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新月柄杆菌的蛋白质合成延伸因子Tu和Tu.Ts:对奇霉素的敏感性及在Qβ复制酶中的活性

Protein synthesis elongation factors Tu and Tu.Ts from Caulobacter crescentus: sensitivity to kirromycin and activity in Q beta replicase.

作者信息

Stringfellow L A, Douglass J, Blumenthal T

出版信息

J Bacteriol. 1980 Jul;143(1):389-95. doi: 10.1128/jb.143.1.389-395.1980.

Abstract

The protein synthesis elongation factors Tu and Ts are responsible for binding aminoacyl-transfer ribonucleic acid (RNA) to the ribosome. In addition, they perform an undefined function, as the EF-Tu.Ts complex, in the RNA phage RNA replicases. In an effort to obtain insight into these two apparently unrelated roles, we purified the elongation factors from Caulobacter crescentus and compared them to the analogous Escherichia coli polypeptides. Although most physical and functional characteristics were found to be similar, significant differences were found in the molecular weight of EF-Ts and relative affinities of guanine nucleotides, sensitivity to trypsin cleavage, and rate of heat denaturation of EF-Tu. The antibiotic kirromycin was active with EF-Tu from both bacterial species. When C. crescentus EF-Tu.Ts was substituted for the E. coli elongation factors in Q beta phage RNA replicase, an enzyme capable of apparently normal RNA synthetic activity was formed.

摘要

蛋白质合成延伸因子Tu和Ts负责将氨酰基转移核糖核酸(RNA)与核糖体结合。此外,它们作为EF-Tu.Ts复合物,在RNA噬菌体RNA复制酶中发挥一种尚不明确的功能。为了深入了解这两种明显不相关的作用,我们从新月柄杆菌中纯化了延伸因子,并将它们与类似的大肠杆菌多肽进行比较。尽管发现大多数物理和功能特性相似,但在EF-Ts的分子量、鸟嘌呤核苷酸的相对亲和力、对胰蛋白酶切割的敏感性以及EF-Tu的热变性速率方面存在显著差异。抗生素奇霉素对这两种细菌的EF-Tu均有活性。当用新月柄杆菌的EF-Tu.Ts替代Qβ噬菌体RNA复制酶中的大肠杆菌延伸因子时,形成了一种显然具有正常RNA合成活性的酶。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5dde/294253/2da59dd5c46d/jbacter00568-0407-a.jpg

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