Lebart M C, Méjean C, Roustan C, Benyamin Y
Centre de Recherches de Biochimie Macromoléculaire, U. 249 Institut National de la Santé et de la Recherche Médicale, Université de Montpellier I, France.
J Biol Chem. 1993 Mar 15;268(8):5642-8.
The interaction between alpha-actinin and actin was further characterized using natural and synthetic peptides of actin together with anti-actin antibodies of known specificity. We demonstrated that two alpha-actinin binding sequences on actin are located within residues 112-125 and 360-372. Each peptide was shown to directly bind alpha-actinin and was able to dissociate the alpha-actinin-actin complex using solid phase binding assays and cosedimentation experiments. Taking into account the three-dimensional structure of actin (Kabsch, W., Mannherz, H. G., Suck, D., Pai, E. F., and Holmes, K. C. (1990) Nature 347, 37-44), we postulate that these two segments, proximal in the actin structure, are part of the same site. In addition, we compared these two segments with those recently found for filamin (Méjean, C., Lebart, M. C., Boyer, M., Roustan, C., and Benyamin, Y. (1992) Eur. J. Biochem. 209, 555-562), Egan, S., Stewart, M., Stossel, T. P., Kwiatkowski, D. J., and Hartwig, J. H. (1990) J. Cell Biol. 111, 1089-1105), and concluded that the two actin-binding proteins interact with closely spaced or overlapping but not identical sequences of actin subdomain 1.
利用肌动蛋白的天然肽和合成肽以及已知特异性的抗肌动蛋白抗体，进一步对α - 辅肌动蛋白与肌动蛋白之间的相互作用进行了表征。我们证明，肌动蛋白上的两个α - 辅肌动蛋白结合序列位于第112 - 125位残基和第360 - 372位残基内。通过固相结合试验和共沉降实验表明，每种肽都能直接结合α - 辅肌动蛋白，并能解离α - 辅肌动蛋白 - 肌动蛋白复合物。考虑到肌动蛋白的三维结构（卡布施，W.，曼赫茨，H. G.，萨克，D.，派，E. F.，和霍姆斯，K. C.（1990年）《自然》347，37 - 44），我们推测在肌动蛋白结构中相邻的这两个片段是同一位点的一部分。此外，我们将这两个片段与最近发现的细丝蛋白（梅让，C.，勒巴特，M. C.，博耶，M.，鲁斯坦，C.，和贝尼亚明，Y.（1992年）《欧洲生物化学杂志》209，555 - 562）、伊根，S.，斯图尔特，M.，斯托塞尔，T. P.，克维亚特科夫斯基，D. J.，和哈特维希，J. H.（1990年）《细胞生物学杂志》111，1089 - 1105）的片段进行了比较，得出结论：这两种肌动蛋白结合蛋白与肌动蛋白亚结构域1中紧密间隔或重叠但不相同的序列相互作用。
