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Functional amyloid in Pseudomonas
Author(s) -
Dueholm Morten S.,
Petersen Steen V.,
Sønderkær Mads,
Larsen Poul,
Christiansen Gunna,
Hein Kim L.,
Enghild Jan J.,
Nielsen Jeppe L.,
Nielsen Kåre L.,
Nielsen Per H.,
Otzen Daniel E.
Publication year - 2010
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2010.07269.x
Subject(s) - operon , biology , pseudomonas fluorescens , escherichia coli , amyloid (mycology) , asparagine , gene , conserved sequence , genetics , biofilm , biochemistry , microbiology and biotechnology , peptide sequence , bacteria , amino acid , botany
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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