On the mechanism of chloramphenicol-induced changes in the photoinduced affinity labeling of Escherichia coli ribosomes by puromycin. Evidence for puromycin and chloramphenicol sites on the 30S subunit.
On the mechanism of chloramphenicol-induced changes in the photoinduced affinity labeling of Escherichia coli ribosomes by puromycin. Evidence for puromycin and chloramphenicol sites on the 30S subunit.
复制标题
氯霉素诱导嘌呤霉素对大肠杆菌核糖体光诱导亲和标记变化的机制研究。
DOI：
10.1021/bi00578a004
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发表时间：
1979
期刊：
影响因子：
2.9
通讯作者：
W. A. Strycharz
中科院分区：
文献类型：
--
作者：
G. P. Grant;B. Cooperman;W. A. Strycharz
P. G. Grant, BS Cooperman,* and WA Strycharz abstract: Chloramphenicol has been shown to cause a major change in the ribosomal protein labeling pattern when Es-cherichia coli ribosomes are photolyzed in thepresence of radioactive puromycin. In the absence of chloramphenicol, the major labeled protein is L23, while in itspresence S14 becomes the major labeled protein [Grant, P. G., Strycharz, WA, Jaynes, E. N., Jr., & Cooperman, BS (1979) Biochemistry (preceding paperin this issue)]. This paper reports a detailed investigation of this change, which has allowed the following conclusions to be drawn.(1) The labeling of S14 by puromycin proceeds from a puromycin binding site.(2) The stimulation of S14 labeling by chloramphenicol requires a specific chloramphenicol binding site.(3) Both of the above
