期刊
CELL
卷 111, 期 1, 页码 129-140出版社
CELL PRESS
DOI: 10.1016/S0092-8674(02)00938-8
关键词
-
资金
- NIGMS NIH HHS [GM59140, GM17129] Funding Source: Medline
- CGH CDC HHS [GH60429] Funding Source: Medline
Ribosome recycling factor (RRF) disassembles post-termination complexes in conjunction with elongation factor EF-G, liberating ribosomes for further rounds of translation. The striking resemblance of its L-shaped structure to that of tRNA has suggested that the mode of action of RRF may be based on mimicry of tRNA. Directed hydroxyl radical probing of 16S and 23S rRNA from Fe(II) tethered to ten positions on the surface of E. coli RRF constrains it to a well-defined location in the subunit interface cavity. Surprisingly, the orientation of RRF in the ribosome differs markedly from any of those previously observed for tRNA, suggesting that structural mimicry does not necessarily reflect functional mimicry.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据