Abstract
The 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.
Original language | English (US) |
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Pages (from-to) | 57-60 |
Number of pages | 4 |
Journal | Prion |
Volume | 2 |
Issue number | 2 |
DOIs | |
State | Published - Apr 2008 |
Externally published | Yes |
ASJC Scopus subject areas
- Biochemistry
- Cellular and Molecular Neuroscience
- Cell Biology
- Infectious Diseases