Document Detail


Recognition of intermolecular G-quadruplexes by full length nucleophosmin. Effect of a leukaemia-associated mutation.
MedLine Citation:
PMID:  23742937     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Nucleophosmin (NPM) is a nucleolar protein involved in ribosome biogenesis. NPM 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.
Authors:
Sonia Bañuelos; Benoît Lectez; Stefka G Taneva; Georgina Ormaza; Marián Alonso-Mariño; Xabier Calle; María A Urbaneja
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-6-3
Journal Detail:
Title:  FEBS letters     Volume:  -     ISSN:  1873-3468     ISO Abbreviation:  FEBS Lett.     Publication Date:  2013 Jun 
Date Detail:
Created Date:  2013-6-7     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0155157     Medline TA:  FEBS Lett     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2013. Published by Elsevier B.V.
Affiliation:
Biophysics Unit (CSIC/UPV-EHU), Department of Biochemistry and Molecular Biology, University of Basque Country (UPV-EHU), POB 644, 48080 Bilbao, Spain. Electronic address: sonia.banuelos@ehu.es.
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