Journal article
RPA involvement in the damage-recognition and incision steps of nucleotide excision repair
Nature (London), Vol.374(6522), pp.566-569
04/1995
DOI: 10.1038/374566a0
PMID: 7700386
Abstract
Human replication protein (RPA) functions in DNA replication, homologous recombination and nucleotide excision repair. This multisubunit single-stranded DNA-binding protein may be required to make unique protein-protein contacts because heterologous single-stranded binding proteins cannot substitute for RPA in these diverse DNA transactions. We report here that, by using affinity chromatography and immunoprecipitation, we found that human RPA bound specifically and directly to two excision repair proteins, the xeroderma pigmentosum damage-recognition protein XPA (refs 8, 9) and the endonuclease XPG (refs 10-13). Although it had been suggested that RPA might function before the DNA synthesis repair stage, our finding that a complex of RPA and XPA showed a striking cooperativity in binding to DNA lesions indicates that RPA may function at the very earliest stage of excision repair. In addition, by binding XPG, RPA may target this endonuclease to damaged DNA.
Details
- Title: Subtitle
- RPA involvement in the damage-recognition and incision steps of nucleotide excision repair
- Creators
- Zhigang HeLeigh A HenricksenMarc S WoldC. James Ingles
- Resource Type
- Journal article
- Publication Details
- Nature (London), Vol.374(6522), pp.566-569
- DOI
- 10.1038/374566a0
- PMID
- 7700386
- ISSN
- 0028-0836
- eISSN
- 1476-4687
- Language
- English
- Date published
- 04/1995
- Academic Unit
- Radiation Oncology; Biochemistry and Molecular Biology
- Record Identifier
- 9984024514202771
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