Protein methylation plays a key role in physiological function and signaling pathway modulation. CN and TG (consumables) were supported by the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) under Germany’s Excellence Strategy-EXC 2167-390884018.” The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.Ĭompeting interests: The authors have declared that no competing interests exist. CW and MK were funded (consumables) by the Helmholtz Association funding agency IVF (Initiative and Networking Fund, ). This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.ĭata Availability: All relevant data are within the manuscript and its Supporting Information files.įunding: MK received financial support by the European Research Council under the European Community’s Seventh Framework Program (FP7/2007-2013, grant no. Received: AugAccepted: OctoPublished: November 17, 2021Ĭopyright: © 2021 Wang et al.
Baumler, University of California Davis School of Medicine, UNITED STATES (2021) Flagellin lysine methyltransferase FliB catalyzes a mediated methyl transfer reaction. Our work sets a stage for understanding the roles of oxygen sensitive iron-sulfur cluster in flagellar modification and entero-bacterial pathogenesis.Ĭitation: Wang C, Nehls C, Baabe D, Burghaus O, Hurwitz R, Gutsmann T, et al. We further found that FliB modifies flagellar subunits using an iron-sulfur cluster dependent mechanism and requires a reducing environment. The FliB methyltransferase coordinates a cluster at its active site by several cysteine residues that were highly conserved in many entero-pathogens. We show that FliB forms oligomers that localize in close proximity to the bacterial cell membrane. In this study, we isolated and characterized FliB of S. However, little is known about the properties of the methylase FliB, that catalyzes flagellar methylation. In Salmonella, the surface of the flagellar filaments is heavily modified by methylation on their lysine residues, contributing to efficient gut colonization and successful invasion of the host. The bacterial flagella are tail-like appendages that play important roles in motility and host cell infection. Our data indicate that the cluster is coordinated by a cysteine rich motif in FliB that is highly conserved among multiple genera of the Enterobacteriaceae family. Using X-band electron paramagnetic resonance (EPR) spectroscopy, zero-field 57Fe Mössbauer spectroscopy, methylation assays and chromatography coupled mass spectrometry (MS) analysis, we further found that FliB contains an oxygen sensitive cluster that is essential for the methyl transfer reaction and might mediate a radical mechanism. We show that FliB is an S-adenosylmethionine (SAM) dependent methyltransferase, forming a membrane associated oligomer that modifies flagellin in the bacterial cytosol. In this study, we investigated the properties and mechanisms of FliB from S. The role of FliB in this process, however, remained enigmatic. Flagellin methylation, reported originally in 1959, was recently shown to enhance host cell adhesion and invasion by increasing the flagellar hydrophobicity.
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Links in the actual PDF manual do work.The methyltransferase FliB posttranslationally modifies surface-exposed ɛ-N-lysine residues of flagellin, the protomer of the flagellar filament in Salmonella enterica (S. (Links between the following PDF files may not work depending on your operating system, browser, and PDF reader software. You can also view the Igor Pro manual via the web using the links on this page.
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