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Trans-oligomerization of duplicated aminoacyl-tRNA synthetases maintains genetic code fidelity under stress

Opened Access Trans-oligomerization of duplicated aminoacyl-tRNA synthetases maintains genetic code fidelity under stress

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Autor: Rubio Gómez, Miguel Ángel
Napolitano, Mauro
Santamaría Gómez, Javier
Ochoa de Alda, Jesús A. G.
Patterson, Carl J.
Luque Romero, Ignacio
Fecha: 2015
Publicado en: Nucleic Acids Research, 43 (20), 9905-9917.
Tipo de documento: Artículo
Resumen: Aminoacyl-tRNA synthetases (aaRSs) play a key role in deciphering the genetic message by producing charged tRNAs and are equipped with proofreading mechanisms to ensure correct pairing of tRNAs with their cognate amino acid. Duplicated aaRSs are very frequent in Nature, with 25,913 cases observed in 26,837 genomes. The oligomeric nature of many aaRSs raises the question of how the functioning and oligomerization of duplicated enzymes is organized. We characterized this issue in a model prokaryotic organism that expresses two different threonyl-tRNA synthetases, responsible for Thr-tRNAThr synthesis: one accurate and constitutively expressed (T1) and another (T2) with impaired proofreading activity that also generates mischarged Ser-tRNAThr. Low zinc promotes dissociation of dimeric T1 into monomers deprived of aminoacylation activity and simultaneous induction of T2, which is active for aminoacylation under low zinc. T2 either forms homodimers or heterodimerizes with T1 subunits that ...
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Cita: Rubio Gómez, M.Á., Napolitano, M., Santamaría Gómez, J., Ochoa de Alda, J.A.G., Patterson, C.J. y Luque Romero, I. (2015). Trans-oligomerization of duplicated aminoacyl-tRNA synthetases maintains genetic code fidelity under stress. Nucleic Acids Research, 43 (20), 9905-9917.
Tamaño: 2.830Mb
Formato: PDF

URI: http://hdl.handle.net/11441/64108

DOI: 10.1093/nar/gkv1020

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