Curli biogenesis: order out of disorder.
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.
Department of Molecular, Cellular and Developmental Biology, University of Michigan, 830 North University, Ann Arbor, MI 48109, USA.
Margery L
ML
Evans
Department of Molecular, Cellular and Developmental Biology, University of Michigan, 830 North University, Ann Arbor, MI 48109, USA. Electronic address: chapmanm@umich.edu.
Matthew R
MR
Chapman
D000682:Amyloid / Q000737:chemistry* / Q000378:metabolism; D058227:Amyloidogenic Proteins / Q000737:chemistry* / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D018441:Biofilms / Q000254:growth & development; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D006801:Humans; D017510:Protein Folding; D021381:Protein Transport
D000682:Amyloid; D058227:Amyloidogenic Proteins; D001426:Bacterial Proteins; C077481:Crl protein, Bacteria
Aggregate; Biofilm; Curli; Functional amyloid; Nucleation–precipitation; Type VIII secretion