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增加翻译阻遏物与RNA亲和力的突变。

Mutations that increase the affinity of a translational repressor for RNA.

作者信息

Lim F, Peabody D S

机构信息

Department of Cell Biology, University of New Mexico School of Medicine, Albuquerque 87131.

出版信息

Nucleic Acids Res. 1994 Sep 11;22(18):3748-52. doi: 10.1093/nar/22.18.3748.

Abstract

The coat protein of the RNA bacteriophage MS2 is a specific RNA binding protein that represses translation of the viral replicase gene during the infection cycle. As an approach to characterizing the RNA-binding site of coat protein we have isolated a series of coat mutants that suppress the effects of a mutation in the translational operator. Each of the mutants exhibits a super-repressor phenotype, more tightly repressing both the mutant and wild-type operators than does the wild-type protein. The variant coat proteins were purified and subjected to filter binding assays to determine their affinities for the mutant and wild-type operators. Each protein binds the operators from 3 to 7.5-fold more tightly than normal coat protein. The amino acid substitutions seem to extend the normal binding site by introducing new interactions with RNA.

摘要

RNA噬菌体MS2的外壳蛋白是一种特异性RNA结合蛋白,在感染周期中可抑制病毒复制酶基因的翻译。作为表征外壳蛋白RNA结合位点的一种方法,我们分离出了一系列外壳突变体,这些突变体可抑制翻译操纵子中一个突变的影响。每个突变体都表现出超阻遏物表型,与野生型蛋白相比,能更紧密地抑制突变型和野生型操纵子。对这些变异的外壳蛋白进行了纯化,并进行滤膜结合试验以确定它们对突变型和野生型操纵子的亲和力。每种蛋白与操纵子的结合紧密程度比正常外壳蛋白高3至7.5倍。氨基酸取代似乎通过引入与RNA的新相互作用来扩展正常结合位点。

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