DNA structuration by a bacterial amyloid
Expected breakthroughs of the proposal consist in the investigation of a self-assembled amyloid nucleoprotein nanostructure. Small angle neutron scattering will be applied to follow the effect of an amyloid structure formed by Hfq, a key protein involved in the control of bacterial virulence, on DNA. Precisely, a peptide issued from Hfq results in a specific helicoidal fibrillar structure where DNA is a part of the complex. Nevertheless, the precise organization of the complex and whether DNA is located inside the fibre is not known. Solvent contrast matching will allow to match out the signal from Hfq peptide conserving however its influence on the DNA structure. In this way, only the structure of DNA under the influence of the amyloidogenic peptide will be seen. It should thus be possible to accurately determine the Hfq amyloid fibers shape and the conformation of the DNA inside the fiber. As Hfq is a virulence factor, the expected long-term benefits for this project will be opportunities for the development of new antibiotics.
The data is currently only available to download if you are a member of the proposal team.
The recommended format for citing this dataset in a research publication is in the following format:
Arluison; MARTEL Anne; MATSUO Tatsuhito; PETERS Judith; PREVOST Sylvain; QU Xiaoli and Frank Wien. (2021). DNA structuration by a bacterial amyloid. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-03-1038
This data is not yet public
This data is not yet public
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