NDLI: Molecular Basis of S-layer Glycoprotein Glycan Biosynthesis in Geobacillus $stearothermophilus^{*S⃞}$

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Molecular Basis of S-layer Glycoprotein Glycan Biosynthesis in Geobacillus $stearothermophilus^{*S⃞}$

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Hofinger, Andreas Messner, Paul Zarschler, Kristof Schäffer, Christina Werz, Daniel B. Novotny, René Seeberger, Peter H. Steiner, Kerstin Kosma, Paul
Description	Author Affiliation: Steiner K ( Center for NanoBiotechnology, University of Natural Resources and Applied Life Sciences, Vienna, Austria.)
Abstract	The Gram-positive bacterium Geobacillus stearothermophilus NRS 2004/3a possesses a cell wall containing an oblique surface layer (S-layer) composed of glycoprotein subunits. O-Glycans with the structure $[→2)-α-l-Rhap-(1→3)-β-l-Rhap-(1→2)-α-l-Rhap-(1→]_{n}$ $_{=$ 13-18, a2-O-methyl group capping the terminal repeating unit at the nonreducing end and a $→2)-α-l-Rhap-[(1→3)-α-l-Rhap]_{n}$ $_{=$ 1-2(1→3)- adaptor are linked via a β-d-Galp residue to distinct sites of the S-layer protein SgsE. S-layer glycan biosynthesis is encoded by a polycistronic slg (surface layer glycosylation) gene cluster. Four assigned glycosyltransferases named WsaC-WsaF, were investigated by a combined biochemical and NMR approach, starting from synthetic octyl-linked saccharide precursors. We demonstrate that three of the enzymes are rhamnosyltransferases that are responsible for the transfer of l-rhamnose from a dTDP-β-l-Rha precursor to the nascent S-layer glycan, catalyzing the formation of the α1,3- (WsaC and WsaD) and β1,2-linkages (WsaF) present in the adaptor saccharide and in the repeating units of the mature S-layer glycan, respectively. These enzymes work in concert with a multifunctional methylrhamnosyltransferase (WsaE). The N-terminal portion of WsaE is responsible for the S-adenosylmethionine-dependent methylation reaction of the terminal α1,3-linked l-rhamnose residue, and the central and C-terminal portions are involved in the transfer of l-rhamnose from dTDP-β-l-rhamnose to the adaptor saccharide to form the α1,2- and α1,3-linkages during S-layer glycan chain elongation, with the methylation and the glycosylation reactions occurring independently. Characterization of these enzymes thus reveals the complete molecular basis for S-layer glycan biosynthesis.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	30
Volume Number	283
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2008-07-25
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Gene Expression Regulation, Bacterial Geobacillus Stearothermophilus Metabolism Membrane Glycoproteins Chemistry Polysaccharides Chromatography, Thin Layer Escherichia Coli Glycosylation Magnetic Resonance Spectroscopy Models, Biological Models, Chemical Multigene Family Plasmids Biosynthesis Protein Structure, Tertiary Recombinant Proteins Spectrometry, Mass, Electrospray Ionization Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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