Purification and biochemical characterization of actin fromCaenorhabditis elegans: Its difference from rabbit muscle actin in the interaction with nematode ADF/cofilin
✍ Scribed by Ono, Shoichiro
- Publisher
- John Wiley and Sons
- Year
- 1999
- Tongue
- English
- Weight
- 168 KB
- Volume
- 43
- Category
- Article
- ISSN
- 0886-1544
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✦ Synopsis
Biochemical analysis of cytoskeletal proteins of the nematode Caenorhabditis elegans can be combined with a vast resource of genetic information in order to understand the regulation and function of the cytoskeleton in vivo. Here, I report an improved and efficient method to purify actin from wild-type C. elegans and characterization of its biochemical properties. The purified actin was highly pure and free of several known actin-binding proteins. G-actin was polymerized into F-actin in a similar kinetic process to rabbit muscle actin. G-actin interacted with bovine DNase I and inhibited its activity. However, UNC-60B, an isoform of ADF/cofilin in C. elegans, showed a marked depolymerizing activity on C. elegans actin but not on rabbit muscle actin. The results indicate that C. elegans actin shares common biochemical properties with rabbit muscle actin, while actinbinding proteins can interact with C. elegans actin in a distinct manner from rabbit muscle actin. Cell Motil.