ArticleThe Journal of biological chemistry2011
Polynucleotide kinase and aprataxin-like forkhead-associated protein (PALF) acts as both a single-stranded DNA endonuclease and a single-stranded DNA 3' exonuclease and can participate in DNA end joining in a biochemical system.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 47 citations in OpenAlex.
- Critical DNA damaging pathways in tumorigenesis.Seminars in cancer biology · 2022Review
- The origin of unwanted editing byproducts in gene editing.Acta biochimica et biophysica Sinica · 2022Article
- Review
- Repair of DNA Double-Strand Breaks by the Nonhomologous End Joining Pathway.Annual review of biochemistry · 2021Review
- The molecular basis and disease relevance of non-homologous DNA end joining.Nature reviews. Molecular cell biology · 2020Review
- DNA Damage Response Pathways in Dinoflagellates.Microorganisms · 2019Article
- Evolutionary diversity and novelty of DNA repair genes in asexual Bdelloid rotifers.BMC evolutionary biology · 2018Article
- Nonhomologous DNA end-joining for repair of DNA double-strand breaks.The Journal of biological chemistry · 2018Review
- Effects of DNA end configuration on XRCC4-DNA ligase IV and its stimulation of Artemis activity.The Journal of biological chemistry · 2017Article
- Non-homologous DNA end joining and alternative pathways to double-strand break repair.Nature reviews. Molecular cell biology · 2017Review
- Structural and functional characterization of the PNKP-XRCC4-LigIV DNA repair complex.Nucleic acids research · 2017Article
- Mechanisms of DNA damage, repair, and mutagenesis.Environmental and molecular mutagenesis · 2017Review
- Coordination of DNA single strand break repair.Free radical biology & medicine · 2017Review
- An Intrinsically Disordered APLF Links Ku, DNA-PKcs, and XRCC4-DNA Ligase IV in an Extended Flexible Non-homologous End Joining Complex.The Journal of biological chemistry · 2016Article
- Different DNA End Configurations Dictate Which NHEJ Components Are Most Important for Joining Efficiency.The Journal of biological chemistry · 2016Article
- Programmed DNA breaks in lymphoid cells: repair mechanisms and consequences in human disease.Immunology · 2016Review
- Review
- The structural basis of XRCC1-mediated DNA repair.DNA repair · 2015Review
- Article
- Understanding the DNA damage response in order to achieve desired gene editing outcomes in mosquitoes.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2015Review
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Polynucleotide kinase and aprataxin-like forkhead-associated protein (PALF, also called aprataxin- and PNK-like factor (APLF)) has been shown to have nuclease activity and to use its forkhead-associated domain to bind to x-ray repair complementing defective repair in Chinese hamster cells 4 (XRCC4). Because XRCC4 is a key component of the ligase IV complex that is central to the nonhomologous DNA end joining (NHEJ) pathway, this raises the possibility that PALF might play a role in NHEJ. For this reason, we further studied the nucleolytic properties of PALF, and we searched for any modulation of PALF by NHEJ components. We verified that PALF has 3' exonuclease activity. However, PALF also possesses single-stranded DNA endonuclease activity. This single-stranded DNA endonuclease activity can act at all single-stranded sites except those within four nucleotides 3' of a double-stranded DNA junction, suggesting that PALF minimally requires approximately four nucleotides of single-strandedness. Ku, DNA-dependent protein kinase catalytic subunit, and XRCC4-DNA ligase IV do not modulate PALF nuclease activity on single-stranded DNA or overhangs of duplex substrates. PALF does not open DNA hairpins. However, in a reconstituted end joining assay that includes Ku, XRCC4-DNA ligase IV, and PALF, PALF is able to resect 3' overhanging nucleotides and permit XRCC4-DNA ligase IV to complete the joining process in a manner that is as efficient as Artemis. Reduction of PALF in vivo reduces the joining of incompatible DNA ends. Hence, PALF can function in concert with other NHEJ proteins.
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