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

Robert Keller | Zendy; Romina Mossi | Zendy; Giovanni Maga | Zendy; Ralf Erik Wellinger | Zendy; Ulrich Hübscher | Zendy; José M. Sogo | Zendy

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

Author(s) -

Robert Keller,

Romina Mossi,

Giovanni Maga,

Ralf Erik Wellinger,

Ulrich Hübscher,

José M. Sogo

Publication year - 1999

Publication title -

nucleic acids research

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 9.008

H-Index - 537

eISSN - 1362-4954

pISSN - 0305-1048

DOI - 10.1093/nar/27.17.3433

Subject(s) - biology , proliferating cell nuclear antigen , dna replication , dna clamp , replication factor c , replication protein a , primer (cosmetics) , dna , microbiology and biotechnology , dna polymerase delta , dna polymerase ii , hmg box , biophysics , eukaryotic dna replication , dna binding protein , genetics , reverse transcriptase , gene , transcription factor , chemistry , rna , organic chemistry

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.

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