{"title":"收支相抵","authors":"Sylvie Doublié","doi":"10.1038/s41594-025-01578-6","DOIUrl":null,"url":null,"abstract":"Two papers offer a first glimpse at complexes of the helicase-like domain of DNA polymerase θ (Polθ-HD) bound to DNA. Together, they provide structural insights into how the dimeric form of Polθ-HD grabs and aligns single-stranded DNA tails near the 3′ termini, a process that is accompanied by large conformational changes within Polθ-HD.","PeriodicalId":18822,"journal":{"name":"Nature structural & molecular biology","volume":"18 1","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2025-05-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Making 3′ ends meet\",\"authors\":\"Sylvie Doublié\",\"doi\":\"10.1038/s41594-025-01578-6\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Two papers offer a first glimpse at complexes of the helicase-like domain of DNA polymerase θ (Polθ-HD) bound to DNA. Together, they provide structural insights into how the dimeric form of Polθ-HD grabs and aligns single-stranded DNA tails near the 3′ termini, a process that is accompanied by large conformational changes within Polθ-HD.\",\"PeriodicalId\":18822,\"journal\":{\"name\":\"Nature structural & molecular biology\",\"volume\":\"18 1\",\"pages\":\"\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2025-05-22\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Nature structural & molecular biology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1038/s41594-025-01578-6\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Nature structural & molecular biology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1038/s41594-025-01578-6","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Two papers offer a first glimpse at complexes of the helicase-like domain of DNA polymerase θ (Polθ-HD) bound to DNA. Together, they provide structural insights into how the dimeric form of Polθ-HD grabs and aligns single-stranded DNA tails near the 3′ termini, a process that is accompanied by large conformational changes within Polθ-HD.
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