Abstract
RPA is the replicative single-strand DNA (ssDNA) binding protein of eukaryotic chromosomes. This report shows that human RPA interacts with EBNA1, the latent origin binding protein of Epstein-Barr virus (EBV). RPA binds to EBNA1 both in solution, and when EBNA1 is bound to the EBV origin. RPA is a heterotrimer, and the main contact with EBNA1 is formed through the 70 kDa subunit of RPA, the subunit which binds to ssDNA. We propose that this interaction between RPA and EBNA1 is an early step in activation of the latent origin of EBV.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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DNA, Viral / chemistry
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DNA, Viral / metabolism
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DNA-Binding Proteins / genetics
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DNA-Binding Proteins / metabolism*
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Dimerization
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Epstein-Barr Virus Nuclear Antigens / genetics
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Epstein-Barr Virus Nuclear Antigens / metabolism*
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Escherichia coli / genetics
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Herpesvirus 4, Human / genetics
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Humans
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Peptide Fragments / genetics
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Peptide Fragments / metabolism
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Recombinant Proteins / metabolism
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Replication Protein A
Substances
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DNA, Viral
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DNA-Binding Proteins
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Epstein-Barr Virus Nuclear Antigens
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Peptide Fragments
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RPA1 protein, human
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Recombinant Proteins
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Replication Protein A