{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Shiekh S"],"funding":["NSF","Kent State University","NIH","NIH HHS"],"pagination":["12885-12895"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9825182"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["50(22)"],"pubmed_abstract":["Telomeres terminate with a 50-300 bases long single-stranded G-rich overhang, which can be misrecognized as a DNA damage repair site. Shelterin plays critical roles in maintaining and protecting telomere ends by regulating access of various physiological agents to telomeric DNA, but the underlying mechanism is not well understood. Here, we measure how shelterin affects the accessibility of long telomeric overhangs by monitoring transient binding events of a short complementary peptide nucleic acid (PNA) probe using FRET-PAINT in vitro. We observed that the POT1 subunit of shelterin reduces the accessibility of the PNA probe by ∼2.5-fold, indicating that POT1 effectively binds to and protects otherwise exposed telomeric sequences. In comparison, a four-component shelterin stabilizes POT1 bi"],"journal":["Nucleic acids research"],"pubmed_title":["Shelterin reduces the accessibility of telomeric overhangs."],"pmcid":["PMC9825182"],"funding_grant_id":["1R15GM146180","R01GM130745","1R15GM123443","R01GM134426","MCB 1954449","R35GM136414"],"pubmed_authors":["Saurabh A","Kodikara SG","Hoque ME","Shiekh S","Gyawali P","Balci H","Jack A","Presse S","Mustafa G","Yildiz A"],"additional_accession":[]},"is_claimable":false,"name":"Shelterin reduces the accessibility of telomeric overhangs.","description":"Telomeres terminate with a 50-300 bases long single-stranded G-rich overhang, which can be misrecognized as a DNA damage repair site. Shelterin plays critical roles in maintaining and protecting telomere ends by regulating access of various physiological agents to telomeric DNA, but the underlying mechanism is not well understood. Here, we measure how shelterin affects the accessibility of long telomeric overhangs by monitoring transient binding events of a short complementary peptide nucleic acid (PNA) probe using FRET-PAINT in vitro. We observed that the POT1 subunit of shelterin reduces the accessibility of the PNA probe by ∼2.5-fold, indicating that POT1 effectively binds to and protects otherwise exposed telomeric sequences. In comparison, a four-component shelterin stabilizes POT1 bi","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Dec","modification":"2025-04-04T07:22:17.691Z","creation":"2025-04-04T07:22:17.691Z"},"accession":"S-EPMC9825182","cross_references":{"pubmed":["36511858"],"doi":["10.1093/nar/gkac1176"]}}