{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Li J"],"funding":["National Institute of Allergy and Infectious Diseases","NIDCR NIH HHS","NIAID NIH HHS","National Cancer Institute","National Institute of Dental and Craniofacial Research","NCI NIH HHS"],"pagination":["eaaw7373"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6785261"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["5(10)"],"pubmed_abstract":["Protein nuclear translocation is highly regulated and crucial for diverse biological processes. However, our understanding concerning protein nuclear import is incomplete. Here we report that a cellular purine synthesis enzyme inhibits protein nuclear import via deamidation. Employing human Kaposi's sarcoma-associated herpesvirus (KSHV) to probe the role of protein deamidation, we identified a purine synthesis enzyme, phosphoribosylformylglycinamidine synthetase (PFAS) that inhibits KSHV transcriptional activation. PFAS deamidates the replication transactivator (RTA), a transcription factor crucial for KSHV lytic replication. Mechanistically, deamidation of two asparagines flanking a positively charged nuclear localization signal impaired the binding of RTA to an importin β subunit, thus d"],"journal":["Science advances"],"pubmed_title":["Antiviral activity of a purine synthesis enzyme reveals a key role of deamidation in regulating protein nuclear import."],"pmcid":["PMC6785261"],"funding_grant_id":["DE026003","DE027556","P01 CA180779","R03 DE022521","R35 DE027557","R01 CA203923","R35 DE027556","AI134105","CA221521","R01 CA221521","R21 AI134105"],"pubmed_authors":["Tarakanova V","Li J","Tian M","Zhang J","Lee K","Zeng Y","Zhang S","Gao R","Xiao J","Feng H","Lan K","Xu S","Zhao J","Feng P"],"additional_accession":[]},"is_claimable":false,"name":"Antiviral activity of a purine synthesis enzyme reveals a key role of deamidation in regulating protein nuclear import.","description":"Protein nuclear translocation is highly regulated and crucial for diverse biological processes. However, our understanding concerning protein nuclear import is incomplete. Here we report that a cellular purine synthesis enzyme inhibits protein nuclear import via deamidation. Employing human Kaposi's sarcoma-associated herpesvirus (KSHV) to probe the role of protein deamidation, we identified a purine synthesis enzyme, phosphoribosylformylglycinamidine synthetase (PFAS) that inhibits KSHV transcriptional activation. PFAS deamidates the replication transactivator (RTA), a transcription factor crucial for KSHV lytic replication. Mechanistically, deamidation of two asparagines flanking a positively charged nuclear localization signal impaired the binding of RTA to an importin β subunit, thus d","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 Oct","modification":"2025-04-19T17:10:25.709Z","creation":"2019-10-30T08:19:13Z"},"accession":"S-EPMC6785261","cross_references":{"pubmed":["31633017"],"doi":["10.1126/sciadv.aaw7373"]}}