Role of serine/threonine protein kinase STN7 in the formation of two distinct photosystem I supercomplexes in Physcomitrium patens.
Arabidopsis
/ metabolism
Arabidopsis Proteins
/ metabolism
Bryopsida
/ genetics
Light
Light-Harvesting Protein Complexes
/ genetics
Phosphorylation
Photosystem I Protein Complex
/ metabolism
Photosystem II Protein Complex
/ metabolism
Protein Serine-Threonine Kinases
Serine
/ metabolism
Threonine
/ metabolism
Journal
Plant physiology
ISSN: 1532-2548
Titre abrégé: Plant Physiol
Pays: United States
ID NLM: 0401224
Informations de publication
Date de publication:
29 08 2022
29 08 2022
Historique:
received:
05
04
2022
accepted:
26
05
2022
pubmed:
24
6
2022
medline:
9
9
2022
entrez:
23
6
2022
Statut:
ppublish
Résumé
Reversible thylakoid protein phosphorylation provides most flowering plants with dynamic acclimation to short-term changes in environmental light conditions. Here, through generating Serine/Threonine protein kinase 7 (STN7)-depleted mutants in the moss Physcomitrella (Physcomitrium patens), we identified phosphorylation targets of STN7 kinase and their roles in short- and long-term acclimation of the moss to changing light conditions. Biochemical and mass spectrometry analyses revealed STN7-dependent phosphorylation of N-terminal Thr in specific Light-Harvesting Complex II (LHCII) trimer subunits (LHCBM2 and LHCBM4/8) and provided evidence that phospho-LHCBM accumulation is responsible for the assembly of two distinct Photosystem I (PSI) supercomplexes (SCs), both of which are largely absent in STN7-depleted mutants. Besides the canonical state transition complex (PSI-LHCI-LHCII), we isolated the larger moss-specific PSI-Large (PSI-LHCI-LHCB9-LHCII) from stroma-exposed thylakoids. Unlike PSI-LHCI-LHCII, PSI-Large did not demonstrate short-term dynamics for balancing the distribution of excitation energy between PSII and PSI. Instead, PSI-Large contributed to a more stable increase in PSI antenna size in Physcomitrella, except under prolonged high irradiance. Additionally, the STN7-depleted mutants revealed altered light-dependent phosphorylation of a monomeric antenna protein, LHCB6, whose phosphorylation displayed a complex regulation by multiple kinases. Collectively, the unique phosphorylation plasticity and dynamics of Physcomitrella monomeric LHCB6 and trimeric LHCBM isoforms, together with the presence of PSI SCs with different antenna sizes and responsiveness to light changes, reflect the evolutionary position of mosses between green algae and vascular plants, yet with clear moss-specific features emphasizing their adaptation to terrestrial low-light environments.
Identifiants
pubmed: 35736511
pii: 6613940
doi: 10.1093/plphys/kiac294
pmc: PMC9434285
doi:
Substances chimiques
Arabidopsis Proteins
0
Light-Harvesting Protein Complexes
0
Photosystem I Protein Complex
0
Photosystem II Protein Complex
0
Threonine
2ZD004190S
Serine
452VLY9402
Protein Serine-Threonine Kinases
EC 2.7.11.1
STN7 protein, Arabidopsis
EC 2.7.11.1
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
698-713Informations de copyright
© The Author(s) 2022. Published by Oxford University Press on behalf of American Society of Plant Biologists.
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