Imperial College London
Alternate

Professor Angelika Gründling

Faculty of Medicine, Department of Infectious Disease

Professor of Molecular Microbiology
 
 
 
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Contact

 

+44 (0)20 7594 5256a.grundling Website

 
 
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Location

 

6.22Flowers buildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Wu:2021:10.1016/j.jbc.2021.100384,
author = {Wu, C-H and Rismondo, J and Morgan, RML and Shen, Y and Loessner, MJ and Larrouy-Maumus, G and Freemont, PS and Grundling, A},
doi = {10.1016/j.jbc.2021.100384},
journal = {Journal of Biological Chemistry},
pages = {1--14},
title = {Bacillus subtilis YngB contributes to wall teichoic acid glucosylation and glycolipid formation during anaerobic growth},
url = {http://dx.doi.org/10.1016/j.jbc.2021.100384},
volume = {296},
year = {2021}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - UTP-glucose-1-phosphate uridylyltransferases are enzymes that produce UDP-glucose from UTP and glucose-1-phosphate. In Bacillus subtilis 168, UDP-glucose is required for the decoration of wall teichoic acid (WTA) with glucose residues and the formation of glucolipids. The B. subtilis UGPase GtaB is essential for UDP-glucose production under standard aerobic growth conditions, and gtaB mutants display severe growth and morphological defects. However, bioinformatics predictions indicate that two other UTP-glucose-1-phosphate uridylyltransferases are present in B. subtilis. 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 in vitro using UTP and glucose-1-phosphate as substrates. Expression of YngB from a synthetic promoter in a B. subtilis gtaB mutant resulted in the reintroduction of glucose residues on WTA and production of glycolipids, demonstrating that the enzyme can function as UGPase in vivo. When WT and mutant B. subtilis 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 yngB 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 during oxygen-limited growth condition.
AU  - Wu,C-H
AU  - Rismondo,J
AU  - Morgan,RML
AU  - Shen,Y
AU  - Loessner,MJ
AU  - Larrouy-Maumus,G
AU  - Freemont,PS
AU  - Grundling,A
DO  - 10.1016/j.jbc.2021.100384
EP  - 14
PY  - 2021///
SN  - 0021-9258
SP  - 1
TI  - Bacillus subtilis YngB contributes to wall teichoic acid glucosylation and glycolipid formation during anaerobic growth
T2  - Journal of Biological Chemistry
UR  - http://dx.doi.org/10.1016/j.jbc.2021.100384
UR  - https://www.sciencedirect.com/science/article/pii/S0021925821001563
UR  - http://hdl.handle.net/10044/1/87726
VL  - 296
ER  -
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