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Bactéries pathogènes et phosphorylation des protéines (C. Grangeasse)

Since a decade, bacterial genomic has revealed the widespread presence of atypical tyrosine-kinases (BYK) and eukaryotic-like serine/threonine-kinases (STKP). These enzymes have been shown to participate in the regulation of some important cellular processes. However, their mode of action is still elusive and underlying regulatory mechanisms remain largely unknown. In addition, recent high-throughput and site-specific phosphoproteomic studies lead to the publication of long lists of bacterial phosphoproteins, suggesting that cellular functions of BYKs and STKPs could be far more complex than predicted. Studying BYKs and STKPs represents therefore a promising approach to decipher the inner workings of the bacterial cell.

Our research projects focus on the structural and functional characterization of BYKs and STKPs. The rationale behind our projects is to decipher phosphorylation networks in which BYKs and STKPs partake in the bacterial cell, to integrate all components into signaling pathways and understand how BYKs- and STKPs-mediated protein phosphorylation governs bacterial physiology.

Our project should also open new avenues towards specific inhibition of STKPs and BYKs and thus pave the way towards new antibacterial compounds to combat bacterial infectious diseases.

Our analytical strategies strongly rely on specific competencies and we use the synergy created between our team and our collaborators to apply molecular biology, bacterial genetics, biochemistry, microscopy and structural biology approaches. The main bacterial model used for our studies is the gram-positive bacterium Streptococcus pneumoniae

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