Discovery of a proteolytic flagellin family in diverse bacterial phyla that assembles enzymatically active flagella
Ulrich Eckhard, Hina Bandukwala, Michael J. Mansfield, Giada Marino, Jiujun Cheng, Iain Wallace, Todd Holyoak, Trevor C. Charles, John Austin, Christopher M. Overall & Andrew C. Doxey
LSI researchers proudly continue to produce leading edge life sciences research. The latest example is a ground-breaking discovery by the Overall Lab in collaboration with Andrew.C. Doxey’s Lab at the University of Waterloo, published in Nature on September 12th. This paper presents the first ever report of enzymatic activity in bacterial flagella. 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. The authors report the bioinformatics-driven discovery of a class of enzymatic flagellins that assemble to form proteolytically active flagella in at least 74 bacterial species. Purified flagellar filaments and recombinant flagellin from Clostridium haemolyticum exhibit extracellular proteolytic activity, cleaving nearly 1000 different peptides. The findings in this paper reveal this proteolytic flagellin family as enzymatic biopolymers that mediate interactions with diverse peptide substrates.
(The above description is based on the Abstract published in Nature)
— UBC Life Sciences (@ubclifesciences) September 13, 2017