Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 114, Issue 49, Pages 12934-12939Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1707674114
Keywords
2 '-O-methylation; fibrillarin; ribosomal RNA; translational control; RNA epigenetics
Categories
Funding
- Agence Nationale pour la Recherche [RIBOMETH ANR-13-BSV8-0012-01, PC201507]
- Programme d'Actions Integrees de Recherche RiboTEM (PAIR)
- Programme d'Actions Integrees de Recherche RiboTEM (Institut National du Cancer)
- Programme d'Actions Integrees de Recherche RiboTEM (Fondation ARC pour la Recherche sur le Cancer)
- Programme d'Actions Integrees de Recherche RiboTEM (Ligue Nationale Contre le Cancer)
- Ligue Nationale Contre le Cancer
- Ligue Contre le Cancer, Comite Departemental de la Drome, du Rhone, du Puy-de-Dome, et de l'Allier
- Fondation ARC pour la Recherche sur le Cancer
- French Ministry for Research and Education
- Agence Nationale de la Recherche -Deutsche Forschungsgemeinschaft [ANR-13-ISV8-0001/HE 3397/8-1]
- ProFi Grant [ANR-10-INBS-08-01]
- European Research Council [294312]
- Russian Government Program of Competitive Growth of Kazan Federal University
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Ribosomal RNAs (rRNAs) are main effectors of messenger RNA (mRNA) decoding, peptide-bond formation, and ribosome dynamics during translation. Ribose 2'-O-methylation (2'-O-Me) is the most abundant rRNA chemical modification, and displays a complex pattern in rRNA. 2'-O-Me was shown to be essential for accurate and efficient protein synthesis in eukaryotic cells. However, whether rRNA 2'-O-Me is an adjustable feature of the human ribosome and a means of regulating ribosome function remains to be determined. Here we challenged rRNA 2'-O-Me globally by inhibiting the rRNA methyl-transferase fibrillarin in human cells. Using RiboMethSeq, a nonbiased quantitative mapping of 2'-O-Me, we identified a repertoire of 2'-O-Me sites subjected to variation and demonstrate that functional domains of ribosomes are targets of 2'-O-Me plasticity. Using the cricket paralysis virus internal ribosome entry site element, coupled to in vitro translation, we show that the intrinsic capability of ribosomes to translate mRNAs is modulated through a 2'-O-Me pattern and not by nonribosomal actors of the translational machinery. Our data establish rRNA 2'-O-Me plasticity as a mechanism providing functional specificity to human ribosomes.
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