Key result
Single-molecule fluorescence tracking revealed that peptide release induces a post-termination rotated ribosomal state, acting as the crucial intermediate for ribosome recycling.
The study identifies the post-termination rotated state of the ribosome as the crucial intermediate for the transition from termination to recycling in bacteria.
No immediate clinical implications; leaves open whether this bacterial ribosomal intermediate applies to eukaryotic or mitochondrial translation.
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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Prabhakar et al. (2017) studied this question. Single-molecule fluorescence tracking revealed that peptide release induces a post-termination rotated ribosomal state, acting as the crucial intermediate for ribosome recycling.
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