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dc.contributor.authorYu, Xupeng
dc.contributor.authorGray, Sean
dc.contributor.authorFerreira, Helder
dc.date.accessioned2023-01-18T11:30:12Z
dc.date.available2023-01-18T11:30:12Z
dc.date.issued2023-01-25
dc.identifier282877913
dc.identifierc0aab2ef-9132-4333-b67f-c8c1399d382c
dc.identifier000905185900001
dc.identifier85147047332
dc.identifier.citationYu , X , Gray , S & Ferreira , H 2023 , ' POT-3 preferentially binds the terminal DNA-repeat on the telomeric G-overhang ' , Nucleic Acids Research , vol. 51 , no. 2 , pp. 610–618 . https://doi.org/10.1093/nar/gkac1203en
dc.identifier.issn0305-1048
dc.identifier.otherBibtex: 10.1093/nar/gkac1203
dc.identifier.otherORCID: /0000-0001-9143-504X/work/126553814
dc.identifier.urihttps://hdl.handle.net/10023/26770
dc.descriptionFunding: The China Scholarship Scheme supported Xupeng Yu [201904910787]; some strains were provided by the CGC, which is funded by NIH Office of Research Infrastructure Programs [P40 OD010440]. Funding for open access charge: Scottish Higher Education Digital Library Consortium (SHEDL) Read and Publish agreement.en
dc.description.abstractEukaryotic chromosomes typically end in 3′ telomeric overhangs. The safeguarding of telomeric single-stranded DNA overhangs is carried out by factors related to the protection of telomeres 1 (POT1) protein in humans. Of the three POT1-like proteins in Caenorhabditis elegans, POT-3 was the only member thought to not play a role at telomeres. Here, we provide evidence that POT-3 is a bona fide telomere-binding protein. Using a new loss-of-function mutant, we show that the absence of POT-3 causes telomere lengthening and increased levels of telomeric C-circles. We find that POT-3 directly binds the telomeric G-strand in vitro and map its minimal DNA binding site to the six-nucleotide motif, GCTTAG. We further show that the closely related POT-2 protein binds the same motif, but that POT-3 shows higher sequence selectivity. Crucially, in contrast to POT-2, POT-3 prefers binding sites immediately adjacent to the 3′ end of DNA. These differences are significant as genetic analyses reveal that pot-2 and pot-3 do not function redundantly with each other in vivo. Our work highlights the rapid evolution and specialisation of telomere binding proteins and places POT-3 in a unique position to influence activities that control telomere length.
dc.format.extent9
dc.format.extent1767843
dc.language.isoeng
dc.relation.ispartofNucleic Acids Researchen
dc.subjectQD Chemistryen
dc.subjectQH426 Geneticsen
dc.subjectNDASen
dc.subjectMCCen
dc.subject.lccQDen
dc.subject.lccQH426en
dc.titlePOT-3 preferentially binds the terminal DNA-repeat on the telomeric G-overhangen
dc.typeJournal articleen
dc.contributor.institutionUniversity of St Andrews. School of Biologyen
dc.contributor.institutionUniversity of St Andrews. St Andrews Bioinformatics Uniten
dc.contributor.institutionUniversity of St Andrews. Biomedical Sciences Research Complexen
dc.identifier.doihttps://doi.org/10.1093/nar/gkac1203
dc.description.statusPeer revieweden


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