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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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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-3D5D-7 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-3D5F-3
Genre: Journal Article

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 Creators:
Pesaresi, P.1, Author              
Lunde, C., Author
Jahns, P., Author
Tarantion, D., Author
Meurer, J., Author
Varotto, C.1, 2, Author              
Hirtz, R. D.1, Author              
Soave, C., Author
Scheller, H. V., Author
Salamini, F.1, Author              
Leister, D.1, Author              
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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Free keywords: Arabidopsis; mutant; photosynthesis; photosystem I; state transition
 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.

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Language(s): eng - English
 Dates: 2002-10
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: eDoc: 28773
ISI: 000178995100007
 Degree: -

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Title: Planta
  Alternative Title : Planta
Source Genre: Journal
 Creator(s):
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Publ. Info: -
Pages: - Volume / Issue: 215 (6) Sequence Number: - Start / End Page: 940 - 948 Identifier: ISSN: 0032-0935