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The distribution of photosynthetic excitation energy in the psae1-1 mutant of Arabidopsis is arrested in state 2 due to constitutive association of LHCII with photosystem I (Articolo in rivista)
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- Label
- The distribution of photosynthetic excitation energy in the psae1-1 mutant of Arabidopsis is arrested in state 2 due to constitutive association of LHCII with photosystem I (Articolo in rivista) (literal)
- Anno
- 2002-01-01T00:00:00+01:00 (literal)
- Alternative label
Pesaresi P., C. Lunde P. Jahns D. Tarantino J. Meurer C. Varotto, Hirtz R.D., Soave C., Scheller H.V., Salamini F., Leister D. (2002)
The distribution of photosynthetic excitation energy in the psae1-1 mutant of Arabidopsis is arrested in state 2 due to constitutive association of LHCII with photosystem I
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- Pesaresi P., C. Lunde P. Jahns D. Tarantino J. Meurer C. Varotto, Hirtz R.D., Soave C., Scheller H.V., Salamini F., Leister D. (literal)
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- Titolo
- The distribution of photosynthetic excitation energy in the psae1-1 mutant of Arabidopsis is arrested in state 2 due to constitutive association of LHCII with photosystem I (literal)
- 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. (literal)
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