ArticleProtein science : a publication of the Protein Society2019
Imperfect repeats in the functional amyloid protein FapC reduce the tendency to fragment during fibrillation.
Article in Protein science : a publication of the Protein Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 48 citations in OpenAlex.
- The Importance of Being Imperfect: Structure and Function of Bacterial Amyloid.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
- Structural basis ofScience advances · 2025Article
- Natural Design of a Stabilized Cross-β Fold: Structure of the FuA FapC from Pseudomonas Sp. UK4 Reveals a Critical Role for Stacking of Imperfect Repeats.Advanced materials (Deerfield Beach, Fla.) · 2025Article
- Capturing the micro-communities: Insights into biogenesis and architecture of bacterial biofilms.BBA advances · 2025Article
- Amyloid formation and depolymerization of tumor suppressor p16Nature communications · 2024Article
- In vitro and in silico evaluation of the serrapeptase effect on biofilm and amyloids of Pseudomonas aeruginosa.Applied microbiology and biotechnology · 2023Article
- Alzheimer's Progenitor Amyloid-β Targets and Dissolves Microbial Amyloids and Impairs Biofilm Function.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Molecular characterization of the N-terminal half of TasA during amyloid-like assembly and its contribution to Bacillus subtilis biofilm formation.NPJ biofilms and microbiomes · 2023Article
- Cell specialization in cyanobacterial biofilm development revealed by expression of a cell-surface and extracellular matrix protein.NPJ biofilms and microbiomes · 2023Article
- Uncovering the universality of self-replication in protein aggregation and its link to disease.Science advances · 2022Article
- Functional Bacterial Amyloids: Understanding Fibrillation, Regulating Biofilm Fibril Formation and Organizing Surface Assemblies.Molecules (Basel, Switzerland) · 2022Review
- Functional amyloids from bacterial biofilms - structural properties and interaction partners.Chemical science · 2022Review
- Co-aggregation and secondary nucleation in the life cycle of human prolactin/galanin functional amyloids.eLife · 2022Article
- Induction, inhibition, and incorporation: Different roles for anionic and zwitterionic lysolipids in the fibrillation of the functional amyloid FapC.The Journal of biological chemistry · 2022Article
- Chaperones mainly suppress primary nucleation during formation of functional amyloid required for bacterial biofilm formation.Chemical science · 2022Article
- Interaction of membrane vesicles with theBBA advances · 2022Article
- Nanotargeting of Resistant Infections with a Special Emphasis on the Biofilm Landscape.Bioconjugate chemistry · 2021Review
- Article
- Quantitating denaturation by formic acid: imperfect repeats are essential to the stability of the functional amyloid protein FapC.The Journal of biological chemistry · 2020Article
- Accelerated Amyloid Beta Pathogenesis by Bacterial Amyloid FapC.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2020Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Functional amyloid (FA) is widespread in bacteria and serves multiple purposes such as strengthening of biofilm and contact with eukaryotic hosts. Unlike pathological amyloid, FA has been subjected to evolutionary optimization which is likely to be reflected in the aggregation mechanism. FA from different bacteria, including Escherichia coli (CsgA) and Pseudomonas (FapC), contains a number of imperfect repeats which may be key to efficient aggregation. Here we report on the aggregative behavior of FapC constructs which represent all single, double, and triple deletions of the protein's three imperfect repeats. Analysis of the fibrillation kinetics by the program Amylofit reveals that the removal of these repeats increases the tendency of the growing fibrils to fragment and also generally increases aggregation half-times. Remarkably, even the mutant lacking all three repeats was able to fibrillate, although fibrillation was much more irregular and led to significantly altered and destabilized fibrils. We conclude that imperfect repeats can promote fibrillation efficiency thanks to their modular design, though the context of the imperfect repeats also plays a significant role.
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