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@ARTICLE{Geinguenaud:861352,
author = {Geinguenaud, Frédéric and Calandrini, Vania and Teixeira,
José and Mayer, Claudine and Liquier, Jean and Lavelle,
Christophe and Arluison, Véronique},
title = {{C}onformational transition of {DNA} bound to {H}fq probed
by infrared spectroscopy},
journal = {Physical chemistry, chemical physics},
volume = {13},
number = {3},
issn = {1463-9084},
address = {Cambridge},
publisher = {RSC Publ.66479},
reportid = {FZJ-2019-01834},
pages = {1222 - 1229},
year = {2011},
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.},
cin = {IAS-5 / INM-9},
ddc = {540},
cid = {I:(DE-Juel1)IAS-5-20120330 / I:(DE-Juel1)INM-9-20140121},
pnm = {899 - ohne Topic (POF3-899)},
pid = {G:(DE-HGF)POF3-899},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:21082116},
UT = {WOS:000285750100048},
doi = {10.1039/C0CP01084G},
url = {https://juser.fz-juelich.de/record/861352},
}