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- W2063089090 abstract "Eukaryotic ribosomes are preassembled in the nucleus and mature in the cytoplasm. Release of the antiassociation factor Tif6 by the translocase-like guanosine triphosphatase Efl1 is a critical late maturation step. In this paper, we show that a loop of Rpl10 that embraces the P-site transfer ribonucleic acid was required for release of Tif6, 90 Å away. Mutations in this P-site loop blocked 60S maturation but were suppressed by mutations in Tif6 or Efl1. Molecular dynamics simulations of the mutant Efl1 proteins suggest that they promote a conformation change in Efl1 equivalent to changes that elongation factor G and eEF2 undergo during translocation. These results identify molecular signaling from the P-site to Tif6 via Efl1, suggesting that the integrity of the P-site is interrogated during maturation. We propose that Efl1 promotes a functional check of the integrity of the 60S subunit before its first round of translation." @default.
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- W2063089090 date "2012-06-11" @default.
- W2063089090 modified "2023-10-05" @default.
- W2063089090 title "Integrity of the P-site is probed during maturation of the 60S ribosomal subunit" @default.
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- W2063089090 doi "https://doi.org/10.1083/jcb.201112131" @default.
- W2063089090 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3373404" @default.
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