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Federici, L. et al.

Luca Federici, Alessandro Arcovito, Giovanni L. Scaglione, Flavio Scaloni, Carlo Lo Sterzo, Adele Di Matteo, Brunangelo Falini, Bruno Giardina, Maurizio Brunori,

Nucleophosmin C-terminal leukemia-associated domain interacts with G-rich quadruplex forming DNA.

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.[1]

References

Nucleophosmin C-terminal leukemia-associated domain interacts with G-rich quadruplex forming DNA. Federici, L., Arcovito, A., Scaglione, G.L., Scaloni, F., Lo Sterzo, C., Di Matteo, A., Falini, B., Giardina, B., Brunori, M. J. Biol. Chem. (2010) [Pubmed]

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