Abstract
The purified human single-stranded DNA binding protein, replication protein A (RP-A), forms specific complexes with purified SV40 large T antigen and with purified DNA polymerase alpha-primase, as shown by ELISA and a modified immunoblotting technique. RP-A associated efficiently with the isolated primase, as well as with intact polymerase alpha-primase. The 70 kDa subunit of RP-A was sufficient for association with polymerase alpha-primase. Purified SV40 large T antigen bound to intact RP-A and to polymerase-primase, but not to any of the separated subunits of RP-A or to the isolated primase. These results suggest that the specific protein-protein interactions between RP-A, polymerase-primase and T antigen may play a role in the initiating of SV40 DNA replication.
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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Amino Acid Sequence
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Animals
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Antibodies, Monoclonal
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Antigens, Polyomavirus Transforming / metabolism*
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Cattle
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DNA Primase
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DNA-Binding Proteins / metabolism*
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Enzyme-Linked Immunosorbent Assay
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Escherichia coli / metabolism*
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Immunoblotting
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Kinetics
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Macromolecular Substances
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Models, Structural
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Molecular Sequence Data
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Protein Binding
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Protein Conformation
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RNA Nucleotidyltransferases / isolation & purification
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RNA Nucleotidyltransferases / metabolism*
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Replication Protein A
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Simian virus 40 / metabolism*
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Thymus Gland / enzymology
Substances
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Antibodies, Monoclonal
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Antigens, Polyomavirus Transforming
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DNA-Binding Proteins
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Macromolecular Substances
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Replication Protein A
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DNA Primase
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RNA Nucleotidyltransferases