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

Youngzee Song, Huihao Zhou, My-Nuong Vo, Yi Shi, Mir Hussain Nawaz, Oscar Vargas-Rodriguez, Jolene K. Diedrich, John R. Yates, Shuji Kishi, Karin Musier-Forsyth and Paul Schimmel ()
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Youngzee Song: The Scripps Research Institute
Huihao Zhou: The Scripps Research Institute
My-Nuong Vo: The Scripps Research Institute
Yi Shi: The Scripps Research Institute
Mir Hussain Nawaz: The Scripps Research Institute
Oscar Vargas-Rodriguez: The Ohio State University
Jolene K. Diedrich: The Scripps Research Institute
John R. Yates: The Scripps Research Institute
Shuji Kishi: The Scripps Research Institute
Karin Musier-Forsyth: The Ohio State University
Paul Schimmel: The Scripps Research Institute

Nature Communications, 2017, vol. 8, issue 1, 1-8

Abstract: Abstract 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.

Date: 2017
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DOI: 10.1038/s41467-017-02201-z

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