ArticleBiochemistry2008
Interactions of human O(6)-alkylguanine-DNA alkyltransferase (AGT) with short double-stranded DNAs.
Article in Biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 29 citations in OpenAlex.
- DNA methylation, nucleic acid structure, and rett mutations tune MeCP2 binding affinity and cooperativity.The Journal of biological chemistry · 2026Article
- The DNA Alkyltransferase Family of DNA Repair Proteins: Common Mechanisms, Diverse Functions.International journal of molecular sciences · 2023Review
- Resolving the subtle details of human DNA alkyltransferase lesion search and repair mechanism by single-molecule studies.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Review
- Quantifying length-dependent DNA end-binding by nucleoproteins.Biophysical chemistry · 2019Article
- Quaternary interactions and supercoiling modulate the cooperative DNA binding of AGT.Nucleic acids research · 2017Article
- Structure-function relationships governing activity and stability of a DNA alkylation damage repair thermostable protein.Nucleic acids research · 2015Article
- Resolving the contributions of two cooperative mechanisms to the DNA binding of AGT.Biopolymers · 2015Article
- Repair of O6-methylguanine adducts in human telomeric G-quadruplex DNA by O6-alkylguanine-DNA alkyltransferase.Nucleic acids research · 2014Article
- Insight into the cooperative DNA binding of the O⁶-alkylguanine DNA alkyltransferase.DNA repair · 2014Review
- Lesion-specific DNA-binding and repair activities of human O⁶-alkylguanine DNA alkyltransferase.Nucleic acids research · 2012Article
- Cooperative cluster formation, DNA bending and base-flipping by O6-alkylguanine-DNA alkyltransferase.Nucleic acids research · 2012Article
- 6-Carboxyfluorescein and structurally similar molecules inhibit DNA binding and repair by O⁶-alkylguanine DNA alkyltransferase.DNA repair · 2011Article
- Multifaceted roles of alkyltransferase and related proteins in DNA repair, DNA damage, resistance to chemotherapy, and research tools.Chemical research in toxicology · 2011Review
- Mutations that probe the cooperative assembly of O⁶-alkylguanine-DNA alkyltransferase complexes.Biochemistry · 2011Article
- Analysis of PKR activation using analytical ultracentrifugation.Macromolecular bioscience · 2010Article
- Hexahistidine-tag-specific optical probes for analyses of proteins and their interactions.Analytical biochemistry · 2010Article
- Repair of O4-alkylthymine by O6-alkylguanine-DNA alkyltransferases.The Journal of biological chemistry · 2010Article
- Topologies of complexes containing O6-alkylguanine-DNA alkyltransferase and DNA.Journal of molecular biology · 2009Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
O(6)-alkylguanine-DNA alkyltransferase (AGT) is a ubiquitous enzyme with an amino acid sequence that is conserved in Eubacteria, Archaea, and Eukarya. It repairs O(6)-alkylguanine and O(4)-alkylthymine adducts in single-stranded and duplex DNAs. In performing these functions, AGT must partition between adduct-containing sites and the large excess of adduct-free DNA distributed throughout the genome. Here, we characterize the binding of human AGT to linear double-stranded, adduct-free DNAs ranging in length from 11 bp to 2686 bp. Moderately cooperative binding (22.6 +/- 3.7 < or = omega < or = 145.0 +/- 37.0) results in an all-or-nothing association pattern on short templates. The apparent binding site size S(app) (mean = 4.39 +/- 0.02 bp) oscillates with increasing template length. Oscillations in cooperativity factor omega have the same frequency but are of opposite phase to S(app), with the result that the most stable protein-protein and protein-DNA interactions occur at the highest packing densities. The oscillation period (4.05 +/- 0.02 bp/protein) is nearly identical to the occluded binding site size obtained at the highest measured binding density (4 bp/protein) and is significantly smaller than the contour length ( approximately 8 bp) occupied in crystalline complexes. A model in which protein molecules overlap along the DNA contour is proposed to account for these features. High AGT densities resulting from cooperative binding may allow efficient search for lesions in the context of chromatin remodeling and DNA replication.
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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.