Journal Article

FZJ-2019-01834

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Conformational transition of DNA bound to Hfq probed by infrared spectroscopy

Geinguenaud, F. ; Calandrini, V.FZJ* ; Teixeira, J. ; Mayer, C. ; Liquier, J. ; Lavelle, C. ; Arluison, V. (Corresponding author)

2011
RSC Publ.66479 Cambridge

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Please use a persistent id in citations: doi:10.1039/C0CP01084G

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.

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Contributing Institute(s):

1. Computational Biomedicine (IAS-5)
2. Computational Biomedicine (INM-9)

Research Program(s):

1. 899 - ohne Topic (POF3-899) (POF3-899)

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Database coverage:
; Allianz-Lizenz / DFG ; Clarivate Analytics Master Journal List ; Current Contents - Physical, Chemical and Earth Sciences ; IF < 5 ; JCR ; NCBI Molecular Biology Database ; National-Konsortium ; Nationallizenz ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Web of Science Core Collection

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