{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":["Walter M"],"funding":["NIAID NIH HHS","NIH HHS"],"pubmed_abstract":["SARS-CoV-2 non-structural protein Nsp14 is a highly conserved enzyme necessary for viral replication. Nsp14 forms a stable complex with non-structural protein Nsp10 and exhibits exoribonuclease and N7-methyltransferase activities. Protein-interactome studies identified human sirtuin 5 (SIRT5) as a putative binding partner of Nsp14. SIRT5 is an NAD-dependent protein deacylase critical for cellular metabolism that removes succinyl and malonyl groups from lysine residues. Here we investigated the nature of this interaction and the role of SIRT5 during SARS-CoV-2 infection. We showed that SIRT5 stably interacts with Nsp14, but not with Nsp10, suggesting that SIRT5 and Nsp10 are parts of separate complexes. We found that SIRT5 catalytic domain is necessary for the interaction with Nsp14, but th"],"journal":["bioRxiv : the preprint server for biology"],"pagination":["2022.01.04.474979"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8750649"],"repository":["biostudies-literature"],"pubmed_title":["SIRT5 is a proviral factor that interacts with SARS-CoV-2 Nsp14 protein."],"pmcid":["PMC8750649"],"funding_grant_id":["S10 OD010786","S10 OD016281","F31 AI164671"],"pubmed_authors":["Chen IP","Krogan NJ","Shah S","Kim IJ","Lam VL","Cruz A","Walter M","Bielska O","Schilling B","Vallejo-Gracia A","Ott M","Hayashi JM","Gross JD","Verdin E"],"additional_accession":[]},"is_claimable":false,"name":"SIRT5 is a proviral factor that interacts with SARS-CoV-2 Nsp14 protein.","description":"SARS-CoV-2 non-structural protein Nsp14 is a highly conserved enzyme necessary for viral replication. Nsp14 forms a stable complex with non-structural protein Nsp10 and exhibits exoribonuclease and N7-methyltransferase activities. Protein-interactome studies identified human sirtuin 5 (SIRT5) as a putative binding partner of Nsp14. SIRT5 is an NAD-dependent protein deacylase critical for cellular metabolism that removes succinyl and malonyl groups from lysine residues. Here we investigated the nature of this interaction and the role of SIRT5 during SARS-CoV-2 infection. We showed that SIRT5 stably interacts with Nsp14, but not with Nsp10, suggesting that SIRT5 and Nsp10 are parts of separate complexes. We found that SIRT5 catalytic domain is necessary for the interaction with Nsp14, but th","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Jan","modification":"2026-05-01T03:15:04.353Z","creation":"2022-02-11T16:19:48.556Z"},"accession":"S-EPMC8750649","cross_references":{"pubmed":["35018374"],"doi":["10.1101/2022.01.04.474979"]}}