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lüll Curli provide the template for understanding controlled amyloid propagation Wang X; Chapman MRPrion 2008[Apr]; 2 (2): 57-60The uncontrolled formation of amyloid fibers is the hallmark of more than twenty human diseases. In contrast to disease-associated amyloids, which are the products of protein misfolding, E. coli assembles functional amyloid fibers called curli on its surface using an elegant biogenesis machine. Composed of a major subunit, CsgA, and a minor subunit, CsgB, curli play important roles in host cell adhesion, long-term survival and other bacterial community behaviors. Assembly of curli fibers is a template-directed conversion process where membrane-tethered CsgB initiates CsgA polymerization. The CsgA amyloid core is composed of five imperfect repeating units. In a series of in vivo and in vitro experiments, we determined the sequence and structural determinants that guide the initiation and propagation of CsgA polymers. The CsgA N- and C-terminal repeating units govern its polymerization and responsiveness to CsgB. Specifically, conserved glutamine and asparagine residues present in the CsgA N- and C-terminal repeating units are required for CsgB-mediated nucleation and efficient self-assembly.|*Protein Folding[MESH]|Amyloid/genetics/*metabolism[MESH]|Animals[MESH]|Bacterial Adhesion/physiology[MESH]|Bacterial Proteins/genetics/*metabolism[MESH]|Escherichia coli Proteins/genetics/*metabolism[MESH]|Escherichia coli/genetics/*metabolism[MESH]|Humans[MESH]|Protein Structure, Quaternary/physiology[MESH]|Protein Structure, Tertiary/physiology[MESH] |