title: Modification of the wobble uridine in bacterial and mitochondrial tRNAs reading NNA/NNG triplets of 2-codon boxes.
abstract: Posttranscriptional modification of the uridine located at the wobble position (U34) of tRNAs is crucial for optimization of translation. Defects in the U34 modification of mitochondrial-tRNAs are associated with a group of rare diseases collectively characterized by the impairment of the oxidative phosphorylation system. Retrograde signaling pathways from mitochondria to nucleus are involved in the pathophysiology of these diseases. These pathways may be triggered by not only the disturbance of the mitochondrial (mt) translation caused by hypomodification of tRNAs, but also as a result of nonconventional roles of mt-tRNAs and mt-tRNA-modifying enzymes. The evolutionary conservation of these enzymes supports their importance for cell and organismal functions. Interestingly, bacterial and eukaryotic cells respond to stress by altering the expression or activity of these tRNA-modifying enzymes, which leads to changes in the modification status of tRNAs. This review summarizes recent findings about these enzymes and sets them within the previous data context.
authors.affiliation: a Laboratory of RNA Modification and Mitochondrial Diseases ; Centro de Investigación Príncipe Felipe ; Valencia , Spain.
authors.forename: M Eugenia
authors.initials: ME
authors.lastname: Armengod
authors.forename: Salvador
authors.initials: S
authors.lastname: Meseguer
authors.forename: Magda
authors.initials: M
authors.lastname: Villarroya
authors.forename: Silvia
authors.initials: S
authors.lastname: Prado
authors.forename: Ismaïl
authors.initials: I
authors.lastname: Moukadiri
authors.forename: Rafael
authors.initials: R
authors.lastname: Ruiz-Partida
authors.forename: M José
authors.initials: MJ
authors.lastname: Garzón
authors.forename: Carmen
authors.initials: C
authors.lastname: Navarro-González
authors.forename: Ana
authors.initials: A
authors.lastname: Martínez-Zamora
mesh_terms: D000926:Anticodon / Q000378:metabolism; D002467:Cell Nucleus / Q000235:genetics / Q000378:metabolism; D003062:Codon / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000235:genetics / Q000378:metabolism; D020558:GTP Phosphohydrolases / Q000235:genetics / Q000378:metabolism; D008928:Mitochondria / Q000235:genetics / Q000378:metabolism; D009097:Multienzyme Complexes / Q000235:genetics / Q000378:metabolism; D019875:One-Carbon Group Transferases / Q000235:genetics / Q000378:metabolism; D010085:Oxidative Phosphorylation; D012313:RNA / Q000235:genetics / Q000378:metabolism*; D012323:RNA Processing, Post-Transcriptional; D000077278:RNA, Mitochondrial; D012345:RNA, Transfer, Amino Acid-Specific / Q000235:genetics / Q000378:metabolism; D015398:Signal Transduction; D014529:Uridine / Q000031:analogs & derivatives* / Q000378:metabolism*
chemical_list: C117148:5-carboxy-methylaminomethyl-2'-O-methyluridine; D000926:Anticodon; D003062:Codon; D029968:Escherichia coli Proteins; C488767:MnmC protein, E coli; D009097:Multienzyme Complexes; D000077278:RNA, Mitochondrial; D012345:RNA, Transfer, Amino Acid-Specific; D012313:RNA; C546582:MnmG protein, E coli; D019875:One-Carbon Group Transferases; D020558:GTP Phosphohydrolases; C492932:MnmE protein, E coli; D014529:Uridine
keywords: GTPBP3; MELAS; MTO1; MnmA; MnmC; MnmE; MnmG; TRMU/MTU1; TrmL; mitochondrial diseases; tRNA modification