Pseudouridylation at Position 32 of Mitochondrial and Cytoplasmic tRNAs Requires Two Distinct Enzymes in Saccharomyces cerevisiae - Cancéropôle du Grand Est Accéder directement au contenu
Article Dans Une Revue Journal of Biological Chemistry Année : 2004

Pseudouridylation at Position 32 of Mitochondrial and Cytoplasmic tRNAs Requires Two Distinct Enzymes in Saccharomyces cerevisiae

Résumé

Cytoplasmic and mitochondrial tRNAs contain several pseudouridylation sites, and the tRNA:-synthase acting at position 32 had not been identified in Saccha-romyces cerevisiae. By combining genetic and biochemical analyses, we demonstrate that two enzymes, Rib2/ Pus8p and Pus9p, are required for 32 formation in cytoplasmic and mitochondrial tRNAs, respectively. Pus9p acts mostly in mitochondria, and Rib2/Pus8p is strictly cytoplasmic. This is the first case reported so far of two distinct tRNA modification enzymes acting at the same position but present in two different compartments. This peculiarity may be the consequence of a gene fusion that occurred during yeast evolution. Indeed , Rib2/Pus8p displays two distinct catalytic activities involved in completely unrelated metabolism: its C-terminal domain has a DRAP-deaminase activity required for riboflavin biogenesis in the cytoplasm, whereas its N-terminal domain carries the tRNA:32-synthase activity. Pus9p has only a tRNA:32-synthase activity and contains a characteristic mitochondrial targeting sequence at its N terminus. These results are discussed in terms of RNA:-synthase evolution.
Fichier principal
Vignette du fichier
Behm-Ansmant et al., 2004, JBC, Pus8_9.pdf (468.49 Ko) Télécharger le fichier
Origine : Fichiers éditeurs autorisés sur une archive ouverte
Loading...

Dates et versions

hal-01738505 , version 1 (20-03-2018)

Identifiants

Citer

Isabelle Behm-Ansmant, Henri H. Grosjean, Séverine Massenet, Yuri Motorin, Christiane Branlant. Pseudouridylation at Position 32 of Mitochondrial and Cytoplasmic tRNAs Requires Two Distinct Enzymes in Saccharomyces cerevisiae. Journal of Biological Chemistry, 2004, 279 (51), pp.52998-53006. ⟨10.1074/jbc.M409581200⟩. ⟨hal-01738505⟩
75 Consultations
109 Téléchargements

Altmetric

Partager

Gmail Facebook X LinkedIn More