Please use this identifier to cite or link to this item: https://doi.org/10.1093/nar/gkx431
Title: Compaction and condensation of DNA mediated by the C-terminal domain of Hfq
Authors: Malabirade, Antoine
Jiang, Kai 
Kubiak, Krzysztof
Diaz-Mendoza, Alvaro
Liu, Fan 
van Kan, Jeroen A 
Berret, Jean-Francois
Arluison, Veronique
van der Maarel, Johan RC 
Keywords: Science & Technology
Life Sciences & Biomedicine
Biochemistry & Molecular Biology
ISOTHERMAL TITRATION CALORIMETRY
BINDING-PROTEIN HFQ
ESCHERICHIA-COLI
SINGLE DNA
H-NS
BENDING RIGIDITY
RNA
MOLECULES
BACTERIAL
GENE
Issue Date: 7-Jul-2017
Publisher: OXFORD UNIV PRESS
Citation: Malabirade, Antoine, Jiang, Kai, Kubiak, Krzysztof, Diaz-Mendoza, Alvaro, Liu, Fan, van Kan, Jeroen A, Berret, Jean-Francois, Arluison, Veronique, van der Maarel, Johan RC (2017-07-07). Compaction and condensation of DNA mediated by the C-terminal domain of Hfq. NUCLEIC ACIDS RESEARCH 45 (12) : 7299-7308. ScholarBank@NUS Repository. https://doi.org/10.1093/nar/gkx431
Abstract: Hfq is a bacterial protein that is involved in several aspects of nucleic acids metabolism. It has been described as one of the nucleoid associated proteins shaping the bacterial chromosome, although it is better known to influence translation and turnover of cellular RNAs. Here, we explore the role of Escherichia coli Hfq's C-terminal domain in the compaction of double stranded DNA. Various experimental methodologies, including fluorescence microscopy imaging of single DNA molecules confined inside nanofluidic channels, atomic force microscopy, isothermal titration microcalorimetry and electrophoretic mobility assays have been used to follow the assembly of the C-terminal and N-terminal regions of Hfq on DNA. Results highlight the role of Hfq's C-terminal arms in DNA binding, change in mechanical properties of the double helix and compaction of DNA into a condensed form. The propensity for bridging and compaction of DNA by the C-terminal domain might be related to aggregation of bound protein and may have implications for protein binding related gene regulation.
Source Title: NUCLEIC ACIDS RESEARCH
URI: https://scholarbank.nus.edu.sg/handle/10635/215520
ISSN: 03051048
13624962
DOI: 10.1093/nar/gkx431
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