ArticleThe Journal of biological chemistry2010
Nucleophosmin C-terminal leukemia-associated domain interacts with G-rich quadruplex forming DNA.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 63 citations in OpenAlex.
- Collision-induced transfer enhances ligand-binding kinetics in guanine quadruplex DNA.Nucleic acids research · 2026Article
- Multisite phosphorylation of the AML-linked C-terminal of nucleophosmin (NPM1) orchestrates protein stability, DNA binding and charge block-driven phase separation.Nucleic acids research · 2026Article
- Identifying G-quadruplex-interacting proteins in cancer-related gene promoters.Communications chemistry · 2025Article
- Profiling of i-motif-binding proteins reveals functional roles of nucleolin in regulation of high-order DNA structures.Nucleic acids research · 2024Article
- The Histone Chaperones SET/TAF-1β and NPM1 Exhibit Conserved Functionality in Nucleosome Remodeling and Histone Eviction in a Cytochrome c-Dependent Manner.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Nucleolus assembly impairment leads to two-cell transcriptional repression via NPM1-mediated PRC2 recruitment.Nature structural & molecular biology · 2023Article
- A Quantitative Proteomic Approach for the Identification of DNA Guanine Quadruplex-Binding Proteins.Journal of proteome research · 2021Article
- BG-flow, a new flow cytometry tool for G-quadruplex quantification in fixed cells.BMC biology · 2021Article
- G-quadruplexes: a promising target for cancer therapy.Molecular cancer · 2021Review
- Nucleophosmin in Its Interaction with Ligands.International journal of molecular sciences · 2020Review
- NPM1 upregulates the transcription of PD-L1 and suppresses T cell activity in triple-negative breast cancer.Nature communications · 2020Article
- New insights into the biology of acute myeloid leukemia with mutated NPM1.International journal of hematology · 2019Review
- C9orf72 Poly(PR) Dipeptide Repeats Disturb Biomolecular Phase Separation and Disrupt Nucleolar Function.Molecular cell · 2019Article
- Nucleoli in embryos: a central structural platform for embryonic chromatin remodeling?Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2019Review
- Human AP-endonuclease (Ape1) activity on telomeric G4 structures is modulated by acetylatable lysine residues in the N-terminal sequence.DNA repair · 2019Article
- Self-interaction of NPM1 modulates multiple mechanisms of liquid-liquid phase separation.Nature communications · 2018Article
- Conformational stabilization as a strategy to prevent nucleophosmin mislocalization in leukemia.Scientific reports · 2017Article
- Article
- Structural investigation of nucleophosmin interaction with the tumor suppressor Fbw7γ.Oncogenesis · 2017Article
- Chromosomal passenger complex hydrodynamics suggests chaperoning of the inactive state by nucleoplasmin/nucleophosmin.Molecular biology of the cell · 2017Article
Corrections and comments
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Authors and funding
9 authors at 7 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nucleophosmin (NPM1) is a nucleocytoplasmic shuttling phosphoprotein, mainly localized at nucleoli, that plays a key role in ribogenesis, centrosome duplication, and response to stress stimuli. Mutations at the C-terminal domain of NPM1 are the most frequent genetic lesion in acute myeloid leukemia and cause the aberrant and stable translocation of the protein in the cytoplasm. The NPM1 C-terminal domain was previously shown to bind nucleic acids. Here we further investigate the DNA binding properties of the NPM1 C-terminal domain both at the protein and nucleic acid levels; we investigate the domain boundaries and identify key residues for high affinity recognition. Furthermore, we demonstrate that the NPM1 C-terminal domain has a preference for G-quadruplex forming DNA regions and induces the formation of G-quadruplex structures in vitro. Finally we show that a specific sequence found at the SOD2 gene promoter, which was previously shown to be a target of NPM1 in vivo, is indeed folded as a G-quadruplex in vitro under physiological conditions. Our data extend considerably present knowledge on the DNA binding properties of NPM1 and suggest a general role in the transcription of genes characterized by the presence of G-quadruplex forming regions at their promoters.
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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.