{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,15]],"date-time":"2026-10-15T12:25:09Z","timestamp":1792067109745,"version":"4.4.0"},"reference-count":54,"publisher":"American Society for Microbiology","issue":"14","license":[{"start":{"date-parts":[[2018,7,15]],"date-time":"2018-07-15T00:00:00Z","timestamp":1531612800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"funder":[{"DOI":"10.13039\/501100000038","name":"Gouvernement du Canada | Natural Sciences and Engineering Research Council of Canada","doi-asserted-by":"publisher","award":["RGPIN\/435375-2013"],"award-info":[{"award-number":["RGPIN\/435375-2013"]}],"id":[{"id":"10.13039\/501100000038","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100008794","name":"Research Manitoba","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100008794","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Virol"],"published-print":{"date-parts":[[2018,7,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Far-upstream element (FUSE) binding protein 1 (FUBP1) was originally identified as a regulator of the oncogene\n            <jats:italic>c-Myc<\/jats:italic>\n            via binding to the FUSE within the\n            <jats:italic>c-Myc<\/jats:italic>\n            promoter and activating the expression of the gene. Recent studies have identified FUBP1 as a regulator of transcription, translation, and splicing via its DNA and RNA binding activities. Here we report the identification of FUBP1 as a novel binding partner of E1A. FUBP1 binds directly to E1A via the N terminus (residues 1 to 82) and conserved region 3 (residues 139 to 204) of adenovirus 5 E1A. The depletion of FUBP1 via short interfering RNAs (siRNA) reduces virus growth and drives the upregulation of the cellular stress response by activating the expression of p53-regulated genes. During infection, FUBP1 is relocalized within the nucleus, and it is recruited to viral promoters together with E1A while at the same time being lost from the FUSE upstream of the\n            <jats:italic>c-Myc<\/jats:italic>\n            promoter. The depletion of FUBP1 affects viral and cellular gene expression. Importantly, in FUBP1-depleted cells, p53-responsive genes are upregulated, p53 occupancy on target promoters is enhanced, and histone H3 lysine 9 is hyperacetylated. This is likely due to the loss of the FUBP1-mediated suppression of p53 DNA binding. We also observed that E1A stabilizes the FUBP1-p53 complex, preventing p53 promoter binding. Together, our results identify, for the first time, FUBP1 as a novel E1A binding protein that participates in aspects of viral replication and is involved in the E1A-mediated suppression of p53 function.\n          <\/jats:p>\n          <jats:p>\n            <jats:bold>IMPORTANCE<\/jats:bold>\n            Viral infection triggers innate cellular defense mechanisms that have evolved to block virus replication. To overcome this, viruses have counterevolved mechanisms that ensure that cellular defenses are either disarmed or not activated to guarantee successful replication. One of the key regulators of cellular stress is the tumor suppressor p53 that responds to a variety of cellular stress stimuli and safeguards the integrity of the genome. During infection, many viruses target the p53 pathway in order to deactivate it. Here we report that human adenovirus 5 coopts the cellular protein FUBP1 to prevent the activation of the p53 stress response pathway that would block viral replication. This finding adds to our understanding of p53 deactivation by adenovirus and highlights its importance in infection and innate immunity.\n          <\/jats:p>","DOI":"10.1128\/jvi.00439-18","type":"journal-article","created":{"date-parts":[[2018,5,8]],"date-time":"2018-05-08T09:40:15Z","timestamp":1525772415000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":20,"title":["Adenovirus 5 E1A-Mediated Suppression of p53 via FUBP1"],"prefix":"10.1128","volume":"92","author":[{"given":"Jasmine Rae","family":"Frost","sequence":"first","affiliation":[{"name":"Department of Microbiology, University of Manitoba, Winnipeg, MB, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Megan","family":"Mendez","sequence":"additional","affiliation":[{"name":"Department of Microbiology, University of Manitoba, Winnipeg, MB, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrea Michelle","family":"Soriano","sequence":"additional","affiliation":[{"name":"Department of Microbiology, University of Manitoba, Winnipeg, MB, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Leandro","family":"Crisostomo","sequence":"additional","affiliation":[{"name":"Department of Microbiology, University of Manitoba, Winnipeg, MB, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Oladunni","family":"Olanubi","sequence":"additional","affiliation":[{"name":"Department of Microbiology, University of Manitoba, Winnipeg, MB, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sandi","family":"Radko","sequence":"additional","affiliation":[{"name":"Department of Microbiology, University of Manitoba, Winnipeg, MB, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Peter","family":"Pelka","sequence":"additional","affiliation":[{"name":"Department of Microbiology, University of Manitoba, Winnipeg, MB, Canada"},{"name":"Department of Medical Microbiology, University of Manitoba, Winnipeg, MB, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","volume-title":"Fields virology","author":"Knipe DM","year":"2013","unstructured":"Knipe DM, Howley PM, Cohen JI, Griffin DE, Lamb RA, Martin MA, Racaniello VR, Roizman B (ed). 2013. 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