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{Pompeo:2018:10.1038/s41598-018-35696-7,
author = {Pompeo, F and Rismondo, J and Gründling, A and Galinier, A},
doi = {10.1038/s41598-018-35696-7},
journal = {Scientific Reports},
title = {Investigation of the phosphorylation of Bacillus subtilis LTA synthases by the serine/threonine kinase PrkC},
url = {http://dx.doi.org/10.1038/s41598-018-35696-7},
volume = {8},
year = {2018}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Bacillus subtilis possesses four lipoteichoic acid synthases LtaS, YfnI, YvgJ and YqgS involved in the synthesis of cell wall. The crystal structure of the extracellular domain of LtaS revealed a phosphorylated threonine and YfnI was identified in two independent phosphoproteome studies. Here, we show that the four LTA synthases can be phosphorylated in vitro by the Ser/Thr kinase PrkC. Phosphorylation neither affects the export/release of YfnI nor its substrate binding. However, we observed that a phosphomimetic form of YfnI was active whereas its phosphoablative form was inactive. The phenotypes of the strains deleted for prkC or prpC (coding for a phosphatase) are fairly similar to those of the strains producing the phosphoablative or phosphomimetic YfnI proteins. Clear evidence proving that PrkC phosphorylates YfnI in vivo is still missing but our data suggest that the activity of all LTA synthases may be regulated by phosphorylation. Nonetheless, their function is non-redundant in cell. Indeed, the deletion of either ltaS or yfnI gene could restore a normal growth and shape to a ΔyvcK mutant strain but this was not the case for yvgJ or yqgS. The synthesis of cell wall must then be highly regulated to guarantee correct morphogenesis whatever the growth conditions.
AU  - Pompeo,F
AU  - Rismondo,J
AU  - Gründling,A
AU  - Galinier,A
DO  - 10.1038/s41598-018-35696-7
PY  - 2018///
SN  - 2045-2322
TI  - Investigation of the phosphorylation of Bacillus subtilis LTA synthases by the serine/threonine kinase PrkC
T2  - Scientific Reports
UR  - http://dx.doi.org/10.1038/s41598-018-35696-7
UR  - http://hdl.handle.net/10044/1/64740
VL  - 8
ER  -
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