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The molecular pH-response mechanism of the plant light-stress sensor PsbS
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Journal Article
The molecular pH-response mechanism of the plant light-stress sensor PsbS
2021
Overview
Plants need to protect themselves from excess light, which causes photo-oxidative damage and lowers the efficiency of photosynthesis. Photosystem II subunit S (PsbS) is a pH sensor protein that plays a crucial role in plant photoprotection by detecting thylakoid lumen acidification in excess light conditions via two lumen-faced glutamates. However, how PsbS is activated under low-pH conditions is unknown. To reveal the molecular response of PsbS to low pH, here we perform an NMR, FTIR and 2DIR spectroscopic analysis of
Physcomitrella patens
PsbS and of the E176Q mutant in which an active glutamate has been replaced. The PsbS response mechanism at low pH involves the concerted action of repositioning of a short amphipathic helix containing E176 facing the lumen and folding of the luminal loop fragment adjacent to E71 to a 3
10
-helix, providing clear evidence of a conformational pH switch. We propose that this concerted mechanism is a shared motif of proteins of the light-harvesting family that may control thylakoid inter-protein interactions driving photoregulatory responses.
Photosystem II subunit S (PsbS) senses thylakoid lumen acidification when plants are exposed to excess light. Here the authors use NMR and IR spectroscopy to show that low pH causes repositioning of an amphipathic helix and folding of a loop involving critical pH sensing glutamate residues in PsbS.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 140/131
/ 631/1647
/ 631/57
/ 82/16
/ 82/80
/ 82/83
/ Bryopsida - radiation effects
/ Folding
/ Humanities and Social Sciences
/ Hydrogen-Ion Concentration - radiation effects
/ NMR
/ Nuclear Magnetic Resonance, Biomolecular
/ Photosystem II Protein Complex - genetics
/ Photosystem II Protein Complex - isolation & purification
/ Photosystem II Protein Complex - metabolism
/ Photosystem II Protein Complex - ultrastructure
/ Protein Conformation, alpha-Helical
/ Proteins
/ Recombinant Proteins - genetics
/ Recombinant Proteins - isolation & purification
/ Recombinant Proteins - metabolism
/ Recombinant Proteins - ultrastructure
/ Science
