IBR   13079
INSTITUTO DE BIOLOGIA MOLECULAR Y CELULAR DE ROSARIO
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
The nucleic acid chaperone protein CNBP binds G-rich nucleic acids that may form G-quartets.
Autor/es:
NASIF, S.; CALCATERRA, N.B.; ARMAS, P.
Lugar:
Mar del Plata, Buenos Aires, Argentina.
Reunión:
Congreso; XLIII Annual Meeting of the Argentine Society for Biochemestry and Molecular Biology Research.; 2007
Resumen:
Cellular nucleic acid binding protein (CNBP) is a single-stranded nucleic acid binding protein made of seven CCHC Zn knuckles and a RGG box. CNBP is conserved among vertebrates and plays broad-spectrum functions. It is required for rostral head development during vertebrate embryogenesis and acts as a nucleic acid chaperone, remodeling and stabilizing the secondary structure of its targets. Neither the consensus sequence of these targets nor their structural features were still elucidated. Our main goal was to gain insights into the identification of common features among the preferred CNBP molecular targets. We studied CNBP binding to single-stranded nucleic acid probes representing its main reported putative targets. Analysis of mutant and artificial probes shows that the preferred CNBP targets contain unpaired guanosine-rich stretches. Some of these probes contain the consensus sequence for the formation of stable G-quartet structures. Besides, experimental data from a “Systematic Evolution of Ligands by Exponential Enrichment” (SELEX) suggest that CNBP preferred nucleic acid targets may contain G-quartets consensus. Therefore, these results begin to dissect how CNBP performs its essential biological function: recognizing and probably acting as a nucleic acid chaperone on G-quartets structures, which have been described as pivotal elements for gene expression regulation.