Imperial College London
Alternate

DrGeraldLarrouy-Maumus

Faculty of Natural Sciences, Department of Life Sciences

Reader in Molecular Microbiology
 
 
 
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Contact

 

+44 (0)20 7594 7463g.larrouy-maumus

 
 
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Location

 

3.42Flowers buildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@unpublished{Wu:2020:10.1101/2020.11.30.405621,
author = {Wu, C-H and Rismondo, J and Morgan, RML and Shen, Y and Loessner, MJ and Larrouy-Maumus, G and Freemont, PS and Gründling, A},
doi = {10.1101/2020.11.30.405621},
title = {<i>Bacillus subtilis</i>YngB contributes to wall teichoic acid glucosylation and glycolipid formation during anaerobic growth},
url = {http://dx.doi.org/10.1101/2020.11.30.405621},
year = {2020}
}
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RIS format (EndNote, RefMan)

TY  - UNPB
AB  - <jats:title>Abstract</jats:title><jats:p>UTP-glucose-1-phosphate uridylyltransferases (UGPases) are enzymes that produce UDP-glucose from UTP and glucose-1-phosphate. In<jats:italic>Bacillus subtilis</jats:italic>168, UDP-glucose is required for the decoration of wall teichoic acid (WTA) with glucose residues and the formation of glucolipids. The<jats:italic>B. subtilis</jats:italic>UGPase GtaB is essential for UDP-glucose production under standard aerobic growth conditions, and<jats:italic>gtaB</jats:italic>mutants display severe growth and morphological defects. However, bioinformatics predictions indicate that two other UGPases, are present in<jats:italic>B. subtilis</jats:italic>. Here, we investigated the function of one of them named YngB. The crystal structure of YngB revealed that the protein has the typical fold and all necessary active site features of a functional UGPase. Furthermore, UGPase activity could be demonstrated<jats:italic>in vitro</jats:italic>using UTP and glucose-1-phosphate as substrates. Expression of YngB from a synthetic promoter in a<jats:italic>B. subtilis gtaB</jats:italic>mutant resulted in the reintroduction of glucose residues on WTA and production of glycolipids, demonstrating that the enzyme can function as UGPase<jats:italic>in vivo</jats:italic>. When wild-type and mutant<jats:italic>B. subtilis</jats:italic>strains were grown under anaerobic conditions, YngB-dependent glycolipid production and glucose decorations on WTA could be detected, revealing that YngB is expressed from its native promoter under anaerobic condition. Based on these findings, along with the structure of the operon containing<jats:italic>yngB</jats:italic>and the transcription factor thought to be required for its expression, we propose that besides WTA, potentially other cell wall components might be decorated with glucose residues
AU  - Wu,C-H
AU  - Rismondo,J
AU  - Morgan,RML
AU  - Shen,Y
AU  - Loessner,MJ
AU  - Larrouy-Maumus,G
AU  - Freemont,PS
AU  - Gründling,A
DO  - 10.1101/2020.11.30.405621
PY  - 2020///
TI  - <i>Bacillus subtilis</i>YngB contributes to wall teichoic acid glucosylation and glycolipid formation during anaerobic growth
UR  - http://dx.doi.org/10.1101/2020.11.30.405621
ER  -
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