The Open Biochemistry Journal

ISSN: 1874-091X ― Volume 13, 2019

A Functional Role for the Monomethylated Gln-51 and Lys-53 Residues of the 49GGQTK53 Motif of eL42 from Human 80S Ribosomes

Stéphanie Eustache1, 2, Jean-Bernard Créchet3, Tahar Bouceba4, Jun-ichi Nakayama5, Mayo Tanaka5, Mieko Suzuki5, Anne Woisard1, Pierre Tuffery2, Soria Baouz1, Codjo Hountondji1, *
1 Sorbonne Universités, UPMC Univ Paris 06, Laboratoire “Enzymologie de l’ARN”, UPMC-UR6, (Tour 32), Case courrier 60 - 4, Place Jussieu, F-75252, Paris Cedex 05, France
2 Université Paris-Diderot, Sorbonne-Paris-Cité, INSERM-UMR-S973 and RPBS, Paris, France
3 Ecole Polytechnique, Route de Saclay, F-91120 Palaiseau, France
4 Sorbonne Universités, UPMC Univ Paris 06, Institut de Biologie Paris Seine (IBPS) Plateforme d’interactions moléculaires, CNRS-FR3631; 7, Quai Saint Bernard, F-75252, Paris Cedex 05, France
5 Graduate School of Natural Sciences, Nagoya City University, 1 Yamanohata, Mizuho, Nagoya, Aichi 467-8501 Japan



We have previously demonstrated that the eukaryote-specific ribosomal protein eL42 of the human 80S ribosome contains seven monomethylated residues, among which are the Gln-51 and Lys-53 residues contained in the 47GFGGQTK53 sequence conserved in all eukaryotic 80S ribosomes. This sequence contains the methylated and universally conserved GGQ motif common for all class-1 translation termination factors responsible for stop codon recognition and for triggering the hydrolysis of the P site-bound peptidyl-tRNA. We have also recently reported a model of ribosomal ternary eL42-tRNA-eRF1 complex where specific regions of all three macromolecules (the comparably flexible GGQ domains of eRF1 and eL42 and the CCA-arm of tRNA) are involved in interactions.


Here, we have studied the interactions between recombinant eL42 and eRF1 proteins and the tRNA substrate by means of the Biacore assay, using the wild-type eL42 protein, the eL42-Δ(GGQTK) mutant (the eL42 protein whose GGQTK motif has been deleted), the single Q51E and K53Q mutants (eL42-Q51E and eL42-K53Q, respectively), as well as the double Q51A/K53A mutant (eL42-Q51A/K53A).


Our results show that the monomethylated Gln-51 and Lys-53 residues contained in the 47GFGGQTK53 sequence of eL42 and the monomethylated GGQ motif of eRF1 represents the sites of interaction between these two proteins through hydrophobic contacts between methyl groups. We also demonstrate that the interactions between eL42 and tRNA or 28S rRNA are characterized by strong binding affinities (KD values in the nanomolar or picomolar range, respectively) which argue for specific interactions. Strong interactions between eL42 and tRNA are likely to be responsible for the decrease in the poly(U)-dependent poly(Phe) synthesis activity of human 80S or E. coli 70S ribosomes in the presence of added human recombinant eL42. It is proposed that the decrease of the activity of the ribosome is caused by the sequestration of the substrate Phe-tRNAPhe by the added eL42 protein.


Interactions between the monomethylated Gln-51 and Lys-53 residues of the 49GGQTK53 motif of the human eL42 protein and the methylated GGQ motif of eRF1 are likely to play a functional role on translating human 80S ribosomes.

Keywords: eL42 protein, Human 80S ribosomes/GGQTK motif, eL42/monomethylated Gln-51, Lys-53 residues, eL42/human translation termination factor, eRF1/tRNA, 28S rRNA/binding assays, Biacore.

Article Information

Identifiers and Pagination:

Year: 2017
Volume: 11
First Page: 8
Last Page: 26
Publisher Id: TOBIOCJ-11-8
DOI: 10.2174/1874091X01711010008

Article History:

Received Date: 27/10/2016
Revision Received Date: 06/01/2017
Acceptance Date: 10/01/2017
Electronic publication date: 31/03/2017
Collection year: 2017

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© 2017 Eustache et al.

open-access license: This is an open access article distributed under the terms of the Creative Commons Attribution 4.0 International Public License (CC-BY 4.0), a copy of which is available at: This license permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

* Address correspondence to this author at the Sorbonne Universités, UPMC Univ Paris 06, Laboratoire “Enzymologie de l’ARN”, UPMC-UR6, (Tour 32), Case courrier 60 - 4, Place Jussieu, F-75252, Paris Cedex 05, France; Tel: +33144274086; Fax: +33144276151; E-mail:


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