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ProteinLocalization Report Summary

Project ID: 310987
Funded under: FP7-IDEAS-ERC
Country: Portugal

Final Report Summary - PROTEINLOCALIZATION (Finding New Mechanisms for Protein Localization in Bacteria)

Bacterial cells are highly organized, with many proteins having to localise to the right place, at the right time, to correctly perform their function. With this project we wanted to uncover mechanisms of localization of bacterial proteins essential for cell division and for the synthesis of the cell surface. If these proteins are not correctly localised, bacteria may become unable to proliferate or to evade the host immune system, which recognizes conserved structures at the bacterial surface.
Using the gram-positive bacterial pathogen Staphylococcus aureus as a model organism, we have determined how various proteins are recruited to the divisome, the machinery that promotes cell division. Of particular interest were proteins involved in the synthesis of peptidoglycan, the main component of the bacterial surface. Specifically, we found that recruitment of the flippase of the peptidoglycan precursor to the divisome initiated massive peptidoglycan synthesis at that place, which then provided the required force for cell division to proceed.
Looking at localization of proteins in bacterial cells allowed us not only to understand fundamental biological processes, but also to better understand the mode of action of new antimicrobial compounds. This is because inhibition of an essential cellular process often causes delocalization of related proteins. Therefore we made use of staphylococcal strains expressing fluorescent fusions to proteins that catalyse essential processes to understand how antibiotics affect cellular organization.

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