Abstract:
: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.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Williams AH,Redzej A,Rolhion N,Costa TRD,Rifflet A,Waksman G,Cossart Pdoi
10.1038/s41467-019-10782-0subject
Has Abstractpub_date
2019-07-08 00:00:00pages
3005issue
1issn
2041-1723pii
10.1038/s41467-019-10782-0journal_volume
10pub_type
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