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)

Type
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
    in Planta
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • 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)
Pagina inizio
  • 940 (literal)
Pagina fine
  • 948 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 215 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
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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