Suppr超能文献

蛋白质合成中的编辑机制。异亮氨酰 - tRNA合成酶对缬氨酸的排斥。

Editing mechanisms in protein synthesis. Rejection of valine by the isoleucyl-tRNA synthetase.

作者信息

Fersht A R

出版信息

Biochemistry. 1977 Mar 8;16(5):1025-30. doi: 10.1021/bi00624a034.

Abstract

Although the isoleucyl-tRNA synthetase from Escherichia coli (IRS) does not catalyze the overall mischarging of tRNAIle with valine, it does undergo the first step of the reaction, the formation of an IRS-Val-AMP complex. The addition of tRNAIle to this complex leads to its quantitative hydrolysis and the IRS acts as an ATP pyrophosphate in the presence of valine and tRNAIle (Baldwin, A.N., and Berg, P. (1966), J. Biol. Chem. 241, 839). It is shown that during the ATP pyrophosphatase reaction: (a) IRS forms an IRS-Val-AMP complex; (b) the turnover number of the ATP pyrophosphatase reaction is the same at the rate constant for the transfer of isoleucine from IRS-Ile-AMP to tRNAIle over a wide range of temperature and pH; (c) mischarged Val-tRNAIle is hydrolyzed by IRS with a turnover number of 10 s-1 at pH 7.78 and 25 degrees C, compared with a value of 1.2 s-1 for the transfer of isoleucine from IRS-Ile-AMP to tRNA or for the ATP pyrophosphatase reaction. Although this appears to be consistent with an editing mechanism in which there is a slow transfer of the valine from the IRS-Val-AMP to tRNAIle follwed by the rapid hydrolytic step, as recently found for the rejection of threonine by the valyl-tRNA synthetase, there is an inconsistency. This scheme predicts that on mixing IRS.[14C]Val-AMP with tRNAIle there should be a transient misacylation of the tRNA such that about 10% of the [14C]Val is present as [14C]Val-tRNAIle at the peak. But 0.8% or less is found. This could possibly be caused by the IRS having a higher hydrolytic activity during the mischarging reaction than is measured on mixing the unligated enzyme with performed Val-tRNAIle. Alternatively, a two-stage editing mechanism must be considered in which the majority of the Val-AMP is destroyed before the transfer to tRNA in the major editing step, while the hydrolytic activity of the IRS towards Val-tRNAIle is a second editing step to mop up any mischarged tRNA formed by the Val-AMP escaping the first editing step. It is shown that the "kinetic proofreading" mechanism of Hopfield is not consistent with the experimental data.

摘要

尽管来自大肠杆菌的异亮氨酰 - tRNA合成酶(IRS)不会催化缬氨酸对异亮氨酸tRNA(tRNAIle)的整体错配,但它确实会经历反应的第一步,即形成IRS - 缬氨酸 - 腺苷酸(IRS - Val - AMP)复合物。将tRNAIle添加到该复合物中会导致其定量水解,并且在缬氨酸和tRNAIle存在的情况下,IRS会充当ATP焦磷酸酶(鲍德温,A.N.,和伯格,P.(1966年),《生物化学杂志》241卷,839页)。结果表明,在ATP焦磷酸酶反应过程中:(a)IRS形成IRS - Val - AMP复合物;(b)在很宽的温度和pH范围内,ATP焦磷酸酶反应的周转数与异亮氨酸从IRS - 异亮氨酸 - 腺苷酸(IRS - Ile - AMP)转移到tRNAIle的速率常数相同;(c)在pH 7.78和25℃条件下,错配的缬氨酸 - tRNAIle被IRS水解,周转数为10 s-1,而异亮氨酸从IRS - Ile - AMP转移到tRNA或ATP焦磷酸酶反应的周转数为1.2 s-1。尽管这似乎与一种编辑机制一致,即缬氨酸从IRS - Val - AMP缓慢转移到tRNAIle,随后是快速水解步骤,就像最近发现的缬氨酰 - tRNA合成酶排斥苏氨酸的情况一样,但存在不一致之处。该方案预测,将IRS·[14C]Val - AMP与tRNAIle混合时,tRNA应该会有短暂的错酰化,使得在峰值时约10%的[14C]Val以[14C]Val - tRNAIle的形式存在。但实际发现的比例为0.8%或更低。这可能是由于IRS在错配反应过程中的水解活性高于将未结合的酶与预先形成的缬氨酸 - tRNAIle混合时所测得的活性。或者,必须考虑一种两阶段编辑机制,其中在主要编辑步骤中,大部分Val - AMP在转移到tRNA之前被破坏,而IRS对缬氨酸 - tRNAIle的水解活性是第二步编辑,用于清除任何因Val - AMP逃过第一步编辑而形成的错配tRNA。结果表明,霍普菲尔德的“动力学校正”机制与实验数据不一致。

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验