Histone modification via rapid cleavage of C4'-oxidized abasic sites in nucleosome core particles. Academic Article uri icon

abstract

  • 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.

author list (cited authors)

  • Zhou, C., Sczepanski, J. T., & Greenberg, M. M

complete list of authors

  • Zhou, Chuanzheng||Sczepanski, Jonathan T||Greenberg, Marc M

publication date

  • January 1, 2013 11:11 AM