Another burst of smoke: Atomic resolution structures of RF3 bound to the ribosome

McDonald, Megan; Green, Rachel

doi:10.1261/rna.032011.111

Cited by 2 publications

(1 citation statement)

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“…Nonetheless, RF3 is nonessential for cell viability (Grentzmann et al, 1994; O’Connor, 2015), and only a subset of bacterial species have RF3 in their genomes (Margus et al, 2007). This absence suggests that RF3 is not part of a conserved mechanism of termination and that it might merely enhance termination and recycling efficiency (Koutmou et al, 2014; McDonald and Green, 2012). …”

Section: Introductionmentioning

confidence: 99%

Post-termination Ribosome Intermediate Acts as the Gateway to Ribosome Recycling

et al. 2017

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Summary During termination of translation, the nascent peptide is first released from the ribosome, which must be subsequently disassembled into subunits via a process known as ribosome recycling. In bacteria, termination and recycling are mediated by 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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