Description
We describe how the cancer-causing Epstein-Barr virus (EBV), a prototypic herpesvirus, alters proteome at viral replication forks prominently identifies chromatin modifying and transcriptional repression proteins. Specifically, to transition from transcription, the viral DNA polymerase processivity factor EA-D is SUMOylated by the transcriptional corepressor KAP1-TRIM28. KAP1 function is triggered by phosphorylation via the PI3K-related kinase ATM and the helicase RECQ5 at the transcription machinery. SUMO-EA-D recruits the histone loader CAF1 and the methyltransferase SETDB1 to silence the parental genome, prioritizing replication. Thus, DNA repair, epigenetic, and transcription-replication interference pathways orchestrate the handover from transcription to replication, a fundamental feature of DNA viruses
[doi:10.25345/C5VX06D0F]
[dataset license: CC0 1.0 Universal (CC0 1.0)]
Keywords: iPOND
Contact
Principal Investigators:
(in alphabetical order)
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Sumita Bhaduri-McIntosh, University of Florida, USA
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jhaley55
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Distinct condition labels are counted across all files submitted in the "Metadata" category
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Originally identified proteins that were automatically
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SwissProt
human reference database.
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Number of distinct peptide sequences (including modified variants or peptidoforms) reported
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Distinct protein accessions are counted across all files submitted in the "Statistical Analysis
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Number of distinct proteins found to be differentially abundant in at least one comparison
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A protein is differentially abundant if its change in abundance across conditions is found
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Distinct protein accessions are counted across all files submitted in the "Statistical Analysis
of Quantified Analytes" category having a "Protein" column in this dataset.
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This dataset may not contain all raw spectra data as originally deposited in PRIDE.
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