晶体肌动蛋白管

Julian A. Barden, Paul M.G. Curmi, Cristobal G. Dos Remedios
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引用次数: 8

摘要

采用紫外差值法和高分辨率核磁共振波谱法研究了三价阳离子钪(Sc3+)和钇(Y3+)对G-actin构象的影响。与先前获得的三价镧系离子(Ln3+)的数据进行了比较。这些结果表明,第一个和随后的Y离子(离子半径为101.9 pm)的行为与Ln3+完全相同。Sc3+是比任何Ln3+都小的离子(87pm)。第一个Sc3+结合到肌动蛋白上一个Mg2+、Y3+和Ln3+无法进入的位点上。然而,第二个结合的Sc3+表现得像Ln3+。在取代天然二价阳离子(Mg2+)时,Y3+和Sc3+都调动了与肌动蛋白结合的ATP的腺嘌呤环,从而将潜在残留物暴露于溶剂中。当Y3+和Sc3+饱和它们在肌动蛋白上的结合位点时,当离子强度在pH为6.9的KCI下提高到0.1 M时,肌动蛋白聚集。Y3+以6:1的比例与肌动蛋白结合,诱导肌动蛋白聚集成结晶肌动蛋白管,而stsc3 + Sc3+以8:1的比例结合,诱导肌动蛋白无定形聚集。这些结果与肌动蛋白管是由三价阳离子诱导的建议是一致的,主要基于它们的结合化学计量,而这又由离子半径决定。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Crystalline actin tubes

The effect of the trivalent cations scandium (Sc3+) and yttrium (Y3+) on the conformation of G-actin was examined using ultraviolet difference and high resolution 1H-NMR spectroscopy. A comparison was made with data obtained previously with the trivalent lanthanide cations (Ln3+). These results indicate that the first and subsequent Y ions (ionic radius 101.9 pm) behave exactly like Ln3+. Sc3+ is a smaller ion (87 pm) than any of the Ln3+. The first Sc3+ binds to a site on actin that is inaccessible to Mg2+, Y3+ and Ln3+. However, the second Sc3+ to bind behaves like an Ln3+. On replacing the native divalent cation (Mg2+), both Y3+ and Sc3+ mobilize the adenine ring of ATP bound to actin, thus exposing underlying residues to the solvent. When Y3+ and Sc3+ saturate their binding sites on actin, and when the ionic strength is raised to 0.1 M with KCI at pH 6.9, the actin aggregates. Y3+ binds to actin with a ratio of 6 : 1 and induces the aggregation of actin into crystalline actin tubes, whilstSc3+ Sc3+binds with a ratio of 8 : 1 and induces amorphous actin aggregates. These results are consistent with the suggestion that actin tubes are induced by trivalent cations, principally on the basis of their binding stoichiometry, which in turn is determined by ionic radius.

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