ArticlePloS one2014
A DNA sequence recognition loop on APOBEC3A controls substrate specificity.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 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
39 citing papers in PubMed, 55 citations in OpenAlex.
- High-precision cytosine base editors by evolving nucleic-acid-recognition hotspots in deaminase.Nature biotechnology · 2026Article
- Deaminase-driven random mutation enables efficient DNA mutagenesis for protein evolution.Chemical science · 2025Article
- Engineering a bacterial toxin deaminase from the DYW-family into a novel cytosine base editor for plants and mammalian cells.Genome biology · 2025Article
- Deaminase-Driven Reverse Transcription Mutagenesis in Oncogenesis: Critical Analysis of Transcriptional Strand Asymmetries of Single Base Substitution Signatures.International journal of molecular sciences · 2025Review
- Design and Engineering of Light-Induced Base Editors Facilitating Genome Editing with Enhanced Fidelity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Engineered deaminases as a key component of DNA and RNA editing tools.Molecular therapy. Nucleic acids · 2023Review
- Engineering of cytosine base editors with DNA damage minimization and editing scope diversification.Nucleic acids research · 2023Article
- Digital data storage on DNA tape using CRISPR base editors.Nature communications · 2023Article
- Article
- APOBEC3A Catalytic Inactivity Mutation Induces Tertiary Structure Destabilization.ACS medicinal chemistry letters · 2023Article
- APOBEC3: Friend or Foe in Human Papillomavirus Infection and Oncogenesis?Annual review of virology · 2022Review
- The current toolbox for APOBEC drug discovery.Trends in pharmacological sciences · 2022Review
- Single-stranded DNA binding proteins influence APOBEC3A substrate preference.Scientific reports · 2021Article
- The interesting relationship between APOBEC3 deoxycytidine deaminases and cancer: a long road ahead.Open biology · 2020Article
- Current Status and Challenges of DNA Base Editing Tools.Molecular therapy : the journal of the American Society of Gene Therapy · 2020Review
- Computational Investigation of APOBEC3H Substrate Orientation and Selectivity.The journal of physical chemistry. B · 2020Article
- Understanding the structural details of APOBEC3-DNA interactions using graph-based representations.Current research in structural biology · 2020Article
- APOBEC3A Loop 1 Is a Determinant for Single-Stranded DNA Binding and Deamination.Biochemistry · 2019Article
- Pan-cancer transcriptomic analysis dissects immune and proliferative functions of APOBEC3 cytidine deaminases.Nucleic acids research · 2019Article
- RNA-Mediated Dimerization of the Human Deoxycytidine Deaminase APOBEC3H Influences Enzyme Activity and Interaction with Nucleic Acids.Journal of molecular biology · 2018Article
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
APOBEC3A (A3A), one of the seven-member APOBEC3 family of cytidine deaminases, lacks strong antiviral activity against lentiviruses but is a potent inhibitor of adeno-associated virus and endogenous retroelements. In this report, we characterize the biochemical properties of mammalian cell-produced and catalytically active E. coli-produced A3A. The enzyme binds to single-stranded DNA with a Kd of 150 nM and forms dimeric and monomeric fractions. A3A, unlike APOBEC3G (A3G), deaminates DNA substrates nonprocessively. Using a panel of oligonucleotides that contained all possible trinucleotide contexts, we identified the preferred target sequence as TC (A/G). Based on a three-dimensional model of A3A, we identified a putative binding groove that contains residues with the potential to bind substrate DNA and to influence target sequence specificity. Taking advantage of the sequence similarity to the catalytic domain of A3G, we generated A3A/A3G chimeric proteins and analyzed their target site preference. We identified a recognition loop that altered A3A sequence specificity, broadening its target sequence preference. Mutation of amino acids in the predicted DNA binding groove prevented substrate binding, confirming the role of this groove in substrate binding. These findings shed light on how APOBEC3 proteins bind their substrate and determine which sites to deaminate.
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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.