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

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.

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Pesaresi, P.1, Autor           
Lunde, C., Autor
Jahns, P., Autor
Tarantion, D., Autor
Meurer, J., Autor
Varotto, C.1, 2, Autor           
Hirtz, R. D.1, Autor           
Soave, C., Autor
Scheller, H. V., Autor
Salamini, F.1, Autor           
Leister, D.1, Autor           
Affiliations:
1Dept. of Plant Breeding and Yield Physiology (Francesco Salamini), MPI for Plant Breeding Research, Max Planck Society, ou_1113570              
2Dept. of Molecular Plant Genetics (Heinz Saedler), MPI for Plant Breeding Research, Max Planck Society, ou_1113568              

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Schlagwörter: Arabidopsis; mutant; photosynthesis; photosystem I; state transition
 Zusammenfassung: 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.

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Sprache(n): eng - English
 Datum: 2002-10
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: eDoc: 28773
ISI: 000178995100007
 Art des Abschluß: -

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Titel: Planta
  Alternativer Titel : Planta
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 215 (6) Artikelnummer: - Start- / Endseite: 940 - 948 Identifikator: ISSN: 0032-0935