TY - JOUR
T1 - Super-resolving microscopy reveals the localizations and movement dynamics of stressosome proteins in Listeria monocytogenes
AU - Tran, Buu Minh
AU - Linnik, Dmitrii Sergeevich
AU - Punter, Christiaan Michiel
AU - Śmigiel, Wojciech Mikołaj
AU - Mantovanelli, Luca
AU - Iyer, Aditya
AU - O’Byrne, Conor
AU - Abee, Tjakko
AU - Johansson, Jörgen
AU - Poolman, Bert
N1 - Funding Information:
We thank Duarte N. Guerreiro for discussions. We thank Pascal Cossart for sharing the strain L. monocytogenes EGD-e Δprli42 and the plasmid pAD-Prli42-FLAG. This project has received funding from the European Union’s Horizon 2020 Research and Innovation Program under the Marie Skłodowska-Curie grant agreement no. 721456. The EU Marie-Curie ITN project SynCrop (project number 764591) and an ERC Advanced grant “ABCVolume” (grant number 670578).
Publisher Copyright:
© 2023, The Author(s).
PY - 2023/1/14
Y1 - 2023/1/14
N2 - The human pathogen Listeria monocytogenes can cope with severe environmental challenges, for which the high molecular weight stressosome complex acts as the sensing hub in a complicated signal transduction pathway. Here, we show the dynamics and functional roles of the stressosome protein RsbR1 and its paralogue, the blue-light receptor RsbL, using photo-activated localization microscopy combined with single-particle tracking and single-molecule displacement mapping and supported by physiological studies. In live cells, RsbR1 is present in multiple states: in protomers with RsbS, large clusters of stressosome complexes, and in connection with the plasma membrane via Prli42. RsbL diffuses freely in the cytoplasm but forms clusters upon exposure to light. The clustering of RsbL is independent of the presence of Prli42. Our work provides a comprehensive view of the spatial organization and intracellular dynamics of the stressosome proteins in L. monocytogenes, which paves the way towards uncovering the stress-sensing mechanism of this signal transduction pathway.
AB - The human pathogen Listeria monocytogenes can cope with severe environmental challenges, for which the high molecular weight stressosome complex acts as the sensing hub in a complicated signal transduction pathway. Here, we show the dynamics and functional roles of the stressosome protein RsbR1 and its paralogue, the blue-light receptor RsbL, using photo-activated localization microscopy combined with single-particle tracking and single-molecule displacement mapping and supported by physiological studies. In live cells, RsbR1 is present in multiple states: in protomers with RsbS, large clusters of stressosome complexes, and in connection with the plasma membrane via Prli42. RsbL diffuses freely in the cytoplasm but forms clusters upon exposure to light. The clustering of RsbL is independent of the presence of Prli42. Our work provides a comprehensive view of the spatial organization and intracellular dynamics of the stressosome proteins in L. monocytogenes, which paves the way towards uncovering the stress-sensing mechanism of this signal transduction pathway.
UR - http://www.scopus.com/inward/record.url?scp=85146299433&partnerID=8YFLogxK
U2 - 10.1038/s42003-023-04423-y
DO - 10.1038/s42003-023-04423-y
M3 - Article
C2 - 36641529
AN - SCOPUS:85146299433
SN - 2399-3642
VL - 6
JO - Communications biology
JF - Communications biology
IS - 1
M1 - 51
ER -