C‐terminally deleted fragments of 40‐kDa earthworm actin modulator still show gelsolin activities

FEBS Letters

D'Haese, Jochen¹  Giebing, Thomas¹  Fürst, Dieter³  Obermann, Wolfgang M.J² 

[1] Institut für Zoomorphologie, Zellbiologie und Parasitologie, Heinrich-Heine-Universität, 40225 Düsseldorf, Germany;Max-Planck-Institut für Biochemie, 82152 Martinsried, Germany;Institut für Zoophysiologie und Zellbiologie, Universität Potsdam, 14471 Potsdam, Germany

关键词: Gelsolin;    Actin-binding protein;    Actin fragmentation;    Actin nucleation;    Earthworm muscle;    EWAM;    earthwctin modulator or earthworm gelsolin;    E1–3;    the three repeating segments of EWAM;    S1–3;    the three repeating segments of severin;    G1–6;    the six repeating segments of human plasma gelsolin;    IAEDANS;    N-(iodoacetyl)-N-1-sulfo-5-naphthylethylenediamine;    IPTG;    isopropyl-β-d-thiogalactoside;    PI-actin;    G-actin labeled with N-(1-pyrenyl) iodoacetamide;    PhMeSO2F;    phenylmethanesulfonyl fluoride;   

DOI  :  10.1016/S0014-5793(97)01230-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown