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Discovery of a proteolytic flagellin family in diverse bacterial phyla that assembles enzymatically active flagella
Uppsala universitet, Teknisk-naturvetenskapliga vetenskapsområdet, Biologiska sektionen, Institutionen för cell- och molekylärbiologi, Struktur- och molekylärbiologi. Univ British Columbia, Fac Dent, Dept Oral Biol & Med Sci, Inst Life Sci, 2350 Hlth Sci Mall, Vancouver, BC V6T 1Z3, Canada.
Univ Waterloo, Dept Biol, 200 Univ Ave West, Waterloo, ON N2L 3G1, Canada..
Univ Waterloo, Dept Biol, 200 Univ Ave West, Waterloo, ON N2L 3G1, Canada..
Univ British Columbia, Fac Dent, Dept Oral Biol & Med Sci, Inst Life Sci, 2350 Hlth Sci Mall, Vancouver, BC V6T 1Z3, Canada..
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2017 (engelsk)Inngår i: Nature Communications, ISSN 2041-1723, E-ISSN 2041-1723, Vol. 8, 521Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

Bacterial flagella are cell locomotion and occasional adhesion organelles composed primarily of the polymeric protein flagellin, but to date have not been associated with any enzymatic function. Here, we report the bioinformatics-driven discovery of a class of enzymatic flagellins that assemble to form proteolytically active flagella. Originating by a metallopeptidase insertion into the central flagellin hypervariable region, this flagellin family has expanded to at least 74 bacterial species. In the pathogen, Clostridium haemolyticum, metallopeptidase-containing flagellin (which we termed flagellinolysin) is the second most abundant protein in the flagella and is localized to the extracellular flagellar surface. Purified flagellar filaments and recombinant flagellin exhibit proteolytic activity, cleaving nearly 1000 different peptides. With similar to 20,000 flagellin copies per similar to 10-mu m flagella this assembles the largest proteolytic complex known. Flagellum-mediated extracellular proteolysis expands our understanding of the functional plasticity of bacterial flagella, revealing this family as enzymatic biopolymers that mediate interactions with diverse peptide substrates.

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2017. Vol. 8, 521
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URN: urn:nbn:se:uu:diva-335193DOI: 10.1038/s41467-017-00599-0ISI: 000410452800003PubMedID: 28900095OAI: oai:DiVA.org:uu-335193DiVA: diva2:1163688
Tilgjengelig fra: 2017-12-07 Laget: 2017-12-07 Sist oppdatert: 2017-12-07bibliografisk kontrollert

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