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A‐to‐I editing on tRNAs: Biochemical, biological and evolutionary implications
Author(s) -
Torres Adrian Gabriel,
Piñeyro David,
Filonava Liudmila,
Stracker Travis H.,
Batlle Eduard,
Ribas de Pouplana Lluis
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.09.025
Subject(s) - inosine , deamination , biology , transfer rna , genetic code , nucleotide , computational biology , enzyme , rna , genetics , biochemistry , dna , gene
Inosine on transfer RNAs (tRNAs) are post‐transcriptionally formed by a deamination mechanism of adenosines at positions 34, 37 and 57 of certain tRNAs. Despite its ubiquitous nature, the biological role of inosine in tRNAs remains poorly understood. Recent developments in the study of nucleotide modifications are beginning to indicate that the dynamics of such modifications are used in the control of specific genetic programs. Likewise, the essentiality of inosine‐modified tRNAs in genome evolution and animal biology is becoming apparent. Here we review our current understanding on the role of inosine in tRNAs, the enzymes that catalyze the modification and the evolutionary link between such enzymes and other deaminases.

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