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POT-3 preferentially binds the terminal DNA-repeat on the telomeric G-overhang
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dc.contributor.author | Yu, Xupeng | |
dc.contributor.author | Gray, Sean | |
dc.contributor.author | Ferreira, Helder | |
dc.date.accessioned | 2023-01-18T11:30:12Z | |
dc.date.available | 2023-01-18T11:30:12Z | |
dc.date.issued | 2023-01-25 | |
dc.identifier | 282877913 | |
dc.identifier | c0aab2ef-9132-4333-b67f-c8c1399d382c | |
dc.identifier | 000905185900001 | |
dc.identifier | 85147047332 | |
dc.identifier.citation | Yu , 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/gkac1203 | en |
dc.identifier.issn | 0305-1048 | |
dc.identifier.other | Bibtex: 10.1093/nar/gkac1203 | |
dc.identifier.other | ORCID: /0000-0001-9143-504X/work/126553814 | |
dc.identifier.uri | https://hdl.handle.net/10023/26770 | |
dc.description | Funding: 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.abstract | Eukaryotic 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.extent | 9 | |
dc.format.extent | 1767843 | |
dc.language.iso | eng | |
dc.relation.ispartof | Nucleic Acids Research | en |
dc.subject | QD Chemistry | en |
dc.subject | QH426 Genetics | en |
dc.subject | NDAS | en |
dc.subject | MCC | en |
dc.subject.lcc | QD | en |
dc.subject.lcc | QH426 | en |
dc.title | POT-3 preferentially binds the terminal DNA-repeat on the telomeric G-overhang | en |
dc.type | Journal article | en |
dc.contributor.institution | University of St Andrews. School of Biology | en |
dc.contributor.institution | University of St Andrews. St Andrews Bioinformatics Unit | en |
dc.contributor.institution | University of St Andrews. Biomedical Sciences Research Complex | en |
dc.identifier.doi | https://doi.org/10.1093/nar/gkac1203 | |
dc.description.status | Peer reviewed | en |
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