Tryptophan Residues from Cap Binding Slot in eIF4E Family Members: Their Contributions to Near-UV Circular Dichroism Spectra

J. Zuberek, A. Stelmachowska
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引用次数: 1

Abstract

eIF4E, a key factor in the cap-dependent translation initiation, binds cap structure at the 5’ end of mRNA by stacking interaction involving two of its eight conserved tryptophan residues. In this paper, we examined individual contributions of tryptophan residues to the near-UV Circular Dichroism spectra to identify structural similarities and differences in cap binding motif among members of eIF4E family. The near-UV CD spectrum of human eIF4E1a in its apo form, resulting mainly from 1Lb transition and dominated by two vibrionic bands, is conserved among eIF4Es. Based on comparison of CD spectra for eIF4E mutants, we showed that tryptophans involved in stacking interaction give strongest individual contributions, which allow identification of their different orientation with respect to the cap. This indicates that near-UV CD is a quick and powerful tool to analyse tryptophan conformation in eIF4E proteins, and their changes upon binding modified cap analogues.
eIF4E家族成员帽结合槽色氨酸残基对近紫外圆二色光谱的贡献
eIF4E是帽依赖翻译起始的关键因子,通过涉及其8个保守色氨酸残基中的两个的堆叠相互作用,在mRNA的5 '端结合帽结构。在本文中,我们研究了色氨酸残基对近紫外圆二色光谱的个别贡献,以确定eIF4E家族成员之间帽结合基序的结构相似性和差异性。人eIF4E1a载子型的近紫外CD谱在eIF4Es中是保守的,主要由1Lb跃迁引起,并以两条振子带为主。基于对eIF4E突变体CD光谱的比较,我们发现参与堆叠相互作用的色氨酸提供了最强的个体贡献,这使得它们相对于帽的不同取向得以识别。这表明近紫外CD是一种快速而强大的工具,可以分析eIF4E蛋白中色氨酸的构象,以及它们在结合修饰帽类似物时的变化。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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