12/11/2023 0 Comments Spectroscopie rmn terminale sSimeon Minic, Burkhard Annighöfer, Milos Milcic, François Maignen, Annie Brûlet, Sophie CombetĪpomyoglobin (apoMb), a model protein in biochemistry, exhibits a strong propensity to bind various ligands, which makes it a good candidate as a carrier of bioactive hydrophobic drugs. Taken together, our findings reveal a new role for this protein in nucleoid remodeling in vivo, that may serve in response to stress conditions and in adapting to changing environments. Our results indicate that Hfq could regulate nucleoid compaction directly via its interaction with DNA, but also at the post-transcriptional level via its interaction with RNAs. More specifically, Hfq influences nucleoid density especially during the stationary growth phase when it is more abundant. Here, using cryo soft X-ray tomography imaging of native unlabeled cells and using a semi-automatic analysis and segmentation procedure, we show that Hfq significantly remodels the Escherichia coli nucleoid. Recently, it has been shown in vitro that Hfq forms amyloid-like structures through its C-terminal region, hence belonging to the bridging family of NAPs. Although Hfq presence in the nucleoid has been demonstrated for years, its precise role is still unclear. Indeed, Hfq is best known to mediate post-transcriptional regulation by using small noncoding RNA (sRNA). Among these NAPs, Hfq is one of the most intriguing as it plays both direct and indirect roles on DNA structure. The bacterial chromosomic DNA is packed within a membrane-less structure, the nucleoid, due to the association of DNA with proteins called Nucleoid Associated Proteins (NAPs). Antoine Cossa, Sylvain Trépout, Frank Wien, Johannes Groen, Etienne Le Brun, Florian Turbant, Laetitia Besse, Eva Pereiro, Véronique Arluison
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