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

Stefan Gerhardy, Michaela Oborská-Oplová, Ludovic Gillet, Richard Börner, Rob Nues, Alexander Leitner, Erich Michel, Janusz J. Petkowski, Sander Granneman, Roland K. O. Sigel, Ruedi Aebersold and Vikram Govind Panse ()
Additional contact information
Stefan Gerhardy: University of Zurich
Michaela Oborská-Oplová: University of Zurich
Ludovic Gillet: Institute of Molecular Systems Biology, ETH Zurich
Richard Börner: University of Zurich
Rob Nues: University of Edinburgh
Alexander Leitner: Institute of Molecular Systems Biology, ETH Zurich
Erich Michel: University of Zurich
Janusz J. Petkowski: Institute of Biochemistry, ETH Zurich
Sander Granneman: University of Edinburgh
Roland K. O. Sigel: University of Zurich
Ruedi Aebersold: Institute of Molecular Systems Biology, ETH Zurich
Vikram Govind Panse: University of Zurich

Nature Communications, 2021, vol. 12, issue 1, 1-16

Abstract: Abstract 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.

Date: 2021
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/s41467-021-24964-2 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-24964-2

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-021-24964-2

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().