Journal
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
Volume 1843, Issue 8, Pages 1551-1558Publisher
ELSEVIER
DOI: 10.1016/j.bbamcr.2013.09.010
Keywords
Curli; Functional amyloid; Aggregate; Biofilm; Nucleation-precipitation; Type VIII secretion
Categories
Funding
- National Institutes of Health [AI073847]
- University of Michigan Cellular Biotechnology Training Program [NIH NRSA T32 GM008353]
- University of Michigan Rackham Graduate School Predoctoral Fellowship
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Many bacteria assemble extracellular amyloid fibers on their cell surface. Secretion of proteins across membranes and the assembly of complex macromolecular structures must be highly coordinated to avoid the accumulation of potentially toxic intracellular protein aggregates. Extracellular amyloid fiber assembly poses an even greater threat to cellular health due to the highly aggregative nature of amyloids and the inherent toxicity of amyloid assembly intermediates. Therefore, temporal and spatial control of amyloid protein secretion is paramount. The biogenesis and assembly of the extracellular bacterial amyloid curli is an ideal system for studying how bacteria cope with the many challenges of controlled and ordered amyloid assembly. Here, we review the recent progress in the curli field that has made curli biogenesis one of the best-understood functional amyloid assembly pathways. This article is part of a Special Issue entitled: Protein trafficking and secretion in bacteria. Guest Editors: Anastassios Economou and Ross Dalbey. (C) 2013 Elsevier B.V. All rights reserved.
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