ArticleBiomedicines2020
Nucleus Accumbens-Associated Protein 1 Binds DNA Directly through the BEN Domain in a Sequence-Specific Manner.
Article in Biomedicines, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 19 citations in OpenAlex.
- NAC1 Regulates PCK2 Expression and Activates Truncated Gluconeogenesis for Growth Advantage in Ovarian Cancer Cells.International journal of molecular sciences · 2025Article
- CIAA: Integrated Proteomics and Structural Modeling for Understanding Cysteine Reactivity with Iodoacetamide Alkyne.ACS chemical biology · 2025Article
- NAC1/ACOX2 Axis as a Novel Therapeutic Target for Endometriosis-Related Ovarian Neoplasms.International journal of molecular sciences · 2025Article
- Clinicopathological and molecular characterization of astrocytoma.Frontiers in molecular neuroscience · 2025Article
- Nucleus Accumbens Associated Protein 1 in Cancers-The Real Value.International journal of molecular sciences · 2024Article
- DNA-binding proteins from MBD through ZF to BEN: recognition of cytosine methylation status by one arginine with two conformations.Nucleic acids research · 2024Article
- Nacc1 Mutation in Mice Models Rare Neurodevelopmental Disorder with Underlying Synaptic Dysfunction.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024Article
- Identification and characterization of BEND2 as a key regulator of meiosis during mouse spermatogenesis.Science advances · 2022Article
- Mechanisms and Novel Therapeutic Approaches for Gynecologic Cancer.Biomedicines · 2022Article
- Distinct structural bases for sequence-specific DNA binding by mammalian BEN domain proteins.Genes & development · 2022Article
- A New Case ofFrontiers in pediatrics · 2021Article
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Authors and funding
12 authors at 4 institutions in 1 country.
Funding
Abstract
Nucleus accumbens-associated protein 1 (NAC1) is a nuclear protein that harbors an amino-terminal BTB domain and a carboxyl-terminal BEN domain. NAC1 appears to play significant and diverse functions in cancer and stem cell biology. Here we demonstrated that the BEN domain of NAC1 is a sequence-specific DNA-binding domain. We selected the palindromic 6 bp motif ACATGT as a target sequence by using a PCR-assisted random oligonucleotide selection approach. The interaction between NAC1 and target DNA was characterized by gel shift assays, pull-down assays, isothermal titration calorimetry (ITC), chromatin-immunoprecipitation assays, and NMR chemical shifts perturbation (CSP). The solution NMR structure revealed that the BEN domain of human NAC-1 is composed of five conserved α helices and two short β sheets, with an additional hitherto unknown N-terminal α helix. In particular, ITC clarified that there are two sequential events in the titration of the BEN domain of NAC1 into the target DNA. The ITC results were further supported by CSP data and structure analyses. Furthermore, live cell photobleaching analyses revealed that the BEN domain of NAC1 alone was unable to interact with chromatin/other proteins in cells.
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