Mechanism of read-through enhancement by aminoglycosides and mefloquine

O Olga Kolosova (Department of Integrated Structural Biology, Institute of Genetics and Molecular and Cellular Biology, University of Strasbourg) Y Yury Zgadzay (Department of Integrated Structural Biology, Institute of Genetics and Molecular and Cellular Biology, University of Strasbourg) A Artem Stetsenko (Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen) A Anastasia P. Sukhinina (Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University) A Anastasia Atamas (Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen) S Shamil Validov (Laboratory of Structural Biology, Institute of Fundamental Medicine and Biology, Kazan Federal University) A Andrey Rogachev (Moscow Centre for Advanced Studies) K Konstantin Usachev (Laboratory of Structural Biology, Institute of Fundamental Medicine and Biology, Kazan Federal University) L Lasse Jenner (Department of Integrated Structural Biology, Institute of Genetics and Molecular and Cellular Biology, University of Strasbourg) S Sergey E. Dmitriev G Gulnara Yusupova (Department of Integrated Structural Biology, Institute of Genetics and Molecular and Cellular Biology, University of Strasbourg) A Albert Guskov (Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen) M Marat Yusupov (Department of Integrated Structural Biology, Institute of Genetics and Molecular and Cellular Biology, University of Strasbourg)

Abstract

Nonsense mutations are associated with numerous and diverse pathologies, yet effective treatment strategies remain elusive. A promising approach to combat these conditions involves the use of aminoglycosides, particularly in combination with stop-codon read-through enhancers, for developing drugs that can rescue the production of full-length proteins. Using X-ray crystallography and single-particle cryo-EM, we obtained structures of the eukaryotic ribosome in complexes with several aminoglycosides (geneticin G418, paromomycin, and hygromycin B) and the antimalarial drug mefloquine (MFQ), which has also been identified as a read-through enhancer. Our study reveals a binding site of MFQ, which holds significant promise for the development of therapies targeting premature termination codon-related genetic and oncological diseases. The results underscore the crucial role of the bridge B7b/c in mediating the effects of MFQ on subunit rotation dynamics. Through a comprehensive analysis of the interactions between the drugs and the eukaryotic ribosome, we propose a unifying hypothesis for read-through enhancement by small molecules, highlighting the role of decoding center rearrangements and intersubunit rotation dynamics.

Article Details

Volume / Issue Vol. 122, Issue 17
Published April 29, 2025
ISSN 0027-8424
Publisher National Academy of Sciences

Authors (13)

O

Olga Kolosova

Department of Integrated Structural Biology, Institute of Genetics and Molecular and Cellular Biology, University of Strasbourg

Y

Yury Zgadzay

Department of Integrated Structural Biology, Institute of Genetics and Molecular and Cellular Biology, University of Strasbourg

A

Artem Stetsenko

Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen

A

Anastasia P. Sukhinina

Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University

A

Anastasia Atamas

Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen

S

Shamil Validov

Laboratory of Structural Biology, Institute of Fundamental Medicine and Biology, Kazan Federal University

A

Andrey Rogachev

Moscow Centre for Advanced Studies

K

Konstantin Usachev

Laboratory of Structural Biology, Institute of Fundamental Medicine and Biology, Kazan Federal University

L

Lasse Jenner

Department of Integrated Structural Biology, Institute of Genetics and Molecular and Cellular Biology, University of Strasbourg

S

Sergey E. Dmitriev

G

Gulnara Yusupova

Department of Integrated Structural Biology, Institute of Genetics and Molecular and Cellular Biology, University of Strasbourg

A

Albert Guskov

Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen

M

Marat Yusupov

Department of Integrated Structural Biology, Institute of Genetics and Molecular and Cellular Biology, University of Strasbourg