DIFFERENTIAL EFFECTS OF 2 INTERFERON-INDUCED TRANSLATIONAL INHIBITORS ON INITIATION OF PROTEIN-SYNTHESIS

被引：30

作者：

CHERNAJOVSKY, Y

KIMCHI, A

SCHMIDT, A

ZILBERSTEIN, A

REVEL, M

机构：

[1] Department of Virology, Weizmann Institute of Science, Rehovot

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1979年 / 96卷 / 01期

关键词：

D O I：

10.1111/j.1432-1033.1979.tb13010.x

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

At least two different mechanisms for the inhibition of mRNA translation operate in extracts of interferon‐treated L cells. One is mediated by an interferon‐induced protein kinase which, when activated by double‐stranded RNA and ATP, phosphorylates the small subunit of initiation factor eIF‐2. Addition of the purified interferon‐induced protein kinase to L cell extracts, strongly reduces the amount of methionyl‐tRNA bound to 40‐S ribosomal subunits. The second translational inhibition is due to the synthesis of (2′‐5′)oligo(adenylate) by interferon‐induced enzyme E. The oligonucleotide in turn activates a ribonuclease F constitutively present in L cells. Addition of the purified nuclease with its oligonucleotide activator to L cell extracts produces a strong decrease in polyribosome formation and an accumulation of initiation complex. These experiments differentiate the effects of the two interferon‐induced inhibitors on mRNA translation. Copyright © 1979, Wiley Blackwell. All rights reserved

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页码：35 / 41

页数：7

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