Journal of Molecular Biology
Volume 430, Issue 20, 12 October 2018, Pages 3685-3695
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Review
Ecology and Biogenesis of Functional Amyloids in Pseudomonas

https://doi.org/10.1016/j.jmb.2018.05.004Get rights and content
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Highlights

  • New evolutionary analysis identifies the Fap system in 25 additional genera.

  • The list of known Fap protein homologs is greatly expanded for Pseudomonas.

  • Recent structural and mechanistic insight into the Fap amyloid secretion system

  • Structural model for FapC in the amyloid state derived from sequence covariance

Abstract

Functional amyloids can be found in the extracellular matrix produced by many bacteria during biofilm growth. They mediate the initial attachment of bacteria to surfaces and provide stability and functionality to mature biofilms. Efficient amyloid biogenesis requires a highly coordinated system of amyloid subunits, molecular chaperones and transport systems. The functional amyloid of Pseudomonas (Fap) represents such a system. Here, we review the phylogenetic diversification of the Fap system, its potential ecological role and the dedicated machinery required for Fap biogenesis, with a particular focus on the amyloid exporter FapF, the structure of which has been recently resolved. We also present a sequence covariance-based in silico model of the FapC fiber-forming subunit. Finally, we highlight key questions that remain unanswered and we believe deserve further attention by the scientific community.

Abbreviations

Fap
functional amyloid in Pseudomonas
EPS
extracellular polymeric substances
PGPR
plant growth promoting rhizobacteria
QS
quorum sensing
PQS
2-heptyl-3-hydroxy- 4(1H)-quinolone
3-oxo-C12-HSL
N-(3-oxododecanoyl)-l-homoserine lactone

Keywords

Fap
amyloid
diversity
structure
sequence covariance analysis

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