Electron microscopic analysis reveals that replication factor C is sequestered by single-stranded DNA

Replication factor C (RF-C) is a eukaryotic hetero-pentameric 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 sp...

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Veröffentlicht in:Nucleic acids research 1999-09, Vol.27 (17), p.3433-3437
Hauptverfasser: Keller, Robert C., Mossi, Romina, Maga, Giovanni, Wellinger, Ralf E., Hubscher, Ulrich, Sogo, José M.
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Sprache:eng
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Zusammenfassung:Replication factor C (RF-C) is a eukaryotic hetero-pentameric 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.
ISSN:0305-1048
1362-4962
DOI:10.1093/nar/27.17.3433