Grant: Operating Grant

'Amyloids' are organized aggregations of proteins that are often associated with diseases like Alzheimer's, Parkinson's, and rheumatoid arthritis. It had long been thought that amyloid formation was the result of interactions between proteins that had folded incorrectly, and that these interactions were toxic to cells. New research, however, is showing that not all amyloids are toxic, and that there exist 'functional amyloids'. These functional protein aggregates appear to play important roles in a wide variety of biological systems, including skin pigmentation and microbial development/pathogenesis. Our work focuses upon on one class of functional amyloids found in the bacterium Streptomyces coelicolor. The 'chaplin' proteins of S. coelicolor interact to form amyloid fibres on the bacterial cell surface, and are critical for bacterial development. We are working to understand how chaplin interaction is controlled, as it is thought that precise regulation of expression and aggregation is a key factor in determining whether an amyloid is functional or toxic.