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© Institut Pasteur
Cells infected for 24 hrs with C. Trachomatis. The cell nuclei are labelled in blue, the bacteria appear yellow, within the inclusion lumen. A bacterial protein secreted out the inclusion into the host cytoplasm id labelled in red.
Publication : Physical chemistry chemical physics : PCCP

Conformational transition of DNA bound to Hfq probed by infrared spectroscopy

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Physical chemistry chemical physics : PCCP - 16 Nov 2010

Geinguenaud F, Calandrini V, Teixeira J, Mayer C, Liquier J, Lavelle C, Arluison V

Link to Pubmed [PMID] – 21082116

Phys Chem Chem Phys 2011 Jan;13(3):1222-9

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.

http://www.ncbi.nlm.nih.gov/pubmed/21082116