A role for the universal Kae1/Qri7/YgjD (COG0533) family in tRNA modification
Autor: | El Yacoubi, Basma, Hatin, Isabelle, Deutsch, Christopher, Kahveci, Tamer, Rousset, Jean-Pierre, Iwata-Reuyl, Dirk, G Murzin, Alexey, de Crécy-Lagard, Valérie |
---|---|
Přispěvatelé: | Institut de génétique et microbiologie [Orsay] (IGM), Université Paris-Sud - Paris 11 (UP11)-Centre National de la Recherche Scientifique (CNRS) |
Jazyk: | angličtina |
Rok vydání: | 2011 |
Předmět: |
MESH: Genetic Complementation Test
Adenosine Saccharomyces cerevisiae Proteins Genetic Complementation Test Metalloendopeptidases MESH: Metalloendopeptidases MESH: Mitochondrial Proteins Saccharomyces cerevisiae MESH: Multiprotein Complexes MESH: Adenosine MESH: RNA Transfer MESH: Saccharomyces cerevisiae Article Mitochondrial Proteins MESH: Saccharomyces cerevisiae Proteins [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology RNA Transfer Multiprotein Complexes [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology |
Zdroj: | EMBO Journal EMBO Journal, EMBO Press, 2011, 30 (5), pp.882-93. ⟨10.1038/emboj.2010.363⟩ |
ISSN: | 0261-4189 1460-2075 |
Popis: | International audience; The YgjD/Kae1 family (COG0533) has been on the top-10 list of universally conserved proteins of unknown function for over 5 years. It has been linked to DNA maintenance in bacteria and mitochondria and transcription regulation and telomere homeostasis in eukaryotes, but its actual function has never been found. Based on a comparative genomic and structural analysis, we predicted this family was involved in the biosynthesis of N(6)-threonylcarbamoyl adenosine, a universal modification found at position 37 of tRNAs decoding ANN codons. This was confirmed as a yeast mutant lacking Kae1 is devoid of t(6)A. t(6)A(-) strains were also used to reveal that t(6)A has a critical role in initiation codon restriction to AUG and in restricting frameshifting at tandem ANN codons. We also showed that YaeZ, a YgjD paralog, is required for YgjD function in vivo in bacteria. This work lays the foundation for understanding the pleiotropic role of this universal protein family. |
Databáze: | OpenAIRE |
Externí odkaz: |