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

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.

journal_name

Nucleic Acids Res

journal_title

Nucleic acids research

authors

Keller RC,Mossi R,Maga G,Wellinger RE,Hübscher U,Sogo JM

doi

10.1093/nar/27.17.3433

keywords:

subject

Has Abstract

pub_date

1999-09-01 00:00:00

pages

3433-7

issue

17

eissn

0305-1048

issn

1362-4962

pii

gkc534

journal_volume

27

pub_type

杂志文章

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