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© Pierre Gounon
Entrée de Listeria dans une cellule épithéliale (Grossissement X 10000). Image colorisée.
Publication : Nature communications

The cryo-electron microscopy supramolecular structure of the bacterial stressosome unveils its mechanism of activation

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Nature communications - 08 Jul 2019

Williams AH, Redzej A, Rolhion N, Costa TRD, Rifflet A, Waksman G, Cossart P

Link to Pubmed [PMID] – 31285450

Nat Commun 2019 07;10(1):3005

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.

https://www.ncbi.nlm.nih.gov/pubmed/31285450