ArticleProtein expression and purification2012
Expression and purification of active mouse and human NEIL3 proteins.
Article in Protein expression and purification, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 47 citations in OpenAlex.
- DNA repair and disease: insights from the human DNA glycosylase NEIL family.Experimental & molecular medicine · 2025Review
- Structure andmBio · 2024Article
- Review
- Structural and biochemical insights into NEIL2's preference for abasic sites.Nucleic acids research · 2023Article
- An autoinhibitory role for the GRF zinc finger domain of DNA glycosylase NEIL3.The Journal of biological chemistry · 2020Article
- Unhooking of an interstrand cross-link at DNA fork structures by the DNA glycosylase NEIL3.DNA repair · 2020Article
- Emerging Roles of DNA Glycosylases and the Base Excision Repair Pathway.Trends in biochemical sciences · 2019Review
- The Biochemical Role of the Human NEIL1 and NEIL3 DNA Glycosylases on Model DNA Replication Forks.Genes · 2019Article
- Article
- Article
- Processing of NDNA repair · 2019Article
- The Human DNA glycosylases NEIL1 and NEIL3 Excise Psoralen-Induced DNA-DNA Cross-Links in a Four-Stranded DNA Structure.Scientific reports · 2017Article
- NEIL3 Repairs Telomere Damage during S Phase to Secure Chromosome Segregation at Mitosis.Cell reports · 2017Article
- Formation and processing of DNA damage substrates for the hNEIL enzymes.Free radical biology & medicine · 2017Review
- A genome-wide analysis of gene-caffeine consumption interaction on basal cell carcinoma.Carcinogenesis · 2016Article
- Deficiency of base excision repair enzyme NEIL3 drives increased predisposition to autoimmunity.The Journal of clinical investigation · 2016Article
- Article
- The NEIL glycosylases remove oxidized guanine lesions from telomeric and promoter quadruplex DNA structures.Nucleic acids research · 2015Article
- Repair of oxidative DNA damage and cancer: recent progress in DNA base excision repair.Antioxidants & redox signaling · 2014Review
- DNA glycosylases search for and remove oxidized DNA bases.Environmental and molecular mutagenesis · 2013Review
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Endonuclease VIII-like 3 (Neil3) is one of the five DNA glycosylases found in mammals that recognize and remove oxidized bases, and initiate the base excision repair (BER) pathway. Previous attempts to express and purify the mouse and human orthologs of Neil3 in their active form have not been successful. Here we report the construction of bicistronic expression vectors for expressing in Escherichia coli the full-length mouse Neil3 (MmuNeil3), its glycosylase domain (MmuNeil3Δ324), as well as the glycosylase domain of human Neil3 (NEIL3Δ324). The purified Neil3 proteins are all active, and NEIL3Δ324 exhibits similar glycosylase/lyase activity as MmuNeil3Δ324 on both single-stranded and double-stranded substrates containing thymine glycol (Tg), spiroiminodihydantoin (Sp) or an abasic site (AP). We show that N-terminal initiator methionine processing is critical for the activity of both mouse and human Neil3 proteins. Co-expressing an E. coli methionine aminopeptidase (EcoMap) Y168A variant with MmuNeil3, MmuNeil3Δ324 and NEIL3Δ324 improves the N-terminal methionine processing and increases the percentage of active Neil3 proteins in the preparation. The purified Neil3 proteins are suitable for biochemical, structural and functional studies.
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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.