A role for the human single-Stranded DNA binding protein HSSB/RPA in an early stage of nucleotide excision repair (original) (raw)

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Imperial Cancer Research Fund, Clare Hall Laboratories

South Mimms, Herts EN6 3LD, UK

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Imperial Cancer Research Fund, Clare Hall Laboratories

South Mimms, Herts EN6 3LD, UK

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,

Imperial Cancer Research Fund, Clare Hall Laboratories

South Mimms, Herts EN6 3LD, UK

Search for other works by this author on:

Imperial Cancer Research Fund, Clare Hall Laboratories

South Mimms, Herts EN6 3LD, UK

* To whom correpondence should be addressed

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§ Present addresses: CRC Laboratories, Department of Biochemistry, University of Dundee, DD1 4HN, UK

Author Notes

Published:

11 August 1992

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Dawn Coverley, Mark K. Kenny, David P. Lane, Richard D. Wood, A role for the human single-Stranded DNA binding protein HSSB/RPA in an early stage of nucleotide excision repair, Nucleic Acids Research, Volume 20, Issue 15, 11 August 1992, Pages 3873–3880, https://doi.org/10.1093/nar/20.15.3873
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Abstract

The human single-stranded DNA binding protein (HSSB/RPA) is involved In several processes that maintain the integrity of the genome including DNA replication, homologous recombination, and nucleotide excision repair of damaged DNA. We report studies that analyze the role of HSSB in DNA repair. Specific protein-protein interactions appear to be involved in the repair function of HSSB, since it cannot be replaced by heterologous single-stranded DNA binding proteins. Anti-HSSB antibodies that inhibit the ability of HSSB to stimulate DNA polymerase a also inhibit repair synthesis mediated by human cell-free extracts. However, antibodies that neutralize DNA polymerase a do not inhibit repair synthesis. Repair is sensitive to aphidicolin, suggesting that DNA polymerase e or 5 participates in nucleotide excision repair by cell extracts. HSSB has a role other than generally stimulating synthesis by DNA polymerases, as it does not enhance the residual damage-dependent background synthesis displayed by repair-deficient extracts from xeroderma pigmentosum cells. Significantly, when damaged DNA is incised by the Escherichla coli UvrABC repair enzyme, human cell extracts can carry out repair synthesis even when HSSB has been neutralized with antibodies. This suggests that HSSB functions in an early stage of repair, rather than exclusively in repair synthesis. A model for the role of HSSB in repair Is presented.

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Author notes

§ Present addresses: CRC Laboratories, Department of Biochemistry, University of Dundee, DD1 4HN, UK

© 1992 Oxford University Press

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