ArticleJournal of molecular biology2013
The disordered C-terminal domain of human DNA glycosylase NEIL1 contributes to its stability via intramolecular interactions.
Article in Journal of molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 48 citations in OpenAlex.
- Development and characterization of a novel NEIL1 nanobody.DNA repair · 2025Article
- Research progress on the role of the NEIL family in cancer.Frontiers in cell and developmental biology · 2025Review
- How the Intrinsically Disordered N-Terminus of Cancer/Testis Antigen MAGEA10 Is Responsible for Its Expression, Nuclear Localisation and Aberrant Migration.Biomolecules · 2023Article
- Divergent structures of Mammalian and gammaherpesvirus uracil DNA glycosylases confer distinct DNA binding and substrate activity.DNA repair · 2023Article
- Noncatalytic Domains in DNA Glycosylases.International journal of molecular sciences · 2022Review
- Universally Accessible Structural Data on Macromolecular Conformation, Assembly, and Dynamics by Small Angle X-Ray Scattering for DNA Repair Insights.Methods in molecular biology (Clifton, N.J.) · 2022Article
- X-ray scattering reveals disordered linkers and dynamic interfaces in complexes and mechanisms for DNA double-strand break repair impacting cell and cancer biology.Protein science : a publication of the Protein Society · 2021Review
- Heritable pattern of oxidized DNA base repair coincides with pre-targeting of repair complexes to open chromatin.Nucleic acids research · 2021Article
- Macromolecular crowding induces compaction and DNA binding in the disordered N-terminal domain of hUNG2.DNA repair · 2020Article
- A multi-faceted genotoxic network of alpha-synuclein in the nucleus and mitochondria of dopaminergic neurons in Parkinson's disease: Emerging concepts and challenges.Progress in neurobiology · 2020Review
- The C-terminal tail of the NEIL1 DNA glycosylase interacts with the human mitochondrial single-stranded DNA binding protein.DNA repair · 2018Article
- Article
- Destabilization of the PCNA trimer mediated by its interaction with the NEIL1 DNA glycosylase.Nucleic acids research · 2017Article
- Human Apurinic/Apyrimidinic Endonuclease (APE1) Is Acetylated at DNA Damage Sites in Chromatin, and Acetylation Modulates Its DNA Repair Activity.Molecular and cellular biology · 2017Article
- Crystal structure of mimivirus uracil-DNA glycosylase.PloS one · 2017Article
- What Combined Measurements From Structures and Imaging Tell Us About DNA Damage Responses.Methods in enzymology · 2017Review
- Conformational characterization of the intrinsically disordered protein Chibby: Interplay between structural elements in target recognition.Protein science : a publication of the Protein Society · 2016Article
- Tautomerization-dependent recognition and excision of oxidation damage in base-excision DNA repair.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Regulation of limited N-terminal proteolysis of APE1 in tumor via acetylation and its role in cell proliferation.Oncotarget · 2016Article
- Phosphorylation Sites Identified in the NEIL1 DNA Glycosylase Are Potential Targets for the JNK1 Kinase.PloS one · 2016Article
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
NEIL1 [Nei (endonuclease VIII)-like protein 1], one of the five mammalian DNA glycosylases that excise oxidized DNA base lesions in the human genome to initiate base excision repair, contains an intrinsically disordered C-terminal domain (CTD; ~100 residues), not conserved in its Escherichia coli prototype Nei. Although dispensable for NEIL1's lesion excision and AP lyase activities, this segment is required for efficient in vivo enzymatic activity and may provide an interaction interface for many of NEIL1's interactions with other base excision repair proteins. Here, we show that the CTD interacts with the folded domain in native NEIL1 containing 389 residues. The CTD is poised for local folding in an ordered structure that is induced in the purified fragment by osmolytes. Furthermore, deletion of the disordered tail lacking both Tyr and Trp residues causes a red shift in NEIL1's intrinsic Trp-specific fluorescence, indicating a more solvent-exposed environment for the Trp residues in the truncated protein, which also exhibits reduced stability compared to the native enzyme. These observations are consistent with stabilization of the native NEIL1 structure via intramolecular, mostly electrostatic, interactions that were disrupted by mutating a positively charged (Lys-rich) cluster of residues (amino acids 355-360) near the C-terminus. Small-angle X-ray scattering (SAXS) analysis confirms the flexibility and dynamic nature of NEIL1's CTD, a feature that may be critical to providing specificity for NEIL1's multiple, functional interactions.
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