http://www.cnr.it/ontology/cnr/individuo/prodotto/ID11791

Nucleophosmin C-terminal leukaemia-associated domain interacts with G-rich quadruplex forming DNA (Articolo in rivista)

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Nucleophosmin C-terminal leukaemia-associated domain interacts with G-rich quadruplex forming DNA (Articolo in rivista) (literal)

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Federici L; Arcovito A; Scaglione GL; Scaloni F; Lo Sterzo C; Di Matteo A; Falini B; Giardina B; Brunori M. (2010)
Nucleophosmin C-terminal leukaemia-associated domain interacts with G-rich quadruplex forming DNA
in The Journal of biological chemistry (Print); American Society Of Biochemistry And Molecular Biology Inc. (ASBMB), Rockville (Stati Uniti d'America)
(literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

Federici L; Arcovito A; Scaglione GL; Scaloni F; Lo Sterzo C; Di Matteo A; Falini B; Giardina B; Brunori M. (literal)

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1. Univ G dAnnunzio, Dept Biomed Sci, I-66013 Chieti, Italy 2. Univ G dAnnunzio, Ce SI Ctr Excellence Aging, I-66013 Chieti, Italy 3. Univ Cattolica Sacro Cuore, Haemostasis Res Ctr, Inst Biochem & Clin Biochem, I-00168 Rome, Italy 4. Univ Cattolica Sacro Cuore, Haemostasis Res Ctr, Dept Internal Med, I-00168 Rome, Italy 5. Univ Roma La Sapienza, Dept Biochem Sci, I-00185 Rome, Italy 6. Fdn Cenci Bolognetti, Ist Pasteur, I-00185 Rome, Italy 7. CNR, Inst Biol & Mol Pathol, I-00185 Rome, Italy 8. Univ Perugia, Inst Hematol, I-06100 Perugia, Italy 9. CNR, Inst Chem Mol Recognit, I-00168 Rome, Italy (literal)

Titolo

Nucleophosmin C-terminal leukaemia-associated domain interacts with G-rich quadruplex forming DNA (literal)

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. (literal)

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