Nature Communications (Apr 2021)
Wobble tRNA modification and hydrophilic amino acid patterns dictate protein fate
- 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
Affiliations
- Francesca Rapino
- Laboratory of Cancer Signaling, University of Liège
- Zhaoli Zhou
- Laboratory of Cancer Signaling, University of Liège
- Ana Maria Roncero Sanchez
- Laboratory of Cancer Signaling, University of Liège
- Marc Joiret
- Laboratory of Cancer Signaling, University of Liège
- Christian Seca
- Laboratory of Cancer Signaling, University of Liège
- Najla El Hachem
- Laboratory of Cancer Signaling, University of Liège
- Gianluca Valenti
- University of Liège
- Sara Latini
- Laboratory of Cancer Signaling, University of Liège
- Kateryna Shostak
- GIGA-Institute, University of Liège
- Liesbet Geris
- GIGA-Institute, University of Liège
- Ping Li
- Shanghai Key Laboratory of Molecular Imaging, Shanghai University of Medicine and Health Sciences
- Gang Huang
- Shanghai Key Laboratory of Molecular Imaging, Shanghai University of Medicine and Health Sciences
- Gabriel Mazzucchelli
- GIGA-Institute, University of Liège
- Dominique Baiwir
- GIGA-Institute, University of Liège
- Christophe J. Desmet
- GIGA-Institute, University of Liège
- Alain Chariot
- GIGA-Institute, University of Liège
- Michel Georges
- GIGA-Institute, University of Liège
- Pierre Close
- Laboratory of Cancer Signaling, University of Liège
- DOI
- https://doi.org/10.1038/s41467-021-22254-5
- Journal volume & issue
-
Vol. 12,
no. 1
pp. 1 – 14
Abstract
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.
