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Double mimicry evades tRNA synthetase editing by toxic vegetable-sourced non-proteinogenic amino acid

Hundreds of non-proteinogenic (np) amino acids (AA) are found in plants and can in principle enter human protein synthesis through foods. While aminoacyl-tRNA synthetase (AARS) editing potentially provides a mechanism to reject np AAs, some have pathological associations. Co-crystal structures show...

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Detalles Bibliográficos
Autores principales: Song, Youngzee, Zhou, Huihao, Vo, My-Nuong, Shi, Yi, Nawaz, Mir Hussain, Vargas-Rodriguez, Oscar, Diedrich, Jolene K., Yates, John R., Kishi, Shuji, Musier-Forsyth, Karin, Schimmel, Paul
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5741666/
https://www.ncbi.nlm.nih.gov/pubmed/29273753
http://dx.doi.org/10.1038/s41467-017-02201-z
Descripción
Sumario:Hundreds of non-proteinogenic (np) amino acids (AA) are found in plants and can in principle enter human protein synthesis through foods. While aminoacyl-tRNA synthetase (AARS) editing potentially provides a mechanism to reject np AAs, some have pathological associations. Co-crystal structures show that vegetable-sourced azetidine-2-carboxylic acid (Aze), a dual mimic of proline and alanine, is activated by both human prolyl- and alanyl-tRNA synthetases. However, it inserts into proteins as proline, with toxic consequences in vivo. Thus, dual mimicry increases odds for mistranslation through evasion of one but not both tRNA synthetase editing systems.