期刊
CELL REPORTS
卷 20, 期 1, 页码 161-172出版社
CELL PRESS
DOI: 10.1016/j.celrep.2017.06.028
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类别
资金
- NIH [GM51266, GM099687]
- NIH Molecular Biophysics Training Grant [T32-GM008294]
- Stanford Interdisciplinary Graduate Fellowship
- Stanford Bio-X Fellowship
During termination of translation, the nascent peptide is first released from the ribosome, which must be subsequently disassembled into subunits in a process known as ribosome recycling. In bacteria, termination and recycling are mediated by the translation factors RF, RRF, EF-G, and IF3, but their precise roles have remained unclear. Here, we use single-molecule fluorescence to track the conformation and composition of the ribosome in real time during termination and recycling. Our results show that peptide release by RF induces a rotated ribosomal conformation. RRF binds to this rotated intermediate to form the substrate for EF-G that, in turn, catalyzes GTP-dependent subunit disassembly. After the 50S subunit departs, IF3 releases the deacylated tRNA from the 30S subunit, thus preventing reassembly of the 70S ribosome. Our findings reveal the post-termination rotated state as the crucial intermediate in the transition from termination to recycling.
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