Remodeling of algal photosystem I through phosphorylation

Photosystem I (PSI) with its associated light-harvesting system is the most important generator of reducing power in photosynthesis. The PSI core complex is highly conserved, whereas peripheral subunits as well as light-harvesting proteins (LHCI) reveal a dynamic plasticity. Moreover, in green alga,...

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Bibliographic Details
Published in:Bioscience reports Vol. 43; no. 1; p. 1
Main Authors: Younas, Muhammad, Scholz, Martin, Marchetti, Giulia Maria, Hippler, Michael
Format: Journal Article
Language:English
Published: England Portland Press Ltd The Biochemical Society 01.01.2023
Portland Press Ltd
Subjects:
Algae
Aquatic plants
Bioenergetics
Biotechnology
Chlamydomonas reinhardtii - metabolism
Chloroplasts
Electrons
Flowers & plants
Hydrogen bonds
Kinases
Light
Light-Harvesting Protein Complexes - metabolism
Light-harvesting proteins
Microscopy
Molecular Interactions
Phosphorylation
Photosynthesis
Photosystem I
Photosystem I Protein Complex - metabolism
Plant Biology
Post-Translational Modifications
Proteins
Structural Biology
Sulfur
Thylakoids
green algae
phosphorylation/dephosphorylation
Light harvesting proteins
photosystems
ISSN:0144-8463, 1573-4935, 1573-4935
Online Access:Get full text
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Summary:Photosystem I (PSI) with its associated light-harvesting system is the most important generator of reducing power in photosynthesis. The PSI core complex is highly conserved, whereas peripheral subunits as well as light-harvesting proteins (LHCI) reveal a dynamic plasticity. Moreover, in green alga, PSI–LHCI complexes are found as monomers, dimers, and state transition complexes, where two LHCII trimers are associated. Herein, we show light-dependent phosphorylation of PSI subunits PsaG and PsaH as well as Lhca6. Potential consequences of the dynamic phosphorylation of PsaG and PsaH are structurally analyzed and discussed in regard to the formation of the monomeric, dimeric, and LHCII-associated PSI–LHCI complexes.
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ISSN:0144-8463
1573-4935
1573-4935
DOI:10.1042/BSR20220369