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Cell Motil Cytoskeleton. 1999;43(2):128-36.

Purification and biochemical characterization of actin from Caenorhabditis elegans: its difference from rabbit muscle actin in the interaction with nematode ADF/cofilin.

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  • Department of Pathology, Emory University, Atlanta, Georgia 30322, USA. ono@bimcore.emory.edu


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 actin-binding proteins can interact with C. elegans actin in a distinct manner from rabbit muscle actin.

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