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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1979 Jan;76(1):141–144. doi: 10.1073/pnas.76.1.141

DNA binding activity from cultured human fibrolasts that is specific for partially depurinated DNA and that inserts purines into apurinic sites.

W A Deutsch, S Linn
PMCID: PMC382892  PMID: 218192

Abstract

A protein of molecular weight approximately 120,000 was isolated from cultured human fibroblasts and HeLa cells on the basis of its ability to bind specifically to apurinic DNA. After separation from apurinic endonuclease activity, the protein was found to incorporate purine, but not pyrimidine, bases specifically into depurinated DNA so as to protect the apurinic sites from alkali. Purine base insertion activity was sensitive to heating and freezing as well as to caffeine and EDTA; it required K+ but not a divalent cation. Guanine, but not adenine, was incorporated into depurinated poly(dG-dC), whereas adenine, but not guanine, was incorporated into poly(dA-dT). After incorporation into depurinated DNA, guanine could be reisolated as dGMP. Although this activity suggests an alternative pathway for DNA repair that is independent of nucleotide excision, other functions for such an enzyme are possible.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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