{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,9]],"date-time":"2026-09-09T05:13:06Z","timestamp":1788930786827,"version":"build-2803163510"},"reference-count":63,"publisher":"American Society for Microbiology","issue":"12","license":[{"start":{"date-parts":[[2023,12,21]],"date-time":"2023-12-21T00:00:00Z","timestamp":1703116800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/doi.org\/10.1128\/ASMCopyrightv2"},{"start":{"date-parts":[[2023,12,21]],"date-time":"2023-12-21T00:00:00Z","timestamp":1703116800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Virol"],"published-print":{"date-parts":[[2023,12,21]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>Adenovirus small e1a protein modifies host cell physiology to optimize virus replication. The N-terminal ~140 aa of e1a interacts with RB-family proteins to derepress dNTP and DNA synthesis and with EP300\/CREBBP lysine acetyltransferases and EP400-TIP60 chromatin-modifying complexes to inhibit host anti-viral innate immune responses. However, the e1a N-terminal region activates a late host anti-viral response due to stabilization and activation of IRF3. The E1A C-terminal region counteracts IRF3 stabilization through interactions with three host nuclear proteins with seemingly unrelated functions. All three C-terminal interactions are required for e1a-association into a multi-protein complex with scaffold subunits of a CRL4 E3 ubiquitin ligase and DCAF10, a presumed specificity subunit. This e1a-DCAF10-CRL4 prevents IRF3 stabilization indirectly by targeting the essential AAA+ ATPases RUVBL1\/2, subunits of several HSP90 co-chaperones required for quaternary assembly of cellular protein machines required for anti-viral defenses and responses to genotoxic and metabolic stress.<\/jats:p>\n          <jats:sec>\n            <jats:title>IMPORTANCE<\/jats:title>\n            <jats:p>Inactivation of EP300\/CREBB paralogous cellular lysine acetyltransferases (KATs) during the early phase of infection is a consistent feature of DNA viruses. The cell responds by stabilizing transcription factor IRF3 which activates transcription of scores of interferon-stimulated genes (ISGs), inhibiting viral replication. Human respiratory adenoviruses counter this by assembling a CUL4-based ubiquitin ligase complex that polyubiquitinylates RUVBL1 and 2 inducing their proteasomal degradation. This inhibits accumulation of active IRF3 and the expression of anti-viral ISGs, allowing replication of the respiratory HAdVs in the face of inhibition of EP300\/CBEBBP KAT activity by the N-terminal region of E1A.<\/jats:p>\n          <\/jats:sec>","DOI":"10.1128\/jvi.00993-23","type":"journal-article","created":{"date-parts":[[2023,11,14]],"date-time":"2023-11-14T14:00:54Z","timestamp":1699970454000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":5,"title":["Adenovirus E1A binding to DCAF10 targets proteasomal degradation of RUVBL1\/2 AAA+ ATPases required for quaternary assembly of multiprotein machines, innate immunity, and responses to metabolic stress"],"prefix":"10.1128","volume":"97","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-6326-5925","authenticated-orcid":false,"given":"Nathan R.","family":"Zemke","sequence":"first","affiliation":[{"name":"Molecular Biology Institute, University of California, 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