Lebart M C, Méjean C, Boyer M, Roustan C, Benyamin Y
Centre de Recherches de Biochimie Macromoléculaire (CNRS), U. 249 (INSERM), Université de Montpellier I, France.
Biochem Biophys Res Commun. 1990 Nov 30;173(1):120-6. doi: 10.1016/s0006-291x(05)81030-7.
The interaction of filamentous actin with alpha-actinin, an actin cross-linking protein, is well established. On the other hand, monomeric actin-alpha-actinin interaction has been a subject of controversy. In this report, we have characterized the interaction of monomeric actin, coated on plastic plates under conditions of non-polymerization, with alpha-actinin in presence of magnesium. Using specific polyclonal anti-actin antibodies, with the whole molecule or purified peptides, we have localized two sites of interaction on action molecule: one near Thr-103 and a new one in the twenty last amino acids.
丝状肌动蛋白与肌动蛋白交联蛋白α-辅肌动蛋白之间的相互作用已得到充分证实。另一方面,单体肌动蛋白与α-辅肌动蛋白的相互作用一直存在争议。在本报告中,我们描述了在非聚合条件下包被于塑料板上的单体肌动蛋白与镁存在时的α-辅肌动蛋白之间的相互作用。使用针对整个分子或纯化肽段的特异性多克隆抗肌动蛋白抗体,我们在肌动蛋白分子上定位了两个相互作用位点:一个靠近苏氨酸-103,另一个在最后二十个氨基酸中。