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Identification and characterization of RNA guanine-quadruplex binding proteins
Zitatschlüssel Hacht.2014
Autor von Hacht, Annekathrin and Seifert, Oliver and Menger, Marcus and Schütze, Tatjana and Arora, Amit and Konthur, Zoltán and Neubauer, Peter and Wagner, Anke and Weise, Christoph and Kurreck, Jens
Seiten 6630–6644
Jahr 2014
DOI 10.1093/nar/gku290
Journal Nucleic acids research
Jahrgang 42
Nummer 10
Zusammenfassung Guanine quadruplex (G-quadruplex) motifs in the 5' untranslated region (5'-UTR) of mRNAs were recently shown to influence the efficiency of translation. In the present study, we investigate the interaction between cellular proteins and the G-quadruplexes located in two mRNAs (MMP16 and ARPC2). Formation of the G-quadruplexes was confirmed by biophysical characterization and the inhibitory activity on translation was shown by luciferase reporter assays. In experiments with whole cell extracts from different eukaryotic cell lines, G-quadruplex-binding proteins were isolated by pull-down assays and subsequently identified by matrix-assisted laser desorption ionization-time of flight mass spectrometry. The binding partners of the RNA G-quadruplexes we discovered included several heterogeneous nuclear ribonucleoproteins, ribosomal proteins, and splicing factors, as well as other proteins that have previously not been described to interact with nucleic acids. While most of the proteins were specific for either of the investigated G-quadruplexes, some of them bound to both motifs. Selected candidate proteins were subsequently produced by recombinant expression and dissociation constants for the interaction between the proteins and RNA G-quadruplexes in the low nanomolar range were determined by surface plasmon resonance spectroscopy. The present study may thus help to increase our understanding of the mechanisms by which G-quadruplexes regulate translation.
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