Fulgenzi G, Graciotti L, Granata A L, Corsi A, Fucini P, Noegel A A, Kent H M, Stewart M
Department of Experimental Pathology, University of Ancona, Via Ranieri, Ancona, 60131, Italy.
J Mol Biol. 1998 Dec 18;284(5):1255-63. doi: 10.1006/jmbi.1998.2294.
We have used electron microscopy and computer image processing to produce a three-dimensional reconstruction of F-actin filaments decorated with the putative lectin and actin-binding protein comitin. These reconstructions show that comitin binds to F-actin at high radius primarily to actin subdomain 1. This location is distinctly different from the binding site on F-actin for other actin bundling proteins, such as members of the alpha-actinin family, and may result from the positively charged comitin interacting with negatively charged sites near the actin N terminus in subdomain 1. The location of the comitin binding site and its restriction to subdomain 1 on a single actin monomer is consistent with comitin's having a function distinct from other actin-binding proteins and, for example, would enable comitin to link bundled actin filaments to the Golgi.
我们利用电子显微镜和计算机图像处理技术,对用假定的凝集素和肌动蛋白结合蛋白伴肌动蛋白装饰的F-肌动蛋白丝进行了三维重建。这些重建结果表明,伴肌动蛋白主要在高半径处与F-肌动蛋白结合,主要结合到肌动蛋白亚结构域1。这个位置与其他肌动蛋白成束蛋白(如α-辅肌动蛋白家族成员)在F-肌动蛋白上的结合位点明显不同,这可能是由于带正电荷的伴肌动蛋白与亚结构域1中肌动蛋白N端附近带负电荷的位点相互作用所致。伴肌动蛋白结合位点的位置及其对单个肌动蛋白单体上亚结构域1的限制,与伴肌动蛋白具有不同于其他肌动蛋白结合蛋白的功能是一致的,例如,这将使伴肌动蛋白能够将成束的肌动蛋白丝连接到高尔基体。