Zhang J, Robson R M, Schmidt J M, Stromer M H
Department of Biochemistry and Biophysics, Iowa State University, Ames 50011, USA.
Biochem Biophys Res Commun. 1996 Jan 17;218(2):530-7. doi: 10.1006/bbrc.1996.0095.
The talin-actin interaction was examined by using negative staining and cosedimentation assays. At pH 6.4 and low ionic strength, talin extensively crosslinked actin filaments into both networks and bundles. The bundles consist of parallel actin filaments with a center-to-center distance of 13 nm, and talin crossbridges spaced at 36-nm intervals along the bundles. As pH was increased stepwise from 6.4 to 7.3, talin's bundling activity was decreased first, then its networking activity. Qualitatively similar results were obtained at pH 6.4 by increasing ionic strength. Chemical crosslinking indicated talin was present as a dimer from pH 6.4 to 7.3, with or without added KC1. The results show that talin can interact directly with actin filaments by formation of actin filament networks and bundles, with the bundles more sensitive to dissolution by increase in pH or ionic strength.
通过负染和共沉降试验研究了踝蛋白与肌动蛋白的相互作用。在pH 6.4和低离子强度条件下,踝蛋白将肌动蛋白丝广泛交联成网络和束状结构。束状结构由中心距为13 nm的平行肌动蛋白丝组成,踝蛋白的交联桥沿束状结构以36 nm的间隔排列。随着pH从6.4逐步升高到7.3,踝蛋白的束状形成活性首先降低,随后其网络形成活性降低。在pH 6.4时通过增加离子强度也获得了定性相似的结果。化学交联表明,无论是否添加KCl,在pH 6.4至7.3范围内,踝蛋白均以二聚体形式存在。结果表明,踝蛋白可通过形成肌动蛋白丝网络和束状结构直接与肌动蛋白丝相互作用,其中束状结构对pH或离子强度增加引起的溶解更敏感。