Mutational analysis of an actin-binding site of cofilin and characterization of chimeric proteins between cofilin and destrin.

摘要: Cofilin and destrin are two related low molecular weight mammalian actin-binding proteins. is an F-actin side-binding pH-dependent actin-depolymerizing protein, a pH-independent protein. We have introduced few point mutations within sequence of cofilin. Biochemical analyses these mutant proteins clearly shown that Lys112 Lys114 cofilin crucially but differently involved in its interaction with actin phosphatidylinositol 4,5-bisphosphate. This the first example among whose inactivate their vitro. also made characterized series chimeric between to identify regions responsible for pH dependence side binding activity Our results suggest central region consisting 42 amino acid residues carboxyl-terminal quarter both regulation depolymerizing bind along F-actin.