氨基酸
生物化学
泛素
融合蛋白
酿酒酵母
化学
酵母
肽序列
生物
残留物(化学)
基因
重组DNA
作者
Andreas Bachmair,Daniel Finley,Alexander Varshavsky
出处
期刊:Science
[American Association for the Advancement of Science (AAAS)]
日期:1986-10-10
卷期号:234 (4773): 179-186
被引量:1928
标识
DOI:10.1126/science.3018930
摘要
When a chimeric gene encoding a ubiquitin-β-galactosidase fusion protein is expressed in the yeast Saccharomyces cerevisiae , ubiquitin is cleaved off the nascent fusion protein, yielding a deubiquitinated β-galactosidase (βgal). With one exception, this cleavage takes place regardless of the nature of the amino acid residue of βgal at the ubiquitin-βgal junction, thereby making it possible to expose different residues at the amino-termini of the otherwise identical βgal proteins. The βgal proteins thus designed have strikingly different half-lives in vivo, from more than 20 hours to less than 3 minutes, depending on the nature of the amino acid at the amino-terminus of βgal. The set of individual amino acids can thus be ordered with respect to the half-lives that they confer on βgal when present at its amino-terminus (the "N-end rule"). The currently known amino-terminal residues in long-lived, noncompartmentalized intracellular proteins from both prokaryotes and eukaryotes belong exclusively to the stabilizing class as predicted by the N-end rule. The function of the previously described posttranslational addition of single amino acids to protein amino-termini may also be accounted for by the N-end rule. Thus the recognition of an amino-terminal residue in a protein may mediate both the metabolic stability of the protein and the potential for regulation of its stability.
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