C- and N-terminally truncated fragments of earthworm gelsolin were constructed, cloned and expressed in Escherichia coli. G-actin-binding properties of these fragments and their influences on the polymeric state of actin were investigated. A construct lacking a large part of the third segment [E(1-295)] supports actin nucleation similar to the complete protein and shows reduced actin fragmentation property, but is no longer Ca2+-sensitive in its activity. The first and the second segments (E1 and E2) each contain one actin-binding site. In contrast to human gelsolin, E1 in combination with a short N-terminal region of E2 is not sufficient for the F-actin-severing activity of the protein.