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The RGG domain in the C-terminus of the DEAD box helicases Dbp2 and Ded1 is necessary for G-quadruplex destabilization
Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.ORCID iD: 0000-0003-0364-8964
Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.ORCID iD: 0000-0002-4541-7702
2021 (English)In: Nucleic Acids Research, ISSN 0305-1048, E-ISSN 1362-4962, Vol. 49, no 14, p. 8339-8354Article in journal (Refereed) Published
Abstract [en]

The identification of G-quadruplex (G4) binding proteins and insights into their mechanism of action are important for understanding the regulatory functions of G4 structures. Here, we performed an unbiased affinity-purification assay coupled with mass spectrometry and identified 30 putative G4 binding proteins from the fission yeast Schizosaccharomyces pombe. Gene ontology analysis of the molecular functions enriched in this pull-down assay included mRNA binding, RNA helicase activity, and translation regulator activity. We focused this study on three of the identified proteins that possessed putative arginine-glycine-glycine (RGG) domains, namely the Stm1 homolog Oga1 and the DEAD box RNA helicases Dbp2 and Ded1. We found that Oga1, Dbp2, and Ded1 bound to both DNA and RNA G4s in vitro. Both Dbp2 and Ded1 bound to G4 structures through the RGG domain located in the C-terminal region of the helicases, and point mutations in this domain weakened the G4 binding properties of the helicases. Dbp2 and Ded1 destabilized less thermostable G4 RNA and DNA structures, and this ability was independent of ATP but dependent on the RGG domain. Our study provides the first evidence that the RGG motifs in DEAD box helicases are necessary for both G4 binding and G4 destabilization.

Place, publisher, year, edition, pages
Oxford University Press, 2021. Vol. 49, no 14, p. 8339-8354
National Category
Cell and Molecular Biology Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:umu:diva-187116DOI: 10.1093/nar/gkab620ISI: 000692599800043PubMedID: 34302476Scopus ID: 2-s2.0-85114315622OAI: oai:DiVA.org:umu-187116DiVA, id: diva2:1590080
Funder
Wenner-Gren FoundationsKnut and Alice Wallenberg FoundationAvailable from: 2021-09-01 Created: 2021-09-01 Last updated: 2023-09-05Bibliographically approved

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Yan, Kok-PhenObi, IkennaSabouri, Nasim

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