Abstract:
: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.
journal_name
Cell Repjournal_title
Cell reportsauthors
Prabhakar A,Capece MC,Petrov A,Choi J,Puglisi JDdoi
10.1016/j.celrep.2017.06.028subject
Has Abstractpub_date
2017-07-05 00:00:00pages
161-172issue
1issn
2211-1247pii
S2211-1247(17)30825-2journal_volume
20pub_type
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