Nucleosome core particle-catalyzed strand scission at abasic sites.

ABSTRACT: The reactivity of apurinic/apyrimidinic (AP) sites at different locations within nucleosome core particles was examined. AP sites are greatly destabilized in nucleosome core particles compared to free DNA. Their reactivity varied ~5-fold with respect to the location within the nucleosome core particles but followed a common mechanism involving formation of a Schiff base between histone proteins and the lesion. The identity of the histone protein(s) involved in the reaction and the reactivity of the corresponding DNA-protein cross-links varied with the location of the abasic site, indicating that while the relative rate constants for individual steps varied in a complex manner, the overall mechanism remained the same. The source of the accelerated reactivity was probed using nucleosomes con

SUBMITTER: Sczepanski JT 

PROVIDER: S-EPMC3718853 | biostudies-literature | 2013 Mar

REPOSITORIES: biostudies-literature