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Repair of O-alkylpyrimidines in Mammalian Cells: A Present Consensus
T. P. Brent, M. E. Dolan, H. Fraenkel-Conrat, J. Hall, P. Karran, F. Laval, G. P. Margison, R. Montesano, A. E. Pegg, P. M. Potter, B. Singer, J. A. Swenberg and D. B. Yarosh
Proceedings of the National Academy of Sciences of the United States of America
Vol. 85, No. 6 (Mar. 15, 1988), pp. 1759-1762
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/31384
Page Count: 4
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Enzymatic repair of the O-alkylpyrimidines (O2- and O4-alkylthymine, O2-alkylcytosine) and alkyl phosphotriesters has been studied in Escherichia coli, and the two proteins involved, a glycosylase (DNA-3-methyladenine glycosylase) and a methyltransferase (DNA-O6-methylguanine:protein-L-cysteine S-methyltransferase, EC 220.127.116.11), have been well characterized. In mammals or mammalian cells treated with carcinogenic alkylating agents, loss of these derivatives has been demonstrated repeatedly. Nevertheless, mammalian repair proteins that are analogous to those from E. coli do not detectably act on these alkyl derivatives. A variety of techniques has been used by many investigators in the United States and Europe, who conclude here that the mode of O-alkylpyrimidine and alkyl phosphotriester repair in mammalian cells differs from that in E. coli. New approaches and methods are needed to characterize these processes at the biochemical and molecular level.
Proceedings of the National Academy of Sciences of the United States of America © 1988 National Academy of Sciences