title: Conformational transition of DNA bound to Hfq probed by infrared spectroscopy.
abstract: Hfq is a bacterial protein involved in RNA metabolism. Besides this, Hfq's role in DNA restructuring has also been suggested. Since this mechanism remains unclear, we examined the DNA conformation upon Hfq binding by combining vibrational spectroscopy and neutron scattering. Our analysis reveals that Hfq, which preferentially interacts with deoxyadenosine rich sequences, induces partial opening of dA-dT sequences accompanied by sugar repuckering of the dA strand and hence results in a heteronomous A/B duplex. Sugar repuckering is probably correlated with a global dehydration of the complex. By taking into account Hfq's preferential binding to A-tracts, which are commonly found in promoters, potential biological implications of Hfq binding to DNA are discussed.
authors.affiliation: UFR SMBH, Université Paris 13, Bobigny F-93017, France.
authors.forename: Frédéric
authors.initials: F
authors.lastname: Geinguenaud
authors.forename: Vania
authors.initials: V
authors.lastname: Calandrini
authors.forename: José
authors.initials: J
authors.lastname: Teixeira
authors.forename: Claudine
authors.initials: C
authors.lastname: Mayer
authors.forename: Jean
authors.initials: J
authors.lastname: Liquier
authors.forename: Christophe
authors.initials: C
authors.lastname: Lavelle
authors.forename: Véronique
authors.initials: V
authors.lastname: Arluison
mesh_terms: D004247:DNA / Q000737:chemistry*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D035001:Host Factor 1 Protein / Q000737:chemistry*; D033363:Neutron Diffraction; D009690:Nucleic Acid Conformation; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D017550:Spectroscopy, Fourier Transform Infrared
chemical_list: D029968:Escherichia coli Proteins; D035001:Host Factor 1 Protein; D004247:DNA