Wobble tRNA modification and hydrophilic amino acid patterns dictate protein fate

Wobble uridine (U34) tRNA modifications are important for the decoding of AA-ending codons. Here the authors show that while the U34-codon content of mRNAs are predictive of changes in ribosome translation elongation, the resulting outcome in protein expression also relies on specific hydrophilic mo...

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Autores principales:	Francesca Rapino, Zhaoli Zhou, Ana Maria Roncero Sanchez, Marc Joiret, Christian Seca, Najla El Hachem, Gianluca Valenti, Sara Latini, Kateryna Shostak, Liesbet Geris, Ping Li, Gang Huang, Gabriel Mazzucchelli, Dominique Baiwir, Christophe J. Desmet, Alain Chariot, Michel Georges, Pierre Close
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/c065fd32e605402394e0d38dfe8266a8
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spelling	oai:doaj.org-article:c065fd32e605402394e0d38dfe8266a82021-12-02T15:51:04ZWobble tRNA modification and hydrophilic amino acid patterns dictate protein fate10.1038/s41467-021-22254-52041-1723https://doaj.org/article/c065fd32e605402394e0d38dfe8266a82021-04-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-22254-5https://doaj.org/toc/2041-1723Wobble uridine (U34) tRNA modifications are important for the decoding of AA-ending codons. Here the authors show that while the U34-codon content of mRNAs are predictive of changes in ribosome translation elongation, the resulting outcome in protein expression also relies on specific hydrophilic motifs-dependent protein aggregation and clearance.Francesca RapinoZhaoli ZhouAna Maria Roncero SanchezMarc JoiretChristian SecaNajla El HachemGianluca ValentiSara LatiniKateryna ShostakLiesbet GerisPing LiGang HuangGabriel MazzucchelliDominique BaiwirChristophe J. DesmetAlain ChariotMichel GeorgesPierre CloseNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-14 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Francesca Rapino Zhaoli Zhou Ana Maria Roncero Sanchez Marc Joiret Christian Seca Najla El Hachem Gianluca Valenti Sara Latini Kateryna Shostak Liesbet Geris Ping Li Gang Huang Gabriel Mazzucchelli Dominique Baiwir Christophe J. Desmet Alain Chariot Michel Georges Pierre Close Wobble tRNA modification and hydrophilic amino acid patterns dictate protein fate
description	Wobble uridine (U34) tRNA modifications are important for the decoding of AA-ending codons. Here the authors show that while the U34-codon content of mRNAs are predictive of changes in ribosome translation elongation, the resulting outcome in protein expression also relies on specific hydrophilic motifs-dependent protein aggregation and clearance.
format	article
author	Francesca Rapino Zhaoli Zhou Ana Maria Roncero Sanchez Marc Joiret Christian Seca Najla El Hachem Gianluca Valenti Sara Latini Kateryna Shostak Liesbet Geris Ping Li Gang Huang Gabriel Mazzucchelli Dominique Baiwir Christophe J. Desmet Alain Chariot Michel Georges Pierre Close
author_facet	Francesca Rapino Zhaoli Zhou Ana Maria Roncero Sanchez Marc Joiret Christian Seca Najla El Hachem Gianluca Valenti Sara Latini Kateryna Shostak Liesbet Geris Ping Li Gang Huang Gabriel Mazzucchelli Dominique Baiwir Christophe J. Desmet Alain Chariot Michel Georges Pierre Close
author_sort	Francesca Rapino
title	Wobble tRNA modification and hydrophilic amino acid patterns dictate protein fate
title_short	Wobble tRNA modification and hydrophilic amino acid patterns dictate protein fate
title_full	Wobble tRNA modification and hydrophilic amino acid patterns dictate protein fate
title_fullStr	Wobble tRNA modification and hydrophilic amino acid patterns dictate protein fate
title_full_unstemmed	Wobble tRNA modification and hydrophilic amino acid patterns dictate protein fate
title_sort	wobble trna modification and hydrophilic amino acid patterns dictate protein fate
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/c065fd32e605402394e0d38dfe8266a8
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Wobble tRNA modification and hydrophilic amino acid patterns dictate protein fate

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