USP16 counteracts mono-ubiquitination of RPS27a and promotes maturation of the 40S ribosomal subunit.

ELife
Christian MontelleseUlrike Kutay

Abstract

Establishment of translational competence represents a decisive cytoplasmic step in the biogenesis of 40S ribosomal subunits. This involves final 18S rRNA processing and release of residual biogenesis factors, including the protein kinase RIOK1. To identify novel proteins promoting the final maturation of human 40S subunits, we characterized pre-ribosomal subunits trapped on RIOK1 by mass spectrometry, and identified the deubiquitinase USP16 among the captured factors. We demonstrate that USP16 constitutes a component of late cytoplasmic pre-40S subunits that promotes the removal of ubiquitin from an internal lysine of ribosomal protein RPS27a/eS31. USP16 deletion leads to late 40S subunit maturation defects, manifesting in incomplete processing of 18S rRNA and retarded recycling of late-acting ribosome biogenesis factors, revealing an unexpected contribution of USP16 to the ultimate step of 40S synthesis. Finally, ubiquitination of RPS27a appears to depend on active translation, pointing at a potential connection between 40S maturation and protein synthesis.

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Citations

Aug 29, 2020·Proceedings of the National Academy of Sciences of the United States of America·Ye ZhouGustavo M Silva
Aug 4, 2020·ELife·Niladri K SinhaRachel Green
Dec 10, 2020·Viruses·Marina IkedaMasahiro Fujimuro
Nov 20, 2020·Nature·Michael AmeismeierRoland Beckmann
Apr 29, 2021·ELife·Laura PlassartCelia Plisson-Chastang

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Methods Mentioned

BETA
deubiquitination
ubiquitination
affinity purification
affinity purifications
pull down
pull-downs
pull-down
transfection
Tandem affinity purification
genotyping

Software Mentioned

Proteowizzard
tide
peptideProphet
msconvert

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