ArticleDNA repair2008
Activation-induced deaminase, AID, is catalytically active as a monomer on single-stranded DNA.
Article in DNA repair, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 45 citations in OpenAlex.
- Article
- TargetedACS synthetic biology · 2023Article
- Small-Angle X-ray Scattering Models of APOBEC3B Catalytic Domain in a Complex with a Single-Stranded DNA Inhibitor.Viruses · 2021Article
- HPV Meets APOBEC: New Players in Head and Neck Cancer.International journal of molecular sciences · 2021Review
- APOBEC: A molecular driver in cervical cancer pathogenesis.Cancer letters · 2021Review
- Modeling the Embrace of a Mutator: APOBEC Selection of Nucleic Acid Ligands.Trends in biochemical sciences · 2018Review
- Biochemical Regulatory Features of Activation-Induced Cytidine Deaminase Remain Conserved from Lampreys to Humans.Molecular and cellular biology · 2017Article
- Review
- Functions and Malfunctions of Mammalian DNA-Cytosine Deaminases.Chemical reviews · 2016Review
- Structural and functional assessment of APOBEC3G macromolecular complexes.Methods (San Diego, Calif.) · 2016Article
- The APOBEC Protein Family: United by Structure, Divergent in Function.Trends in biochemical sciences · 2016Review
- Functional requirements of AID's higher order structures and their interaction with RNA-binding proteins.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Mismatch repair proteins and AID activity are required for the dominant negative function of C-terminally deleted AID in class switching.Journal of immunology (Baltimore, Md. : 1950) · 2014Article
- AID and Apobec3G haphazard deamination and mutational diversity.Cellular and molecular life sciences : CMLS · 2013Review
- Epigenetic reprogramming: is deamination key to active DNA demethylation?Reproduction (Cambridge, England) · 2011Review
- Atomic force microscopy studies provide direct evidence for dimerization of the HIV restriction factor APOBEC3G.The Journal of biological chemistry · 2011Article
- Heat shock protein 70 (Hsp70)-stimulated deoxycytidine deaminases from a human lymphoma cell but not the activation-induced cytidine deaminase (AID) from Ramos 6.4 human Burkitt's lymphoma cells.Cell stress & chaperones · 2011Article
- The activation-induced cytidine deaminase (AID) efficiently targets DNA in nucleosomes but only during transcription.The Journal of experimental medicine · 2009Article
- APOBEC3G subunits self-associate via the C-terminal deaminase domain.The Journal of biological chemistry · 2008Article
- A model for oligomeric regulation of APOBEC3G cytosine deaminase-dependent restriction of HIV.The Journal of biological chemistry · 2008Article
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6 authors at 2 institutions in 1 country.
Funding
Abstract
Hypermutation and class switch recombination of immunoglobulin genes are antigen-activated mechanisms triggered by AID, a cytidine deaminase. AID deaminates cytidine residues in the DNA of the variable and the switch regions of the immunoglobulin locus. The resulting uracil induces error-prone DNA synthesis in the case of hypermutation or DNA breaks that activate non-homologous recombination in the case of class switch recombination. In vitro studies have demonstrated that AID deaminates single-stranded but not double-stranded substrates unless AID is in a complex with RPA and the substrate is actively undergoing transcription. However, it is not clear whether AID deaminates its substrates primarily as a monomer or as a higher order oligomer. To examine the oligomerization state of AID alone and in the presence of single-stranded DNA substrates of various structures, including loops embedded in double-stranded DNA, we used atomic force microscopy (AFM) to visualize AID protein alone or in complex with DNA. Surprisingly, AFM results indicate that most AID molecules exist as a monomer and that it binds single-stranded DNA substrates as a monomer at concentrations where efficient deamination of single-stranded DNA substrates occur. The rate of deamination, under conditions of excess and limiting protein, also imply that AID can deaminate single-stranded substrates as a monomer. These results imply that non-phosphorylated AID is catalytically active as a monomer on single-stranded DNA in vitro, including single-stranded DNA found in loops similar to those transiently formed in the immunoglobulin switch regions during transcription.
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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.