Abstract
Replication factor C (RF-C) is a eukaryotic heteropentameric protein required for DNA replication and repair processes by loading proliferating cell nuclear antigen (PCNA) onto DNA in an ATP-dependent manner. Prior to loading PCNA, RF-C binds to DNA. This binding is thought to be restricted to a specific DNA structure, namely to a primer/template junction. Using the electron microscope we have examined the affinity of human heteropentameric RF-C and the DNA-binding region within the large subunit of RF-C from Drosophila melanogaster (dRF-Cp140) to heteroduplex DNA. The electron microscopic data indicate that both human heteropentameric RF-C and the DNA-binding region within dRF-Cp140 are sequestered by single-stranded DNA. No preferential affinity for the 3' or 5' transition points from single- to double-stranded DNA was evident.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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DNA, Single-Stranded / chemistry
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DNA, Single-Stranded / physiology*
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DNA, Single-Stranded / ultrastructure
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DNA-Binding Proteins / chemistry
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DNA-Binding Proteins / physiology*
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DNA-Binding Proteins / ultrastructure
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Drosophila / chemistry
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HeLa Cells
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Homeodomain Proteins*
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Humans
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Microscopy, Electron*
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Minor Histocompatibility Antigens
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Nucleic Acid Heteroduplexes / ultrastructure
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Plasmids / chemistry
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Protein Binding
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Proto-Oncogene Proteins c-bcl-2*
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Replication Protein C
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Repressor Proteins*
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Saccharomyces cerevisiae Proteins*
Substances
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BCL2-related protein A1
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DNA, Single-Stranded
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DNA-Binding Proteins
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Homeodomain Proteins
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MATA1 protein, S cerevisiae
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Minor Histocompatibility Antigens
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Nucleic Acid Heteroduplexes
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Proto-Oncogene Proteins c-bcl-2
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Repressor Proteins
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Saccharomyces cerevisiae Proteins
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Replication Protein C