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Structure and Mechanism of Hydroxyl Radical-induced Formation of a DNA-Protein Cross-Link Involving Thymine and Lysine in Nucleohistone

Center for Chemical Technology, National Institute of Standards and Technology, Gaithersburg, Maryland 20899

Hydroxyl radical-induced formation of a DNA-protein cross-link involving thymine and lysine in calf thymus nucleohistone in vitro is reported. Basic amino acids such as lysine constitute a very high proportion of the amino acids of histones, and help histones to bind to DNA in chromatin. For this reason, basic amino acids are likely to participate in DNA-protein cross-linking. For identification of the thymine-lysine cross-link in nucleohistone, hydroxyl radical-induced cross-linking of thymine to lysine was investigated first using a model system, i.e., an aqueous mixture of thymine and lysine. Hydroxyl radicals were generated by exposure of this mixture to ionizing radiation after N₂O saturation. The technique of gas chromatography-mass spectrometry was used to analyze the samples for possible cross-links. One thymine-lysine cross-link was found and its structure was elucidated. Using gas chromatography-mass spectrometry with selected-ion monitoring, this thymine-lysine cross-link was identified in acidic hydrolysates of calf thymus nucleohistone -irradiated in N₂O-saturated aqueous solution. The yield of this DNA-protein cross-link was also measured and found to be a linear function of radiation dose between 15 and 200 Gy. This yield amounted to 0.0085 µmol/J. Possible mechanisms for the formation of this DNA-protein cross-link in nucleohistone were proposed.

¹ To whom requests for reprints should be addressed.

Received 2/ 1/89. Revised 3/30/89. Accepted 4/ 5/89.

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