ArticleProceedings of the National Academy of Sciences of the United States of America2011
Structural basis for the phosphatase activity of polynucleotide kinase/phosphatase on single- and double-stranded DNA substrates.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
24 citing papers in PubMed, 32 citations in OpenAlex.
- Structural basis of end processing in the nucleosome by polynucleotide kinase phosphatase.bioRxiv : the preprint server for biology · 2026Article
- Multi-omics analysis in suspected hereditary breast and ovarian cancer cases reveals novel candidate susceptibility factors.NPJ breast cancer · 2026Article
- B-cell immunodeficiency associated with polynucleotide kinase 3'-phosphatase (PNKP) deficiency.The journal of allergy and clinical immunology. Global · 2025Article
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- CDK-dependent phosphorylation regulates PNKP function in DNA replication.The Journal of biological chemistry · 2024Article
- Structure and mechanism in non-homologous end joining.DNA repair · 2023Article
- Mutations of the DNA repair gene PNKP in a patient with microcephaly, seizures, and developmental delay (MCSZ) presenting with a high-grade brain tumor.Scientific reports · 2022Article
- Species variations in XRCC1 recruitment strategies for FHA domain-containing proteins.DNA repair · 2022Article
- Targeting DNA repair with PNKP inhibition sensitizes radioresistant prostate cancer cells to high LET radiation.PloS one · 2018Article
- Grc3 programs the essential endoribonuclease Las1 for specific RNA cleavage.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Structural and functional characterization of the PNKP-XRCC4-LigIV DNA repair complex.Nucleic acids research · 2017Article
- Protecting DNA from errors and damage: an overview of DNA repair mechanisms in plants compared to mammals.Cellular and molecular life sciences : CMLS · 2017Review
- Characterization of DNA Substrate Binding to the Phosphatase Domain of the DNA Repair Enzyme Polynucleotide Kinase/Phosphatase.Biochemistry · 2017Article
- Characterization of Runella slithyformis HD-Pnk, a Bifunctional DNA/RNA End-Healing Enzyme Composed of an N-Terminal 2',3'-Phosphoesterase HD Domain and a C-Terminal 5'-OH Polynucleotide Kinase Domain.Journal of bacteriology · 2017Article
- Recognition and repair of chemically heterogeneous structures at DNA ends.Environmental and molecular mutagenesis · 2015Review
- Structures of bacterial polynucleotide kinase in a michaelis complex with nucleoside triphosphate (NTP)-Mg2+ and 5'-OH RNA and a mixed substrate-product complex with NTP-Mg2+ and a 5'-phosphorylated oligonucleotide.Journal of bacteriology · 2014Article
- Nonhomologous end joining: a good solution for bad ends.DNA repair · 2014Review
- Rewriting the rules for end joining via enzymatic splicing of DNA 3'-PO4 and 5'-OH ends.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Repair of double-strand breaks by end joining.Cold Spring Harbor perspectives in biology · 2013Review
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Polynucleotide kinase/phosphatase (PNKP) is a critical mammalian DNA repair enzyme that generates 5'-phosphate and 3'-hydroxyl groups at damaged DNA termini that are required for subsequent processing by DNA ligases and polymerases. The PNKP phosphatase domain recognizes 3'-phosphate termini within DNA nicks, gaps, or at double- or single-strand breaks. Here we present a mechanistic rationale for the recognition of damaged DNA termini by the PNKP phosphatase domain. The crystal structures of PNKP bound to single-stranded DNA substrates reveals a narrow active site cleft that accommodates a single-stranded substrate in a sequence-independent manner. Biochemical studies suggest that the terminal base pairs of double-stranded substrates near the 3'-phosphate are destabilized by PNKP to allow substrate access to the active site. A positively charged surface distinct from the active site specifically facilitates interactions with double-stranded substrates, providing a complex DNA binding surface that enables the recognition of diverse substrates.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.