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Recognition of intermolecular G‐quadruplexes by full length nucleophosmin. Effect of a leukaemia‐associated mutation
Author(s) -
Bañuelos Sonia,
Lectez Benoît,
Taneva Stefka G.,
Ormaza Georgina,
Alonso-Mariño Marián,
Calle Xabier,
Urbaneja María A.
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.05.055
Subject(s) - nucleophosmin , ribosome biogenesis , nucleolus , nucleic acid , mutation , rna binding protein , npm1 , dna , biology , chemistry , gene , microbiology and biotechnology , ribosome , rna , cytoplasm , genetics , chromosome , karyotype
Nucleophosmin (NPM) is a nucleolar protein involved in ribosome biogenesis. NPM1 gene is frequently mutated in acute myeloid leukaemia (AML), correlating with aberrant cytoplasmic localization of the protein. NPM attachment to the nucleolus in physiological conditions probably depends on binding to nucleic acids, and this recognition could be altered in AML. NPM associates to guanine‐rich DNA sequences, able to fold as “G‐quadruplexes”. We have analyzed the interaction of pentameric, full length NPM with G‐rich oligonucleotides, finding that the protein binds preferentially high‐order G‐quadruplexes. AML‐associated mutation significantly hampers DNA binding, pointing to a possible mechanism contributing to pathological mislocalization of NPM.