Human tRNAs with inosine 34 are essential to efficiently translate eukarya-specific low-complexity proteins

Author:

Torres Adrian Gabriel1,Rodríguez-Escribà Marta1,Marcet-Houben Marina12,Santos Vieira Helaine Graziele3,Camacho Noelia1,Catena Helena1,Murillo Recio Marina1,Rafels-Ybern Àlbert1,Reina Oscar1,Torres Francisco Miguel1,Pardo-Saganta Ana4,Gabaldón Toni125,Novoa Eva Maria36,Ribas de Pouplana Lluís15ORCID

Affiliation:

1. Institute for Research in Biomedicine, The Barcelona Institute of Science and Technology, Barcelona, Catalonia 08028, Spain

2. Barcelona Supercomputing Centre (BSC-CNS), Barcelona, Catalonia 08034, Spain

3. Centre for Genomic Regulation, The Barcelona Institute of Science and Technology, Barcelona, Catalonia 08003, Spain

4. Centre for Applied Medical Research (CIMA Universidad de Navarra), Pamplona 31008, Spain

5. Catalan Institution for Research and Advanced Studies, Barcelona, Catalonia 08010, Spain

6. University Pompeu Fabra, Barcelona, Catalonia 08003, Spain

Abstract

Abstract The modification of adenosine to inosine at the wobble position (I34) of tRNA anticodons is an abundant and essential feature of eukaryotic tRNAs. The expansion of inosine-containing tRNAs in eukaryotes followed the transformation of the homodimeric bacterial enzyme TadA, which generates I34 in tRNAArg and tRNALeu, into the heterodimeric eukaryotic enzyme ADAT, which modifies up to eight different tRNAs. The emergence of ADAT and its larger set of substrates, strongly influenced the tRNA composition and codon usage of eukaryotic genomes. However, the selective advantages that drove the expansion of I34-tRNAs remain unknown. Here we investigate the functional relevance of I34-tRNAs in human cells and show that a full complement of these tRNAs is necessary for the translation of low-complexity protein domains enriched in amino acids cognate for I34-tRNAs. The coding sequences for these domains require codons translated by I34-tRNAs, in detriment of synonymous codons that use other tRNAs. I34-tRNA-dependent low-complexity proteins are enriched in functional categories related to cell adhesion, and depletion in I34-tRNAs leads to cellular phenotypes consistent with these roles. We show that the distribution of these low-complexity proteins mirrors the distribution of I34-tRNAs in the phylogenetic tree.

Funder

Ministry of Economy and Competitiveness

Australian Research Council

Horizon 2020

Publisher

Oxford University Press (OUP)

Subject

Genetics

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