C-terminally deleted fragments of 40-kDa earthworm actin modulator still show gelsolin activities.
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.
Giebing
T
T
Institut für Zoomorphologie, Zellbiologie und Parasitologie, Heinrich-Heine-Universität, Düsseldorf, Germany.
Obermann
W M
WM
Fürst
D
D
D'Haese
J
J
D000199:Actins / Q000378:metabolism*; D000818:Animals; D002118:Calcium / Q000378:metabolism; D018260:Gelsolin / Q000737:chemistry*; D008840:Microfilament Proteins / Q000737:chemistry*; D009835:Oligochaeta; D011108:Polymers; D011485:Protein Binding; D017384:Sequence Deletion; D013329:Structure-Activity Relationship
D000199:Actins; D018260:Gelsolin; D008840:Microfilament Proteins; D011108:Polymers; D002118:Calcium