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 |
|---|---|
| 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 |
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Keywords
- α-Actin
- Actomyosin
- Fluorescent imaging
- In vitro motility assay
- Polymerization
- Recombinant protein
ASJC Scopus subject areas
- General
Cite this
Recombinant α-actin for specific fluorescent labeling. / Iwane, Atsuko H.; Morimatsu, Masatoshi; Yanagida, Toshio.
In: Proceedings of the Japan Academy Series B: Physical and Biological Sciences, Vol. 85, No. 10, 12.2009, p. 491-499.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Recombinant α-actin for specific fluorescent labeling
AU - Iwane, Atsuko H.
AU - Morimatsu, Masatoshi
AU - Yanagida, Toshio
PY - 2009/12
Y1 - 2009/12
N2 - 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.
AB - 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.
KW - α-Actin
KW - Actomyosin
KW - Fluorescent imaging
KW - In vitro motility assay
KW - Polymerization
KW - Recombinant protein
UR - http://www.scopus.com/inward/record.url?scp=77449145410&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=77449145410&partnerID=8YFLogxK
U2 - 10.2183/pjab.85.491
DO - 10.2183/pjab.85.491
M3 - Article
C2 - 20009382
AN - SCOPUS:77449145410
VL - 85
SP - 491
EP - 499
JO - Proceedings of the Japan Academy Series B: Physical and Biological Sciences
JF - Proceedings of the Japan Academy Series B: Physical and Biological Sciences
SN - 0386-2208
IS - 10
ER -