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

Stefan Gerhardy, Michaela Oborská-Oplová, Ludovic Gillet, Richard Börner, Rob Van Nues, Alexander Leitner, Erich Michel, Janusz J. Petkowski, Sander Granneman, Roland K. O. Sigel, Ruedi Aebersold, Vikram Govind Panse

Research output: Contribution to journalArticlepeer-review


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 Förster 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.
Original languageEnglish
Article number4696
Number of pages16
JournalNature Communications
Publication statusPublished - 4 Aug 2021


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