| Structural highlights
Function
FAPC_PSEFL The major functional amyloid subunit in this bacterium (PubMed:20572935, PubMed:23504942). Intrinsically disordered in its monomeric state (PubMed:37162737, PubMed:38349812). Upon overexpression of the endogenous six-gene locus (fapA-fapF) in situ, cells form large clumps during liquid growth, make large amounts of biofilm and produce amyloid fibrils (PubMed:23504942, PubMed:26500638). Expression of the 6 gene operon in E.coli strain BL21(DE3) induces flocculation and biofilm formation with copious extracellular fibrils (PubMed:20572935, PubMed:28811582).[1] [2] [3] [4] [5] [6]
References
- ↑ Dueholm MS, Petersen SV, Sønderkær M, Larsen P, Christiansen G, Hein KL, Enghild JJ, Nielsen JL, Nielsen KL, Nielsen PH, Otzen DE. Functional amyloid in Pseudomonas. Mol Microbiol. 2010 Aug;77(4):1009-20. PMID:20572935 doi:10.1111/j.1365-2958.2010.07269.x
- ↑ Dueholm MS, Søndergaard MT, Nilsson M, Christiansen G, Stensballe A, Overgaard MT, Givskov M, Tolker-Nielsen T, Otzen DE, Nielsen PH. Expression of Fap amyloids in Pseudomonas aeruginosa, P. fluorescens, and P. putida results in aggregation and increased biofilm formation. Microbiologyopen. 2013 Jun;2(3):365-82. PMID:23504942 doi:10.1002/mbo3.81
- ↑ Zeng G, Vad BS, Dueholm MS, Christiansen G, Nilsson M, Tolker-Nielsen T, Nielsen PH, Meyer RL, Otzen DE. Functional bacterial amyloid increases Pseudomonas biofilm hydrophobicity and stiffness. Front Microbiol. 2015 Oct 7;6:1099. PMID:26500638 doi:10.3389/fmicb.2015.01099
- ↑ Rouse SL, Hawthorne WJ, Berry JL, Chorev DS, Ionescu SA, Lambert S, Stylianou F, Ewert W, Mackie U, Morgan RML, Otzen D, Herbst FA, Nielsen PH, Dueholm M, Bayley H, Robinson CV, Hare S, Matthews S. A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis. Nat Commun. 2017 Aug 15;8(1):263. doi: 10.1038/s41467-017-00361-6. PMID:28811582 doi:https://dx.doi.org/10.1038/s41467-017-00361-6
- ↑ Byeon CH, Wang PC, Byeon IL, Akbey Ü. Solution-state NMR assignment and secondary structure propensity of the full length and minimalistic-truncated prefibrillar monomeric form of biofilm forming functional amyloid FapC from Pseudomonas aeruginosa. Biomol NMR Assign. 2023 Dec;17(2):159-165. PMID:37162737 doi:10.1007/s12104-023-10135-5
- ↑ Byeon CH, Hansen KH, Jeffrey J, Saricayir H, Andreasen M, Akbey Ü. Intrinsically disordered Pseudomonas chaperone FapA slows down the fibrillation of major biofilm-forming functional amyloid FapC. FEBS J. 2024 May;291(9):1925-1943. PMID:38349812 doi:10.1111/febs.17084
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