{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Su K"],"funding":["Beijing Municipal Natural Science Foundation","National Natural Science Foundation of China"],"pagination":["490"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11468200"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["22(1)"],"pubmed_abstract":["<h4>Background</h4>Aberrant accumulation of R-loops leads to DNA damage, genome instability and even cell death. Therefore, the timely removal of harmful R-loops is essential for the maintenance of genome integrity. Nucleolar R-loops occupy up to 50% of cellular R-loops due to the frequent activation of Pol I transcription. However, the mechanisms involved in the nucleolar R-loop resolution remain elusive. The nucleolar acetyltransferase NAT10 harbors a putative RecD helicase domain (RHD), however, if NAT10 acts in the R-loop resolution is still unknown.<h4>Methods</h4>NAT10 knockdown cell lines were constructed using CRISPR/Cas9 technology and short hairpin RNA targeting NAT10 mRNA, respectively. The level of R-loops was detected by immunofluorescent staining combined with RNase H treatme"],"journal":["Cell communication and signaling : CCS"],"pubmed_title":["NAT10 resolves harmful nucleolar R-loops depending on its helicase domain and acetylation of DDX21."],"pmcid":["PMC11468200"],"funding_grant_id":["No. 7212061","No. 82173024"],"pubmed_authors":["Liu X","Jiang Y","Sun S","Du X","Su K","Wang Y","Zhang C","Zhao Z"],"additional_accession":[]},"is_claimable":false,"name":"NAT10 resolves harmful nucleolar R-loops depending on its helicase domain and acetylation of DDX21.","description":"<h4>Background</h4>Aberrant accumulation of R-loops leads to DNA damage, genome instability and even cell death. Therefore, the timely removal of harmful R-loops is essential for the maintenance of genome integrity. Nucleolar R-loops occupy up to 50% of cellular R-loops due to the frequent activation of Pol I transcription. However, the mechanisms involved in the nucleolar R-loop resolution remain elusive. The nucleolar acetyltransferase NAT10 harbors a putative RecD helicase domain (RHD), however, if NAT10 acts in the R-loop resolution is still unknown.<h4>Methods</h4>NAT10 knockdown cell lines were constructed using CRISPR/Cas9 technology and short hairpin RNA targeting NAT10 mRNA, respectively. The level of R-loops was detected by immunofluorescent staining combined with RNase H treatme","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Oct","modification":"2026-07-15T13:11:35.893Z","creation":"2025-04-06T12:31:33.735Z"},"accession":"S-EPMC11468200","cross_references":{"pubmed":["39394182"],"doi":["10.1186/s12964-024-01869-3"]}}