Wobble tRNA modification and hydrophilic amino acid patterns dictate protein fate

Autor: 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
Jazyk: angličtina
Rok vydání: 2021
Předmět:
Zdroj: Nature Communications, Vol 12, Iss 1, Pp 1-14 (2021)
Druh dokumentu: article
ISSN: 2041-1723
DOI: 10.1038/s41467-021-22254-5
Popis: 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.
Databáze: Directory of Open Access Journals