‘View From A Bridge’: A New Perspective on Eukaryotic rRNA Base Modification

Eukaryotic rRNA are modified frequently, although the diversity of modifications is low: in yeast rRNA, there are only 12 different types out of a possible natural repertoire exceeding 112. All nine rRNA base methyltransferases (MTases) and one acetyltransferase have recently been identified in budd...

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Bibliographic Details
Published in:Trends in biochemical sciences (Amsterdam. Regular ed.) 2015-10, Vol.40 (10), p.560-575
Main Authors: Sharma, Sunny, Lafontaine, Denis L.J.
Format: Article
Language:English
Subjects:
acetylation
intersubunit bridge
methylation
nucleolus
Protein Biosynthesis
protein synthesis
ribosome assembly
Ribosomes - metabolism
RNA, Fungal - metabolism
RNA, Ribosomal - metabolism
RNA, Transfer - metabolism
rRNA modification
Saccharomyces cerevisiae - metabolism
translation
yeast
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Summary:Eukaryotic rRNA are modified frequently, although the diversity of modifications is low: in yeast rRNA, there are only 12 different types out of a possible natural repertoire exceeding 112. All nine rRNA base methyltransferases (MTases) and one acetyltransferase have recently been identified in budding yeast, and several instances of crosstalk between rRNA, tRNA, and mRNA modifications are emerging. Although the machinery has largely been identified, the functions of most rRNA modifications remain to be established. Remarkably, a eukaryote-specific bridge, comprising a single ribosomal protein (RP) from the large subunit (LSU), contacts four rRNA base modifications across the ribosomal subunit interface, potentially probing for their presence. We hypothesize in this article that long-range allosteric communication involving rRNA modifications is taking place between the two subunits during translation or, perhaps, the late stages of ribosome assembly. All nine rRNA base methyltransferases have been identified in budding yeast. An 18S rRNA acetyltransferase modifies tRNAs with a specific adaptor. Four methyltransferases are stabilized by a common coactivator. A eukaryote-specific bridge monitors base modifications across the subunit interface.
ISSN:0968-0004
1362-4326
DOI:10.1016/j.tibs.2015.07.008