Cloning and functional analysis of the arginyl-tRNA-protein transferase gene ATE1 of Saccharomyces cerevisiae.
Cloning and functional analysis of the arginyl-tRNA-protein transferase gene ATE1 of Saccharomyces cerevisiae.
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DOI：
10.1016/s0021-9258(19)39136-7
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发表时间：
1990-05
期刊：
影响因子：
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通讯作者：
E. Balzi;M. Choder;Wei Ning Chen;Alexander Varshavsky;André Goffeau
中科院分区：
文献类型：
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作者：
E. Balzi;M. Choder;Wei Ning Chen;Alexander Varshavsky;André Goffeau
氨酰-tRNA-蛋白转移酶（Arg-转移酶）催化特定氨基酸与受体蛋白的氨基末端的翻译后缀合。这些酶在真核生物中的功能已显示涉及使不稳定氨基酸与短寿命蛋白质的氨基末端缀合，这些反应是蛋白质降解的N-末端规则途径的一部分（贡达，D. K.，Bachmair，A.，翁宁岛托拜厄斯，J.W.，Lane，W.美国，和Varshavsky，A.（1989）J.Biol.Chem.264，16700-16712）。我们克隆了酿酒酵母的ATE 1基因，该基因编码N-乙酰-tRNA-蛋白转移酶。ATE 1产生约1.6-脱氢酶mRNA，编码503个残基的蛋白质。酵母ATE 1基因在缺乏Arg-转移酶的大肠杆菌中的表达被用于显示ATE 1蛋白具有Arg-转移酶活性。E1突变体是可行的，但缺乏Arg-转移酶活性，不能降解那些底物的N-末端规则的途径，开始与残基识别的Arg-转移酶。
Aminoacyl-tRNA-protein transferases (Arg-transferases) catalyze post-translational conjugation of specific amino acids to the amino termini of acceptor proteins. A function of these enzymes in eukaryotes has been shown to involve the conjugation of destabilizing amino acids to the amino termini of short-lived proteins, these reactions being a part of the N-end rule pathway of protein degradation (Gonda, D. K., Bachmair, A., Wünning, I., Tobias, J. W., Lane, W. S., and Varshavsky, A. (1989) J. Biol. Chem. 264, 16700-16712). We have cloned the ATE1 gene of the yeast Saccharomyces cerevisiae which encodes arginyl-tRNA-protein transferase. ATE1 gives rise to a approximately 1.6-kilobase mRNA and codes for a 503-residue protein. Expression of the yeast ATE1 gene in Escherichia coli, which lacks Arg-transferases, was used to show that the ATE1 protein possesses the Arg-transferase activity. Null ate1 mutants are viable but lack the Arg-transferase activity and are unable to degrade those substrates of the N-end rule pathway that start with residues recognized by the Arg-transferase.