Puf6 primes 60S pre-ribosome nuclear export at low temperature.

Productive ribosomal RNA (rRNA) compaction during ribosome assembly necessitates establishing correct tertiary contacts between distant secondary structure elements. Here, we quantify the response of the yeast proteome to low temperature (LT), a condition where aberrant mis-paired RNA folding intermediates accumulate. We show that, at LT, yeast cells globally boost production ...
of their ribosome assembly machinery. We find that the LT-induced assembly factor, Puf6, binds to the nascent catalytic RNA-rich subunit interface within the 60S pre-ribosome, at a site that eventually loads the nuclear export apparatus. Ensemble Foerster resonance energy transfer studies show that Puf6 mimics the role of Mg2+ to usher a unique long-range tertiary contact to compact rRNA. At LT, puf6 mutants accumulate 60S pre-ribosomes in the nucleus, thus unveiling Puf6-mediated rRNA compaction as a critical temperature-regulated rescue mechanism that counters rRNA misfolding to prime export competence.
Mesh Terms:
Active Transport, Cell Nucleus, Cell Nucleus, Cold Temperature, GTP Phosphohydrolases, Mutation, Protein Binding, Protein Interaction Domains and Motifs, Proteome, RNA Folding, RNA Precursors, RNA, Ribosomal, RNA-Binding Proteins, Ribosome Subunits, Large, Eukaryotic, Ribosomes, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins
Nat Commun
Date: Dec. 04, 2020
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