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A stable LHCII-PSI aggregate and suppression of photosynthetic state transitions in the psae1-1 mutant of Arabidopsis thaliana

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Pesaresi,  P.
Dept. of Plant Breeding and Yield Physiology (Francesco Salamini), MPI for Plant Breeding Research, Max Planck Society;

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Varotto,  C.
Dept. of Plant Breeding and Yield Physiology (Francesco Salamini), MPI for Plant Breeding Research, Max Planck Society;
Dept. of Molecular Plant Genetics (Heinz Saedler), MPI for Plant Breeding Research, Max Planck Society;

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Hirtz,  R. D.
Dept. of Plant Breeding and Yield Physiology (Francesco Salamini), MPI for Plant Breeding Research, Max Planck Society;

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Salamini,  F.
Dept. of Plant Breeding and Yield Physiology (Francesco Salamini), MPI for Plant Breeding Research, Max Planck Society;

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Leister,  D.
Dept. of Plant Breeding and Yield Physiology (Francesco Salamini), MPI for Plant Breeding Research, Max Planck Society;

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Citation

Pesaresi, P., Lunde, C., Jahns, P., Tarantion, D., Meurer, J., Varotto, C., et al. (2002). A stable LHCII-PSI aggregate and suppression of photosynthetic state transitions in the psae1-1 mutant of Arabidopsis thaliana. Planta, 215(6), 940-948.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0012-3D5D-7
Abstract
During photosynthetic state transitions, a fraction of the major light-harvesting complex (LHCII) shuttles between photosystems II (PSII) and I (PSI), depending on whether or not it is phosphorylated. Its phosphorylation state in turn depends on the relative activity of the two photosystems, which is a function of redox state and illumination parameters. In the psae1-1 mutant of Arabidopsis thaliana (L.) Heynh., amounts of the PSI subunits E, C, D, H and L are decreased. A fraction of LHCII is stably associated with PSI when plants are exposed to low light conditions, giving rise to a high-molecular-mass protein-pigment complex detectable in native protein gels. The formation of this abnormal LHCII-PSI complex is associated with an almost complete suppression of state transitions, a drastic increase in the levels of phosphorylated LHCII under all light regimes tested, and a permanent reduction in PSII antenna size. All these observations suggest that the altered polypeptide composition of PSI perturbs the docking of phosphorylated LHCII, making psae1-1 a unique mutant for the study of PSI- LHCII interactions and additional effects of the mutation, such as a decrease in grana stacking and increased adenylate kinase activity.