Poursuite possible en thèse
Nucleoid associated proteins NAPs are regulators of bacterial gene expression. As architectural proteins, they change the mechanical properties of DNA. We aim to understand how bacterial amyloid self-assemblies can influence DNA compaction.
Sujet détaillé/Full description
Hfq is a bacterial pleiotropic regulator that mediates several aspects of nucleic acids metabolism. The protein notably influences translation and turnover of cellular RNAs. Although most previous contributions concentrated on Hfq’s interaction with RNA, its association to DNA has also been observed. With this project, we want to focus on DNA-compacting properties of Hfq. Various experimental technologies, including fluorescence microscopy imaging, atomic force microscopy, small angle neutron scattering and IR Nanospectroscopy will be used to follow the assembly of Hfq on DNA. In particular, we would like to evaluate how Hfq amyloid region helps to form a nucleoprotein complex in order to compact DNA into a condensed form and how it changes the mechanical properties of the double helix. The conclusions will be paramount to understand the implications of this protein in gene regulation.
K. Jiang, C. Zhang, D. Guttula, F. Liu, J. A. van Kan, C. Lavelle, K. Kubiak, A. Malabirade, A. Lapp, V. Arluison, and J. R. C. van der Maarel, Effects of Hfq on the conformation and compaction of DNA, Nucleic Acids Research 43, 4332-4341 (2015).
J. R. C. van der Maarel, D. Guttula, V. Arluison, S. U. Egelhaaf, I. Grillo, and V. T. Forsyth. Structure of the H-NS-DNA nucleoprotein complex, Soft Matter 12, 3636-4220 (2016)
Molecular Biology, Biochemistry
Molecular Biology, Biophysics, Biochemistry