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E2F1, ARID3A/Bright and Oct-2 factors bind to the Epstein-Barr virus C promoter, EBNA1 and oriP, participating in long-distance promoter-enhancer interactions.

Artikel i vetenskaplig tidskrift
Författare Cecilia Boreström
Alma Forsman
Ulla Rüetschi
Lars Rymo
Publicerad i The Journal of general virology
Volym 93
Sidor 1065-75
ISSN 1465-2099
Publiceringsår 2012
Publicerad vid Institutionen för biomedicin, avdelningen för klinisk kemi och transfusionsmedicin
Sidor 1065-75
Språk en
Länkar dx.doi.org/10.1099/vir.0.038752-0
Ämnesord Chromatography, Affinity, DNA, Viral, metabolism, DNA-Binding Proteins, metabolism, E2F1 Transcription Factor, metabolism, Epstein-Barr Virus Nuclear Antigens, metabolism, Gene Expression Regulation, Viral, Herpesvirus 4, Human, genetics, physiology, Host-Pathogen Interactions, Humans, Immunoblotting, Immunoprecipitation, Mass Spectrometry, Octamer Transcription Factor-2, metabolism, Promoter Regions, Genetic, Protein Binding, Protein Interaction Mapping, Protein Multimerization, Replication Origin, Transcription Factors, metabolism
Ämneskategorier Klinisk kemi

Sammanfattning

The Epstein-Barr virus (EBV) C promoter (Cp) regulates several genes required for B-cell proliferation in latent EBV infection. The family of repeats (FR) region of the latent origin of plasmid replication (oriP) functions as an Epstein-Barr nuclear antigen 1 (EBNA1)-dependent distant enhancer of Cp activity, and the enhancer-promoter interaction is mediated by a higher-order multi-protein complex containing several copies of EBNA1. Using DNA-affinity purification with a 170 bp region of the Cp in combination with mass spectrometry, we identified the cell cycle-regulatory protein E2F1, the E2F-binding protein ARID3A, and the B-cell-specific transcription factor Oct-2 as components of this multi-protein complex. Binding of the three factors to the FR region of oriP was determined by DNA-affinity and immunoblot analysis. Co-immunoprecipitation and proximity ligation analysis revealed that the three factors, E2F1, ARID3A and Oct-2, interact with each other as well as with EBNA1 in the nuclei of EBV-positive cells. Using the chromatin immunoprecipitation assay, we showed that E2F1 and Oct-2 interacted with the FR part of oriP and the Cp, but the ARID3A interaction was, however, only detected at the Cp. Our findings support the hypothesis that EBNA1 initiates transcription at the Cp via interactions between multiple EBNA1 homodimers and cellular transcription factors in a large molecular machinery that forms a dynamic interaction between Cp and FR.

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