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R-loops processing by human apurinic/apyrimidinic endonuclease APE1
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DOI：10.1016/j.biochi.2026.03.012.png)
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Abstract
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R-loops are three-stranded nucleic acid structures that arise during transcription and play important roles in genome regulation, but their unscheduled accumulation can lead to genomic instability. Apurinic/apyrimidinic endonuclease 1 (APE1) is a multifunctional enzyme mainly involved in base excision DNA repair. However, APE1, being both nuclear and cytoplasmic enzyme, could be also considered as important participant of RNA metabolism through their endo- and exoribonuclease as well as RNase H activities. This study investigates the ability of APE1 to process R-loop structures through its various enzymatic activities in vitro. We demonstrate that APE1 exhibits RNase H activity on DNA:RNA hybrids within R-loops, with efficiency decreasing as hybrid length increases beyond 16 nucleotides. Additionally, APE1 cleaves abasic sites in both RNA and DNA strands of R-loops via its APendonuclease activity. Notably, an abasic site in the RNA strand is efficiently processed followed by robust 3 '-5 ' exoribonuclease degradation, while an abasic site in the DNA strand is cleaved less efficiently and strongly inhibits RNase H activity. This functional versatility reinforces the importance of APE1 in nucleic acid metabolism, offering new insights into its biological significance beyond traditional DNA repair pathways. (c) 2026 Elsevier B.V. and Soci & eacute;t & eacute; Fran & ccedil;aise de Biochimie et Biologie Mol & eacute;culaire (SFBBM). All rights are reserved, including those for text and data mining, AI training, and similar technologies.
Keywords:
Human apurinic/apyrimidinic
endonuclease 1 APE1
R-loops
RNase H activity
AP-Endonuclease activity
Multifunctional enzymes
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