| Protein misfolding and aggregation into amyloid structures are associated with dozens of human diseases. Recent studies have provided compelling evidence for the formation of aggregates conformationally related to those underlying such disorders in the bacterial cytosol. Thus, amyloid-like aggregation seems to be an omnipresent process in both eukaryotic and prokaryotic organisms. The ease with which bacteria can be genetically and biochemically manipulated suggest that prokaryotic cells might become useful systems for studying how and why proteins aggregate inside the cell and could provide a tractable environment to rationally model such phenomenon. Toward this aim our lab is trying to characterize the structural and sequential polypeptide traits that influence protein deposition in bacterial backgrounds. |
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