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Histone H3 Lysine 56 Acetylation Enhances AP Endonuclease 1-Mediated Repair of AP Sites in Nucleosome Core Particles. | LitMetric

Histone H3 Lysine 56 Acetylation Enhances AP Endonuclease 1-Mediated Repair of AP Sites in Nucleosome Core Particles.

Biochemistry

Genome Integrity and Structural Biology Laboratory , National Institute of Environmental Health Sciences, Research Triangle Park , North Carolina 27709 , United States.

Published: September 2019

AI Article Synopsis

  • Understanding how DNA repair is affected by chromatin is crucial as the positioning of nucleosomes can influence mutation rates.
  • The study investigates the role of H3K56 acetylation in DNA base excision repair, specifically how it impacts the activity of AP endonuclease 1 (APE1).
  • Findings indicate that APE1 is more effective at incising strands in the presence of acetylated nucleosomes (H3K56Ac-601-NCPs) compared to unacetylated ones, but the protein HMG box 1, which enhances APE1 activity, does not have the same effect with acetylated nucleosomes.

Article Abstract

Deciphering factors modulating DNA repair in chromatin is of great interest because nucleosomal positioning influences mutation rates. H3K56 acetylation (Ac) is implicated in chromatin landscape regulation, impacting genomic stability, yet the effect of H3K56Ac on DNA base excision repair (BER) remains unclear. We determined whether H3K56Ac plays a role in regulating AP site incision by AP endonuclease 1 (APE1), an early step in BER. Our studies of acetylated, well-positioned nucleosome core particles (H3K56Ac-601-NCPs) demonstrate APE1 strand incision is enhanced compared with that of unacetylated WT-601-NCPs. The high-mobility group box 1 protein enhances APE1 activity in WT-601-NCPs, but this effect is not observed in H3K56Ac-601-NCPs. Therefore, our results suggest APE1 activity on NCPs can be modulated by H3K56Ac.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8865897PMC
http://dx.doi.org/10.1021/acs.biochem.9b00433DOI Listing

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