Histone modification via rapid cleavage of C4′-oxidized abasic sites in nucleosome core particles

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[1] Zhou, Chuanzheng
[2] Sczepanski, Jonathan T.
[3] Greenberg, Marc M.
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Greenberg, M.M. (mgreenberg@jhu.edu) | 1600年 / American Chemical Society卷 / 135期
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The C4′-oxidized abasic site is produced in DNA by a variety of oxidizing agents; including potent cytotoxic antitumor agents. Independent generation of this alkali-labile lesion at defined positions within nucleosome core particles reveals that the histone proteins increase strand scission between 130- and 550-fold. Strand scission proceeds via a Schiff base intermediate; but the DNA-protein cross-links are unstable. The oxidized abasic site is removed in its entirety from the DNA and transferred to the lysine-rich tail region of the proximal histone protein in the form of a lactam. The modification is distributed over several residues within the amino-terminal tail of the proximal histone. Transfer of DNA damage to histones could affect gene regulation. © 2013 American Chemical Society;
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