Houmeida A, Hanin V, Feinberg J, Benyamin Y, Roustan C
UPR 8402 Centre de Recherches de Biochimie Macromoléculaire CNRS, U249 INSERM, Université de Montpellier, France.
Biochem J. 1991 Mar 15;274 ( Pt 3)(Pt 3):753-7. doi: 10.1042/bj2740753.
Gelsolin is a Ca2(+)-dependent protein which severs actin filaments, caps their fast-growing ends and promotes nucleation. We report here results that delimit one of the interfaces between serum gelsolin and actin monomer. An actin-derived synthetic peptide (amino acids 305-326 of actin) coupled to a hydrophilic resin was tested for its possible interaction with gelsolin. We selected this sequence because it corresponds to a region implicated in the gelsolin-actin complex in a previous work [Boyer, Feinberg, Hue, Capony, Benyamin & Roustan (1987) Biochem. J. 248, 359-364]. We showed that this actin sequence is located at the surface of the actin molecule and observed a Ca2(+)-sensitive binding of gelsolin to this actin-derived peptide. In addition, by using a chymotryptic digest of gelsolin, we reported that only the C-terminal half of gelsolin interacts with the actin-(305-326)-peptide. These results that the Ca2(+)-sensitive interface includes both amino acids 305-326 of actin and probably amino acids 660-738 of gelsolin.
凝溶胶蛋白是一种依赖钙离子的蛋白质,它能切断肌动蛋白丝,封闭其快速生长的末端并促进成核作用。我们在此报告确定血清凝溶胶蛋白与肌动蛋白单体之间一个界面的结果。测试了一种与亲水性树脂偶联的肌动蛋白衍生合成肽(肌动蛋白的氨基酸305 - 326)与凝溶胶蛋白的可能相互作用。我们选择这个序列是因为它对应于先前工作中涉及凝溶胶蛋白 - 肌动蛋白复合物的一个区域[博耶、费恩伯格、于埃、卡波尼、贝尼亚明和鲁斯坦(1987年)《生物化学杂志》248卷,359 - 364页]。我们表明这个肌动蛋白序列位于肌动蛋白分子表面,并观察到凝溶胶蛋白与这种肌动蛋白衍生肽的钙离子敏感结合。此外,通过使用凝溶胶蛋白的胰凝乳蛋白酶消化产物,我们报告只有凝溶胶蛋白的C末端一半与肌动蛋白 - (305 - 326)肽相互作用。这些结果表明钙离子敏感界面包括肌动蛋白的氨基酸305 - 326以及可能凝溶胶蛋白的氨基酸660 - 738。