4.8 Article

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

期刊

CELL REPORTS
卷 20, 期 1, 页码 161-172

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CELL PRESS
DOI: 10.1016/j.celrep.2017.06.028

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资金

  1. NIH [GM51266, GM099687]
  2. NIH Molecular Biophysics Training Grant [T32-GM008294]
  3. Stanford Interdisciplinary Graduate Fellowship
  4. Stanford Bio-X Fellowship

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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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