Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/153717
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dc.contributor.authorChatain, Jeanen_US
dc.contributor.authorBlond, Alainen_US
dc.contributor.authorPhan, Anh Tuânen_US
dc.contributor.authorSaintomé, Caroleen_US
dc.contributor.authorAlberti, Patriziaen_US
dc.date.accessioned2022-01-17T07:23:20Z-
dc.date.available2022-01-17T07:23:20Z-
dc.date.issued2021-
dc.identifier.citationChatain, J., Blond, A., Phan, A. T., Saintomé, C. & Alberti, P. (2021). GGGCTA repeats can fold into hairpins poorly unfolded by replication protein A : a possible origin of the length-dependent instability of GGGCTA variant repeats in human telomeres. Nucleic Acids Research, 49(13), 7588-7601. https://dx.doi.org/10.1093/nar/gkab518en_US
dc.identifier.issn0305-1048en_US
dc.identifier.urihttps://hdl.handle.net/10356/153717-
dc.description.abstractHuman telomeres are composed of GGGTTA repeats and interspersed with variant repeats. The GGGCTA variant motif was identified in the proximal regions of human telomeres about 10 years ago and was shown to display a length-dependent instability. In parallel, a structural study showed that four GGGCTA repeats folded into a non-canonical G-quadruplex (G4) comprising a Watson-Crick GCGC tetrad. It was proposed that this non-canonical G4 might be an additional obstacle for telomere replication. In the present study, we demonstrate that longer GGGCTA arrays fold into G4 and into hairpins. We also demonstrate that replication protein A (RPA) efficiently binds to GGGCTA repeats structured into G4 but poorly binds to GGGCTA repeats structured into hairpins. Our results (along with results obtained with a more stable variant motif) suggest that GGGCTA hairpins are at the origin of GGGCTA length-dependent instability. They also suggest, as working hypothesis, that failure of efficient binding of RPA to GGGCTA structured into hairpins might be involved in the mechanism of GGGCTA array instability. On the basis of our present and past studies about telomeric G4 and their interaction with RPA, we propose an original point of view about telomeric G4 and the evolution of telomeric motifs.en_US
dc.language.isoenen_US
dc.relation.ispartofNucleic Acids Researchen_US
dc.rights© 2021 The Author(s). Published by Oxford University Press on behalf of Nucleic Acids Research. This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.comen_US
dc.subjectScience::Biological sciencesen_US
dc.titleGGGCTA repeats can fold into hairpins poorly unfolded by replication protein A : a possible origin of the length-dependent instability of GGGCTA variant repeats in human telomeresen_US
dc.typeJournal Articleen
dc.contributor.schoolSchool of Physical and Mathematical Sciencesen_US
dc.contributor.researchNTU Institute of Structural Biologyen_US
dc.identifier.doi10.1093/nar/gkab518-
dc.description.versionPublished versionen_US
dc.identifier.pmid34214172-
dc.identifier.scopus2-s2.0-85112126981-
dc.identifier.issue13en_US
dc.identifier.volume49en_US
dc.identifier.spage7588en_US
dc.identifier.epage7601en_US
dc.subject.keywordsSingle-Stranded-DNAen_US
dc.subject.keywordsWerner-Syndrome Proteinen_US
dc.description.acknowledgementMuseum National d’Histoire Naturelle (MNHN); Centre National de la Recherche Scientifique (CNRS); Institut National de la Sante et de la Recherche Medicale (INSERM); Ministere de l’Enseignement Superieur, de la Recherche de de l’Innovation (MESRI) Ph.D. Fellowship (to J.C.). Funding for open access charge: INSERM.en_US
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