苯丙氨酸
亮氨酸
生物化学
氨基酸
大肠杆菌
精氨酸
酪氨酸
赖氨酸
色氨酸
化学
生物
基因
作者
John W. Tobias,Thomas E. Shrader,Gabrielle Rocap,Alexander Varshavsky
出处
期刊:Science
[American Association for the Advancement of Science]
日期:1991-11-29
卷期号:254 (5036): 1374-1377
被引量:537
标识
DOI:10.1126/science.1962196
摘要
The N-end rule relates the in vivo half-life of a protein to the identity of its amino-terminal residue. Distinct versions of the N-end rule operate in all eukaryotes examined. It is shown that the bacterium Escherichia coli also has the N-end rule pathway. Amino-terminal arginine, lysine, leucine, phenylalanine, tyrosine, and tryptophan confer 2-minute half-lives on a test protein; the other amino-terminal residues confer greater than 10-hour half-lives on the same protein. Amino-terminal arginine and lysine are secondary destabilizing residues in E. coli because their activity depends on their conjugation to the primary destabilizing residues leucine or phenylalanine by leucine, phenylalanine-transfer RNA-protein transferase. The adenosine triphosphate-dependent protease Clp (Ti) is required for the degradation of N-end rule substrates in E. coli .
科研通智能强力驱动
Strongly Powered by AbleSci AI