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Interaction of the lymphocyte-derived Epstein-Barr virus nuclear antigen EBNA-1 with its DNA-binding sites.
J Virol. 1989 Jan; 63(1):101-10.JV

Abstract

The Epstein-Barr virus (EBV) nuclear antigen EBNA-1 plays an integral role in the maintenance of latency in EBV-infected B lymphocytes. EBNA-1 binds to sequences within the plasmid origin of replication (oriP). It is essential for the replication of the latent episomal form of EBV DNA and may also regulate the expression of the EBNA group of latency gene products. We have used sequence-specific DNA-binding assays to purify EBNA-1 away from nonspecific DNA-binding proteins in a B-lymphocyte cell extract. The availability of this eucaryotic protein has allowed an examination of the interaction of EBNA-1 with its specific DNA-binding sites and an evaluation of possible roles for the different binding loci within the EBV genome. DNA filter binding assays and DNase I footprinting experiments showed that the intact Raji EBNA-1 protein recognized the two binding site loci in oriP and the BamHI-Q locus and no other sites in the EBV genome. Competition filter binding experiments with monomer and multimer region I consensus binding sites indicated that cooperative interactions between binding sites have relatively little impact on EBNA-1 binding to region I. An analysis of the binding parameters of the Raji EBNA-1 to the three naturally occurring binding loci revealed that the affinity of EBNA-1 for the three loci differed. The affinity for the sites in region I of oriP was greater than the affinity for the dyad symmetry sites (region II) of oriP, while the physically distant region III locus showed the lowest affinity. This arrangement may provide a mechanism whereby EBNA-1 can lowest affinity. This arrangement may provide a mechanism whereby EBNA-1 can mediate differing regulatory functions through differential binding to its recognition sequence.

Authors+Show Affiliations

Department of Microbiology and Immunology, Emory University School of Medicine, Atlanta, Georgia 30322.No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

2535719

Citation

Jones, C H., et al. "Interaction of the Lymphocyte-derived Epstein-Barr Virus Nuclear Antigen EBNA-1 With Its DNA-binding Sites." Journal of Virology, vol. 63, no. 1, 1989, pp. 101-10.
Jones CH, Hayward SD, Rawlins DR. Interaction of the lymphocyte-derived Epstein-Barr virus nuclear antigen EBNA-1 with its DNA-binding sites. J Virol. 1989;63(1):101-10.
Jones, C. H., Hayward, S. D., & Rawlins, D. R. (1989). Interaction of the lymphocyte-derived Epstein-Barr virus nuclear antigen EBNA-1 with its DNA-binding sites. Journal of Virology, 63(1), 101-10.
Jones CH, Hayward SD, Rawlins DR. Interaction of the Lymphocyte-derived Epstein-Barr Virus Nuclear Antigen EBNA-1 With Its DNA-binding Sites. J Virol. 1989;63(1):101-10. PubMed PMID: 2535719.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Interaction of the lymphocyte-derived Epstein-Barr virus nuclear antigen EBNA-1 with its DNA-binding sites. AU - Jones,C H, AU - Hayward,S D, AU - Rawlins,D R, PY - 1989/1/1/pubmed PY - 1989/1/1/medline PY - 1989/1/1/entrez SP - 101 EP - 10 JF - Journal of virology JO - J Virol VL - 63 IS - 1 N2 - The Epstein-Barr virus (EBV) nuclear antigen EBNA-1 plays an integral role in the maintenance of latency in EBV-infected B lymphocytes. EBNA-1 binds to sequences within the plasmid origin of replication (oriP). It is essential for the replication of the latent episomal form of EBV DNA and may also regulate the expression of the EBNA group of latency gene products. We have used sequence-specific DNA-binding assays to purify EBNA-1 away from nonspecific DNA-binding proteins in a B-lymphocyte cell extract. The availability of this eucaryotic protein has allowed an examination of the interaction of EBNA-1 with its specific DNA-binding sites and an evaluation of possible roles for the different binding loci within the EBV genome. DNA filter binding assays and DNase I footprinting experiments showed that the intact Raji EBNA-1 protein recognized the two binding site loci in oriP and the BamHI-Q locus and no other sites in the EBV genome. Competition filter binding experiments with monomer and multimer region I consensus binding sites indicated that cooperative interactions between binding sites have relatively little impact on EBNA-1 binding to region I. An analysis of the binding parameters of the Raji EBNA-1 to the three naturally occurring binding loci revealed that the affinity of EBNA-1 for the three loci differed. The affinity for the sites in region I of oriP was greater than the affinity for the dyad symmetry sites (region II) of oriP, while the physically distant region III locus showed the lowest affinity. This arrangement may provide a mechanism whereby EBNA-1 can lowest affinity. This arrangement may provide a mechanism whereby EBNA-1 can mediate differing regulatory functions through differential binding to its recognition sequence. SN - 0022-538X UR - https://www.unboundmedicine.com/medline/citation/2535719/Interaction_of_the_lymphocyte_derived_Epstein_Barr_virus_nuclear_antigen_EBNA_1_with_its_DNA_binding_sites_ L2 - http://jvi.asm.org/cgi/pmidlookup?view=long&pmid=2535719 DB - PRIME DP - Unbound Medicine ER -