Impaired photosystem I oxidation induces STN7-dependent phosphorylation of the light-harvesting complex I protein Lhca4 in Arabidopsis thaliana
Planta, 2008•Springer
Reduction of the plastoquinone (PQ) pool is known to activate phosphorylation of thylakoid
proteins. In the Arabidopsis thaliana mutants psad1-1 and psae1-3, oxidation of
photosystem I (PSI) is impaired, and the PQ pool is correspondingly over-reduced. We show
here that, under these conditions, the antenna protein Lhca4 of PSI becomes a target for
phosphorylation. Phosphorylation of the mature Lhca4 protein at Thr16 is suppressed in
stn7 psad1 and s tn7 psae1 double mutants. Thus, under extreme redox conditions …
proteins. In the Arabidopsis thaliana mutants psad1-1 and psae1-3, oxidation of
photosystem I (PSI) is impaired, and the PQ pool is correspondingly over-reduced. We show
here that, under these conditions, the antenna protein Lhca4 of PSI becomes a target for
phosphorylation. Phosphorylation of the mature Lhca4 protein at Thr16 is suppressed in
stn7 psad1 and s tn7 psae1 double mutants. Thus, under extreme redox conditions …
Abstract
Reduction of the plastoquinone (PQ) pool is known to activate phosphorylation of thylakoid proteins. In the Arabidopsis thaliana mutants psad1-1 and psae1-3, oxidation of photosystem I (PSI) is impaired, and the PQ pool is correspondingly over-reduced. We show here that, under these conditions, the antenna protein Lhca4 of PSI becomes a target for phosphorylation. Phosphorylation of the mature Lhca4 protein at Thr16 is suppressed in stn7 psad1 and stn7 psae1 double mutants. Thus, under extreme redox conditions, hyperactivation of thylakoid protein kinases and/or reorganization of thylakoid protein complex distribution increase the susceptibility of PSI to phosphorylation.
Springer
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