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Design and characterization of G-quadruplex RNA aptamers reveal RNA-binding by KDM5 lysine demethylases

Year: 2025
Type: article
Abstract: Here, we show that the histone lysine demethylases KDM5A and KDM5B can bind to RNA through interaction with G-quadruplexes, despite neither being categorized as RNA- nor G-quadruplex binding proteins across numerous experimental large-scale and computational studies. In addition to characterizing the KDM5 G-quadruplex interaction we show that RNA is directly involved in the formation of KDM5-containing protein complexes. Computational predictions and comparisons to other ARID domain containing proteins suggest that the ARID domain is directly interacting with both DNA and RNA across several proteins. Our work highlights that the RNA-binding by KDM5 lysine demethylases is dependent on recognizing G-quadruplex structures and that RNA mediates the formation of alternative KDM5-containing protein complexes.
DOI: 10.1016/j.csbj.2025.06.027
Authors: Johanna Luige, Thomas Conrad, Alexandros Armaos, Annita Louloupi, Anna Vincent, David Meierhofer, Michael Gajhede, Gian Gaetano Tartaglia, Ulf Andersson Vang Ørom
Institutions: Aarhus University, Max Delbrück Center, Italian Institute of Technology, Max Planck Institute for Molecular Genetics, University of Copenhagen, Sapienza University of Rome
Language: English
Open Access status: gold
Estimated APC paid: $3,230
Funders: Alexander von Humboldt-Stiftung, Kræftens Bekæmpelse, Lundbeckfonden, Novo Nordisk, Danmarks Frie Forskningsfond, Novo Nordisk Fonden, H. Lundbeck A/S, European Research Council
OpenAlex ID: W4411334320
FWCI: 0.504
Cites: 100
Cited by: 2
Related to: 10