{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Morgan SM"],"funding":["NIDCR NIH HHS","U.S. Department of Health & Human Services | NIH | National Institute of Dental and Craniofacial Research","U.S. Department of Health & Human Services | NIH | National Institute of Allergy and Infectious Diseases","NIAID NIH HHS","NCI NIH HHS"],"pagination":["187"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8764100"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13(1)"],"pubmed_abstract":["Epstein-Barr virus (EBV) persists in human B-cells by maintaining its chromatinized episomes within the nucleus. We have previously shown that cellular factor Poly [ADP-ribose] polymerase 1 (PARP1) binds the EBV genome, stabilizes CTCF binding at specific loci, and that PARP1 enzymatic activity correlates with maintaining a transcriptionally active latency program. To better understand PARP1's role in regulating EBV latency, here we functionally characterize the effect of PARP enzymatic inhibition on episomal structure through in situ HiC mapping, generating a complete 3D structure of the EBV genome. We also map intragenomic contact changes after PARP inhibition to global binding of chromatin looping factors CTCF and cohesin across the EBV genome. We find that PARP inhibition leads to fewe"],"journal":["Nature communications"],"pubmed_title":["The three-dimensional structure of Epstein-Barr virus genome varies by latency type and is regulated by PARP1 enzymatic activity."],"pmcid":["PMC8764100"],"funding_grant_id":["R01 CA093606","R50 CA211199","P30 CA010815","R01 DE017336","R01 AI130209","R01AI130209"],"pubmed_authors":["Hulse M","Keith K","Tanizawa H","Caruso LB","Tan Y","Lieberman PM","Boyle S","Kossenkov A","Morgan SM","Tempera I","Madzo J"],"additional_accession":[]},"is_claimable":false,"name":"The three-dimensional structure of Epstein-Barr virus genome varies by latency type and is regulated by PARP1 enzymatic activity.","description":"Epstein-Barr virus (EBV) persists in human B-cells by maintaining its chromatinized episomes within the nucleus. We have previously shown that cellular factor Poly [ADP-ribose] polymerase 1 (PARP1) binds the EBV genome, stabilizes CTCF binding at specific loci, and that PARP1 enzymatic activity correlates with maintaining a transcriptionally active latency program. To better understand PARP1's role in regulating EBV latency, here we functionally characterize the effect of PARP enzymatic inhibition on episomal structure through in situ HiC mapping, generating a complete 3D structure of the EBV genome. We also map intragenomic contact changes after PARP inhibition to global binding of chromatin looping factors CTCF and cohesin across the EBV genome. We find that PARP inhibition leads to fewe","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Jan","modification":"2026-05-30T20:55:00.44Z","creation":"2025-04-04T10:01:50.706Z"},"accession":"S-EPMC8764100","cross_references":{"pubmed":["35039491"],"doi":["10.1038/s41467-021-27894-1"]}}