Journal
NATURE COMMUNICATIONS
Volume 12, Issue 1, Pages -Publisher
NATURE PORTFOLIO
DOI: 10.1038/s41467-021-24964-2
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Funding
- Boehringer Ingelheim Fonds Ph.D. fellowship program
- Marie Curie Actions for People COFUND program
- Wellcome Trust [091549]
- Medical Research Council Non-Clinical Senior Research Fellowship [MR/R008205/1]
- Swiss National Science Foundation
- Swiss National Science Foundation [310030_188527]
- NCCR in RNA and Disease
- ETH Zurich
- Novartis Foundation
- Olga Mayenfisch Stiftung
- European Research Council [EURIBIO260676]
- UZH
- Swiss National Science Foundation (SNF) [310030_188527] Funding Source: Swiss National Science Foundation (SNF)
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This study reveals that yeast cells globally increase production of ribosome assembly machinery in response to low temperature. Puf6 binds to the nascent catalytic RNA-rich subunit interface within the 60S pre-ribosome, mimicking the role of Mg2+ to facilitate long-range tertiary contacts for compacting rRNA.
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 Forster 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.
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