The DOI matches its Crossref record; 55 of the 55 references it cites were found in a registry or an index.
Functional amyloid in Pseudomonas
Abstract
Summary: Amyloids are highly abundant in many microbial biofilms and may play an important role in their architecture. Nevertheless, little is known of the amyloid proteins. We report the discovery of a novel functional amyloid expressed by a Pseudomonas strain of the P. fluorescens group. The amyloid protein was purified and the amyloid‐like structure verified. Partial sequencing by MS/MS combined with full genomic sequencing of the Pseudomonas strain identified the gene coding for the major subunit of the amyloid fibril, termed fapC. FapC contains a thrice repeated motif that differs from those previously found in curli fimbrins and prion proteins. The lack of aromatic residues in the repeat shows that aromatic side chains are not needed for efficient amyloid formation. In contrast, glutamine and asparagine residues seem to play a major role in amyloid formation as these are highly conserved in curli, prion proteins and FapC. fapC is conserved in many Pseudomonas strains including the opportunistic pathogen P. aeruginosa and is situated in a conserved operon containing six genes, of which one encodes a fapC homologue. Heterologous expression of the fapA–F operon in Escherichia coli BL21(DE3) resulted in a highly aggregative phenotype, showing that the operon is involved in biofilm formation.
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Cites
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Cited by
Hobley, L., Harkins, C., MacPhee, C. E., & Stanley-Wall, N. R. (2015) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuv015 · Cited by 581
Diversity, biogenesis and function of microbial amyloids
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Besingi, R. N., Wenderska, I. B., Senadheera, D. B., Cvitkovitch, D. G., Long, J. R., Wen, Z. T., & Brady, L. J. (2017) · Microbiology · doi:10.1099/mic.0.000443 · Cited by 99
Donor-strand exchange drives assembly of the TasA scaffold in Bacillus subtilis biofilms
(2022) · doi:10.1038/s41467-022-34700-z · Cited by 91
Microbial functional amyloids serve diverse purposes for structure, adhesion and defence
Shanmugam, N., Baker, M. O. D. G., Ball, S. R., Steain, M., Pham, C. L. L., & Sunde, M. (2019) · Biophysical Reviews · doi:10.1007/s12551-019-00526-1 · Cited by 75
Metadata
- Authors
- Dueholm, M. S., Petersen, S. V., Sønderkær, M., Larsen, P., Christiansen, G., Hein, K. L., Enghild, J. J., Nielsen, J. L., Nielsen, K. L., Nielsen, P. H., & Otzen, D. E.
- Venue
- Molecular Microbiology
- Publisher
- Wiley
- Published
- 2010-08
- Volume
- 77
- Issue
- 4
- Pages
- 1009-1020
- ISSN
- 0950-382X (ISSN-L)
- 1365-2958
- OpenAlex
- W2104700141
- Cited by
- 300
- References
- 55
- FWCI
- 5.32
- Type
- journal article
- Language
- en
- Open access
- closed
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- Dueholm, M. S., Petersen, S. V., Sønderkær, M., Larsen, P., Christiansen, G., Hein, K. L., Enghild, J. J., Nielsen, J. L., Nielsen, K. L., Nielsen, P. H., & Otzen, D. E. (2010). Functional amyloid in Pseudomonas. Molecular Microbiology. https://doi.org/10.1111/j.1365-2958.2010.07269.x
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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