Blog
About

7
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: not found

      Curli provide the template for understanding controlled amyloid propagation.

      Prion

      physiology, Protein Structure, Tertiary, Protein Structure, Quaternary, Protein Folding, Humans, metabolism, genetics, Escherichia coli Proteins, Escherichia coli, Bacterial Proteins, Bacterial Adhesion, Animals, Amyloid

      Read this article at

      ScienceOpenPMC
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          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.

          Related collections

          Author and article information

          Journal
          2634518
          19098444

          Comments

          Comment on this article