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Title

TRNA deamination by ADAT requires substrate-specific recognition mechanisms and can be inhibited by tRFs

AuthorsRoura Frigolé, Helena; Camacho, Noelia; Castellví Coma, María; Fernández-Lozano, Carla; García-Lema, Jorge; Rafels-Ybern, Àlbert; Canals, Albert ; Coll, Miquel ; Ribas de Pouplana, Lluís
KeywordsADAT
Deaminase
tRNA
Adenosine
Inosine
tRF
Issue Date2019
PublisherCold Spring Harbor Laboratory Press
CitationRNA 25: 607-619 (2019)
AbstractAdenosine deaminase acting on transfer RNA (ADAT) is an essential eukaryotic enzyme that catalyzes the deamination of adenosine to inosine at the first position of tRNA anticodons. Mammalian ADATs modify eight different tRNAs, having increased their substrate range from a bacterial ancestor that likely deaminated exclusively tRNAArg. Here we investigate the recognition mechanisms of tRNAArg and tRNAAla by human ADAT to shed light on the process of substrate expansion that took place during the evolution of the enzyme. We show that tRNA recognition by human ADAT does not depend on conserved identity elements, but on the overall structural features of tRNA. We find that ancestral-like interactions are conserved for tRNAArg, while eukaryote-specific substrates use alternative mechanisms. These recognition studies show that human ADAT can be inhibited by tRNA fragments in vitro, including naturally occurring fragments involved in important regulatory pathways.
Publisher version (URL)http://dx.doi.org/10.1261/rna.068189.118
URIhttp://hdl.handle.net/10261/201910
DOI10.1261/rna.068189.118
ISSN1355-8382
E-ISSN1469-9001
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