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Stabilization of the EBNA1 protein on the Epstein-Barr virus latent origin of DNA replication by a DNA looping mechanism.
J Biol Chem. 1994 Jan 14; 269(2):1057-62.JB

Abstract

DNA replication from the Epstein-Barr virus latent origin of replication, oriP, is activated by Epstein-Barr nuclear antigen 1 (EBNA1). This activation involves the binding of EBNA1 dimers to multiple sites present in the two noncontiguous functional elements of oriP, the dyad symmetry element (DS) from which replication initiates, and the family of repeats (FR) enhancer element. EBNA1 complexes formed on the FR and DS elements of oriP interact by a DNA looping mechanism. This interaction requires EBNA1 sequences in addition to those required for DNA binding and dimerization. To map the EBNA1 sequences required for the efficient interaction of FR- and DS-bound EBNA1 complexes, we have overproduced in Escherichia coli and purified a series of EBNA1 N-terminal truncation mutants, all of which retain the DNA binding and dimerization domains. The results of electron microscopy and ligation-enhancement assays using these mutants indicated that EBNA1 sequences between amino acids 350 and 361 are required for the efficient interaction of FR- and DS-bound EBNA1 complexes. EBNA1-mediated FR-DS interactions were shown to stabilize EBNA1 binding to the DS element, while EBNA1-mediated DS-DS interactions did not. These results suggest that the stabilization of EBNA1 on the DS element, which occurs as a result of EBNA1-mediate oriP looping, may be important for the activation of DNA replication from the DS element.

Authors+Show Affiliations

Molecular Virology and Immunology Program, McMaster University, Hamilton, Ontario, Canada.No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

8288561

Citation

Frappier, L, et al. "Stabilization of the EBNA1 Protein On the Epstein-Barr Virus Latent Origin of DNA Replication By a DNA Looping Mechanism." The Journal of Biological Chemistry, vol. 269, no. 2, 1994, pp. 1057-62.
Frappier L, Goldsmith K, Bendell L. Stabilization of the EBNA1 protein on the Epstein-Barr virus latent origin of DNA replication by a DNA looping mechanism. J Biol Chem. 1994;269(2):1057-62.
Frappier, L., Goldsmith, K., & Bendell, L. (1994). Stabilization of the EBNA1 protein on the Epstein-Barr virus latent origin of DNA replication by a DNA looping mechanism. The Journal of Biological Chemistry, 269(2), 1057-62.
Frappier L, Goldsmith K, Bendell L. Stabilization of the EBNA1 Protein On the Epstein-Barr Virus Latent Origin of DNA Replication By a DNA Looping Mechanism. J Biol Chem. 1994 Jan 14;269(2):1057-62. PubMed PMID: 8288561.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Stabilization of the EBNA1 protein on the Epstein-Barr virus latent origin of DNA replication by a DNA looping mechanism. AU - Frappier,L, AU - Goldsmith,K, AU - Bendell,L, PY - 1994/1/14/pubmed PY - 1994/1/14/medline PY - 1994/1/14/entrez SP - 1057 EP - 62 JF - The Journal of biological chemistry JO - J Biol Chem VL - 269 IS - 2 N2 - DNA replication from the Epstein-Barr virus latent origin of replication, oriP, is activated by Epstein-Barr nuclear antigen 1 (EBNA1). This activation involves the binding of EBNA1 dimers to multiple sites present in the two noncontiguous functional elements of oriP, the dyad symmetry element (DS) from which replication initiates, and the family of repeats (FR) enhancer element. EBNA1 complexes formed on the FR and DS elements of oriP interact by a DNA looping mechanism. This interaction requires EBNA1 sequences in addition to those required for DNA binding and dimerization. To map the EBNA1 sequences required for the efficient interaction of FR- and DS-bound EBNA1 complexes, we have overproduced in Escherichia coli and purified a series of EBNA1 N-terminal truncation mutants, all of which retain the DNA binding and dimerization domains. The results of electron microscopy and ligation-enhancement assays using these mutants indicated that EBNA1 sequences between amino acids 350 and 361 are required for the efficient interaction of FR- and DS-bound EBNA1 complexes. EBNA1-mediated FR-DS interactions were shown to stabilize EBNA1 binding to the DS element, while EBNA1-mediated DS-DS interactions did not. These results suggest that the stabilization of EBNA1 on the DS element, which occurs as a result of EBNA1-mediate oriP looping, may be important for the activation of DNA replication from the DS element. SN - 0021-9258 UR - https://www.unboundmedicine.com/medline/citation/8288561/Stabilization_of_the_EBNA1_protein_on_the_Epstein_Barr_virus_latent_origin_of_DNA_replication_by_a_DNA_looping_mechanism_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0021-9258(17)42220-4 DB - PRIME DP - Unbound Medicine ER -