Abstract
Proteins of the gelsolin family are Ca2+-dependent, multifunctional, actin-binding proteins containing three (S1–S3, about 40 kDa) or six (S1–S6, about 80 kDa) highly conserved repeats in the amino acid sequence. The pattern of interaction of these proteins with actin is complex: they can sever actin filaments; promote polymer nucleation after binding to two actin monomers; and cap the growing barbed end of actin filaments. In the present study, an actin polymerizing factor (46 kDa) from the adductor muscle of a bivalve mollusc has been discovered and identified for the first time. This protein has turned out to belong to the gelsolin family of actin regulatory proteins. The expression of gelsolin-like proteins in the tissues of bivalves was predicted after analyzing their proteome, but this is the first study where an actually expressed protein has been found. A primary determination of its physicochemical properties such as molecular weight, charge, resistance to urea, influence on actin polymerization by viscosity, and light scattering is carried out and the molecular structure analyzed.
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