Flagellin lysine methyltransferase FliB catalyzes a [4Fe-4S] mediated methyl transfer reaction.

The methyltransferase FliB posttranslationally modifies surface-exposed ɛ-N-lysine residues of flagellin, the protomer of the flagellar filament in Salmonella enterica (S. enterica). Flagellin methylation, reported originally in 1959, was recently shown to enhance host cell adhesion and invasion by...

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Autores principales:	Chu Wang, Christian Nehls, Dirk Baabe, Olaf Burghaus, Robert Hurwitz, Thomas Gutsmann, Martin Bröring, Michael Kolbe
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2021
Materias:	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/aa696146eae54b8994d1060a5f900c92
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spelling	oai:doaj.org-article:aa696146eae54b8994d1060a5f900c922021-12-02T19:59:52ZFlagellin lysine methyltransferase FliB catalyzes a [4Fe-4S] mediated methyl transfer reaction.1553-73661553-737410.1371/journal.ppat.1010052https://doaj.org/article/aa696146eae54b8994d1060a5f900c922021-11-01T00:00:00Zhttps://doi.org/10.1371/journal.ppat.1010052https://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374The methyltransferase FliB posttranslationally modifies surface-exposed ɛ-N-lysine residues of flagellin, the protomer of the flagellar filament in Salmonella enterica (S. enterica). Flagellin methylation, reported originally in 1959, was recently shown to enhance host cell adhesion and invasion by increasing the flagellar hydrophobicity. The role of FliB in this process, however, remained enigmatic. In this study, we investigated the properties and mechanisms of FliB from S. enterica in vivo and in vitro. We show that FliB is an S-adenosylmethionine (SAM) dependent methyltransferase, forming a membrane associated oligomer that modifies flagellin in the bacterial cytosol. 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 [4Fe-4S] cluster that is essential for the methyl transfer reaction and might mediate a radical mechanism. Our data indicate that the [4Fe-4S] cluster is coordinated by a cysteine rich motif in FliB that is highly conserved among multiple genera of the Enterobacteriaceae family.Chu WangChristian NehlsDirk BaabeOlaf BurghausRobert HurwitzThomas GutsmannMartin BröringMichael KolbePublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 17, Iss 11, p e1010052 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
spellingShingle	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5 Chu Wang Christian Nehls Dirk Baabe Olaf Burghaus Robert Hurwitz Thomas Gutsmann Martin Bröring Michael Kolbe Flagellin lysine methyltransferase FliB catalyzes a [4Fe-4S] mediated methyl transfer reaction.
description	The methyltransferase FliB posttranslationally modifies surface-exposed ɛ-N-lysine residues of flagellin, the protomer of the flagellar filament in Salmonella enterica (S. enterica). Flagellin methylation, reported originally in 1959, was recently shown to enhance host cell adhesion and invasion by increasing the flagellar hydrophobicity. The role of FliB in this process, however, remained enigmatic. In this study, we investigated the properties and mechanisms of FliB from S. enterica in vivo and in vitro. We show that FliB is an S-adenosylmethionine (SAM) dependent methyltransferase, forming a membrane associated oligomer that modifies flagellin in the bacterial cytosol. 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 [4Fe-4S] cluster that is essential for the methyl transfer reaction and might mediate a radical mechanism. Our data indicate that the [4Fe-4S] cluster is coordinated by a cysteine rich motif in FliB that is highly conserved among multiple genera of the Enterobacteriaceae family.
format	article
author	Chu Wang Christian Nehls Dirk Baabe Olaf Burghaus Robert Hurwitz Thomas Gutsmann Martin Bröring Michael Kolbe
author_facet	Chu Wang Christian Nehls Dirk Baabe Olaf Burghaus Robert Hurwitz Thomas Gutsmann Martin Bröring Michael Kolbe
author_sort	Chu Wang
title	Flagellin lysine methyltransferase FliB catalyzes a [4Fe-4S] mediated methyl transfer reaction.
title_short	Flagellin lysine methyltransferase FliB catalyzes a [4Fe-4S] mediated methyl transfer reaction.
title_full	Flagellin lysine methyltransferase FliB catalyzes a [4Fe-4S] mediated methyl transfer reaction.
title_fullStr	Flagellin lysine methyltransferase FliB catalyzes a [4Fe-4S] mediated methyl transfer reaction.
title_full_unstemmed	Flagellin lysine methyltransferase FliB catalyzes a [4Fe-4S] mediated methyl transfer reaction.
title_sort	flagellin lysine methyltransferase flib catalyzes a [4fe-4s] mediated methyl transfer reaction.
publisher	Public Library of Science (PLoS)
publishDate	2021
url	https://doaj.org/article/aa696146eae54b8994d1060a5f900c92
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Flagellin lysine methyltransferase FliB catalyzes a [4Fe-4S] mediated methyl transfer reaction.

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