Nucleic Acids Research, Vol 26, Issue 19 4462-4470, Copyright © 1998 by Oxford University Press
TM Avolio-Hunter and L Frappier
The DNA replication, plasmid segregation and transactivation functions of
Epstein-Barr nuclear antigen 1 (EBNA1) require the binding of EBNA1 to
specific DNA recognition sites in the two non-contiguous functional
elements of the Epstein-Barr virus latent origin of replication, oriP .
EBNA1 molecules bound to these elements interact with each other resulting
in the formation of looped individual DNA molecules and multiply linked DNA
molecules. We have developed a glycerol gradient sedimentation assay
suitable for quantitative analysis of the DNA linking activity of EBNA1 and
used it to investigate the contribution of EBNA1 residues to the linking
interaction and the mechanism of the interaction. Using overlapping
internal deletion mutants, we found that two regions of EBNA1 can cause DNA
linking, amino acids 40-100 and 327- 377, but that the stabilities of the
linked complexes formed by the two regions differ dramatically; only
complexes formed through the latter region are stable to glycerol gradient
sedimentation analysis. Mechanistic studies using EBNA1 in combination with
GAL4-EBNA1 fusion proteins showed that linking interactions mediated by
residues 327-377 are homotypic. Our results also suggest that only the
DNA-bound form of EBNA1 participates in the protein-protein interactions
seen in DNA linking.
ARTICLES
Mechanistic studies on the DNA linking activity of Epstein-Barr nuclear antigen 1
Department of Medical Genetics and Microbiology, University of Toronto, 1 Kings College Circle, Toronto, Ontario, Canada.
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