Imperial College London
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Dr Tiago Costa

Faculty of Natural Sciences, Department of Life Sciences

Senior Lecturer in Bacterial Pathogenesis
 
 
 
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Contact

 

+44 (0)20 7594 3696t.costa Website

 
 
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Location

 

5.02Sir Ernst Chain BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Williams:2019:10.1038/s41467-019-10782-0,
author = {Williams, AH and Redzej, A and Rolhion, N and Costa, TRD and Rifflet, A and Waksman, G and Cossart, P},
doi = {10.1038/s41467-019-10782-0},
journal = {Nature Communications},
title = {The cryo-electron microscopy supramolecular structure of the bacterial stressosome unveils its mechanism of activation},
url = {http://dx.doi.org/10.1038/s41467-019-10782-0},
volume = {10},
year = {2019}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - How the stressosome, the epicenter of the stress response in bacteria, transmits stress signals from the environment has remained elusive. The stressosome consists of multiple copies of three proteins RsbR, RsbS and RsbT, a kinase that is important for its activation. Using cryo-electron microscopy, we determined the atomic organization of the Listeria monocytogenes stressosome at 3.38 Å resolution. RsbR and RsbS are organized in a 60-protomers truncated icosahedron. A key phosphorylation site on RsbR (T209) is partially hidden by an RsbR flexible loop, whose "open" or "closed" position could modulate stressosome activity. Interaction between three glutamic acids in the N-terminal domain of RsbR and the membrane-bound mini-protein Prli42 is essential for Listeria survival to stress. Together, our data provide the atomic model of the stressosome core and highlight a loop important for stressosome activation, paving the way towards elucidating the mechanism of signal transduction by the stressosome in bacteria.
AU  - Williams,AH
AU  - Redzej,A
AU  - Rolhion,N
AU  - Costa,TRD
AU  - Rifflet,A
AU  - Waksman,G
AU  - Cossart,P
DO  - 10.1038/s41467-019-10782-0
PY  - 2019///
SN  - 2041-1723
TI  - The cryo-electron microscopy supramolecular structure of the bacterial stressosome unveils its mechanism of activation
T2  - Nature Communications
UR  - http://dx.doi.org/10.1038/s41467-019-10782-0
UR  - https://www.ncbi.nlm.nih.gov/pubmed/31285450
UR  - http://hdl.handle.net/10044/1/71787
VL  - 10
ER  -
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