal muscle actin was evaluated on Actin filament sliding velocity in vitro motility assay. Recombinant rat alpha-actin demonstrated a sliding velocity of 6.25 mm/s in an in vitro motility assay, consistent with the 6.31 mm/s velocity of wild-type rabbit skeletal muscle actin.
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