大肠杆菌中异常蛋白质的降解（蛋白质分解-蛋白质结构-错译-氨基酸类似物-嘌呤霉素）
Degradation of abnormal proteins in Escherichia coli (protein breakdown-protein structure-mistranslation-amino acid analogs-puromycin).
作者信息
Goldberg A L
出版信息
Proc Natl Acad Sci U S A. 1972 Feb;69(2):422-6. doi: 10.1073/pnas.69.2.422.
Abstract
Evidence is presented that E. coli contains a mechanism for selective degradation of abnormal proteins. Unfinished polypeptides containing puromycin, proteins containing frequent errors in translation, such as those synthesized by strains containing a ram mutation or a missense suppressor, and proteins containing amino-acid analogs were degraded more rapidly than were normal cell proteins. The degradation of analog- or puromycin-containing proteins appears to be an energy-dependent process. Unlike normal proteins, such proteins were degraded at similar rates by growing and by nongrowing cells.
摘要
有证据表明大肠杆菌含有一种选择性降解异常蛋白质的机制。含有嘌呤霉素的未完成多肽、在翻译过程中频繁出错的蛋白质（例如由含有ram突变或错义抑制基因的菌株合成的蛋白质）以及含有氨基酸类似物的蛋白质，其降解速度比正常细胞蛋白质更快。含有类似物或嘌呤霉素的蛋白质的降解似乎是一个能量依赖的过程。与正常蛋白质不同，此类蛋白质在生长细胞和非生长细胞中的降解速度相似。
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