酵母tRNA（Asp）反密码子区域与天冬氨酰-tRNA合成酶紧密接触的足迹证据。

Footprinting evidence for close contacts of the yeast tRNA(Asp) anticodon region with aspartyl-tRNA synthetase.

作者信息

Garcia A, Giege R

机构信息

Unité Propre de Recherche Structure des Macromolécules Biologiques et Mécanismes de Reconnaissance, Institut de Biologie Moléculaire et Cellulaire du Centre National de la Recherche Scientifique, Strasbourg, France.

出版信息

Biochem Biophys Res Commun. 1992 Jul 31;186(2):956-62. doi: 10.1016/0006-291x(92)90839-d.

DOI:10.1016/0006-291x(92)90839-d

PMID:1497679

Abstract

Chemical footprinting experiments on brewer's yeast tRNA(Asp) complexed to its cognate aspartyl-tRNA synthetase are reported: they demonstrate that bases of the anticodon loop, including the anticodon itself, are in close proximity with the synthetase. Contacts were determined using dimethylsulfate as the probe for testing reactivity of guanine and cytosine residues in free and complexed tRNA. Results correlate with the decrease in aspartylation activity of yeast tRNA(Asp) molecules mutated at these contact positions and will be compared with other structural data arising from solution and crystallographic studies on the aspartic acid complex.

摘要

报道了对与同源天冬氨酰 - tRNA合成酶复合的啤酒酵母tRNA（Asp）进行的化学足迹实验：这些实验表明，反密码子环的碱基，包括反密码子本身，与合成酶紧密相邻。使用硫酸二甲酯作为探针来检测游离和复合tRNA中鸟嘌呤和胞嘧啶残基的反应性，从而确定接触位点。结果与在这些接触位置发生突变的酵母tRNA（Asp）分子的天冬氨酰化活性降低相关，并将与来自天冬氨酸复合物的溶液和晶体学研究的其他结构数据进行比较。