Abstract
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 a-actin suggests that actin has a more active role. Because the labeling technique was still immature, however, conclusions regarding the signi-ficance of the different conformations are difficult to make. Here, we describe the preparation of fully active a-actin obtained from a baculovirus expression system. We developed a-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.
Original language | English |
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Pages (from-to) | 491-499 |
Number of pages | 9 |
Journal | Proceedings of the Japan Academy Series B: Physical and Biological Sciences |
Volume | 85 |
Issue number | 10 |
DOIs | |
Publication status | Published - Dec 2009 |
Externally published | Yes |
Keywords
- Actomyosin
- Fluorescent imaging
- In vitro motility assay
- Polymerization
- Recombinant protein
- α-Actin
ASJC Scopus subject areas
- Agricultural and Biological Sciences(all)
- Physics and Astronomy(all)