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

Cited by 21 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献

同舟云学术

1.学者识别学者识别

2.学术分析学术分析

3.人才评估人才评估

"同舟云学术"是以全球学者为主线,采集、加工和组织学术论文而形成的新型学术文献查询和分析系统,可以对全球学者进行文献检索和人才价值评估。用户可以通过关注某些学科领域的顶尖人物而持续追踪该领域的学科进展和研究前沿。经过近期的数据扩容,当前同舟云学术共收录了国内外主流学术期刊6万余种,收集的期刊论文及会议论文总量共计约1.5亿篇,并以每天添加12000余篇中外论文的速度递增。我们也可以为用户提供个性化、定制化的学者数据。欢迎来电咨询!咨询电话:010-8811{复制后删除}0370

www.globalauthorid.com

TOP

Copyright © 2019-2024 北京同舟云网络信息技术有限公司
京公网安备11010802033243号  京ICP备18003416号-3