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Repair of O6-ethylguanine in DNA by a chromatin fraction from rat liver: transfer of the ethyl group to an acceptor protein.

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Proceedings of the National Academy of Sciences of the United States of America, 01 Nov 1981, 78(11):6766-6770
https://doi.org/10.1073/pnas.78.11.6766 PMID: 6947250 PMCID: PMC349131

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Abstract 

Incubation of O6-[3H]ethylguanine-containing DNA with a rat liver chromatin fraction resulted in a decrease in the O6-ethylguanine content of the DNA. Analysis of the products of this reaction showed that the ethyl group had been transferred from the O6-ethylguanine to a protein acceptor. When the incubation mixture was separated on a cesium chloride gradient, the radioactivity removed from O6-ethylguanine appeared in a low-density band. This material has been isolated and subjected to trypsin digestion and high-pressure liquid chromatography analysis; it was sensitive to trypsin and the digest contained new high-pressure liquid chromatography peaks characteristic of oligopeptides. Radioactive peaks from the trypsin digestion have been digested further to the amino acid level and have been shown to contain S-[3H]ethylcysteine. Thus, we conclude that the repair activity in rat liver chromatin removes the ethyl group from O6-ethylguanine and transfers it to a cysteine moiety contained in an acceptor protein.

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Proc Natl Acad Sci U S A. 1981 Nov; 78(11): 6766–6770.
PMCID: PMC349131
PMID: 6947250

Repair of O6-ethylguanine in DNA by a chromatin fraction from rat liver: transfer of the ethyl group to an acceptor protein.

J R Mehta, D B Ludlum, A Renard, and W G Verly
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Abstract

Incubation of O6-[3H]ethylguanine-containing DNA with a rat liver chromatin fraction resulted in a decrease in the O6-ethylguanine content of the DNA. Analysis of the products of this reaction showed that the ethyl group had been transferred from the O6-ethylguanine to a protein acceptor. When the incubation mixture was separated on a cesium chloride gradient, the radioactivity removed from O6-ethylguanine appeared in a low-density band. This material has been isolated and subjected to trypsin digestion and high-pressure liquid chromatography analysis; it was sensitive to trypsin and the digest contained new high-pressure liquid chromatography peaks characteristic of oligopeptides. Radioactive peaks from the trypsin digestion have been digested further to the amino acid level and have been shown to contain S-[3H]ethylcysteine. Thus, we conclude that the repair activity in rat liver chromatin removes the ethyl group from O6-ethylguanine and transfers it to a cysteine moiety contained in an acceptor protein.

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Selected References

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