TY - JOUR
T1 - Tudor staphylococcal nuclease is a docking platform for stress granule components and is essential for SnRK1 activation in Arabidopsis
AU - Gutierrez-Beltran, Emilio
AU - Elander, Pernilla
AU - Dalman, Kerstin
AU - Dayhoff, Guy W.
AU - Moschou, Panagiotis Nikolaou
AU - Uversky, Vladimir N.
AU - Crespo, Jose L.
AU - Bozhkov, Peter
PY - 2021
Y1 - 2021
N2 - Tudor staphylococcal nuclease (TSN; also known as Tudor-SN, p100, or SND1) is a multifunctional, evolutionarily conserved regulator of gene expression, exhibiting cytoprotective activity in animals and plants and oncogenic activity in mammals. During stress, TSN stably associates with stress granules (SGs), in a poorly understood process. Here, we show that in the model plant Arabidopsis thaliana, TSN is an intrinsically disordered protein (IDP) acting as a scaffold for a large pool of other IDPs, enriched for conserved stress granule components as well as novel or plant-specific SG-localized proteins. While approximately 30% of TSN interactors are recruited to stress granules de novo upon stress perception, 70% form a protein-protein interaction network present before the onset of stress. Finally, we demonstrate that TSN and stress granule formation promote heat-induced activation of the evolutionarily conserved energy-sensing SNF1-related protein kinase 1 (SnRK1), the plant orthologue of mammalian AMP-activated protein kinase (AMPK). Our results establish TSN as a docking platform for stress granule proteins, with an important role in stress signalling.
AB - Tudor staphylococcal nuclease (TSN; also known as Tudor-SN, p100, or SND1) is a multifunctional, evolutionarily conserved regulator of gene expression, exhibiting cytoprotective activity in animals and plants and oncogenic activity in mammals. During stress, TSN stably associates with stress granules (SGs), in a poorly understood process. Here, we show that in the model plant Arabidopsis thaliana, TSN is an intrinsically disordered protein (IDP) acting as a scaffold for a large pool of other IDPs, enriched for conserved stress granule components as well as novel or plant-specific SG-localized proteins. While approximately 30% of TSN interactors are recruited to stress granules de novo upon stress perception, 70% form a protein-protein interaction network present before the onset of stress. Finally, we demonstrate that TSN and stress granule formation promote heat-induced activation of the evolutionarily conserved energy-sensing SNF1-related protein kinase 1 (SnRK1), the plant orthologue of mammalian AMP-activated protein kinase (AMPK). Our results establish TSN as a docking platform for stress granule proteins, with an important role in stress signalling.
KW - heat stress
KW - intrinsically disordered regions
KW - SnRK1
KW - SNF1
KW - AMPK
KW - stress granules
KW - tudor staphylococcal nuclease
KW - heat stress
KW - intrinsically disordered regions
KW - SnRK1
KW - SNF1
KW - AMPK
KW - stress granules
KW - tudor staphylococcal nuclease
UR - https://res.slu.se/id/publ/113227
U2 - 10.15252/embj.2020105043
DO - 10.15252/embj.2020105043
M3 - Journal article
SN - 0261-4189
VL - 40
JO - The Embo Journal
JF - The Embo Journal
IS - 17
M1 - e105043
ER -