Functional organization of thylakoid membranes in viable pea mutants with low chlorophyll content.
In: Physiologia Plantarum, Jg. 96 (1996-03-01), Heft 3, S. 439-445
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Zugriff:
The functional organizations of thylakoid membranes from wild type pea (Pisum sativum L. cv. Kapital) and two viable mutants with low chlorophyll (Chl) contents were compared. Nuclear mutations in mutants 7 and 42 led to two- and three-fold decrease in total chlorophyll content, respectively. In spite of low Chl content mutants showed 80% photosynthetic activity, biological productivity, and seed production. It has been shown that mutant membranes differed from that of wild type by Chl distribution between the pigment-protein complexes and by stoichiometry of the main electron-transport complexes. The ratio photosystem I (PSI): photosystem II (PSII): cytochrome (Cyt) b6/f complex: Chl was 1:1.1:1.2:650 in wild type chloroplasts, 1:1.8:1.7:600 in mutant 7, and 1:1.5:1.9:350 in mutant 42. PSI- and PSII-dependent electron-transport activities were enhanced in the mutants per mg Chl in proportion to number of reaction centers. The activity of the non-cyclic electron-transport chain increased in proportion to PSII and Cyt b6/f complexes. The amount of ATP synthetase per unit of Chl as estimated by H+-ATPase activity was much greater in mutant thylakoids, which is favorable for photosynthetic energy transduction. The low content of the light-harvesting complexes (LHC) in mutants is compensated by an increase of the number of PSII and Cyt b6/f complexes, which eliminates the bottleneck at the site of plastoquinone oxidation. [ABSTRACT FROM AUTHOR]
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Functional organization of thylakoid membranes in viable pea mutants with low chlorophyll content.
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Autor/in / Beteiligte Person: | Krendeleva, T. E. ; Kukarskikh, G. P ; Nizovskaya, N. V. ; Rubin, A. B. |
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Zeitschrift: | Physiologia Plantarum, Jg. 96 (1996-03-01), Heft 3, S. 439-445 |
Veröffentlichung: | 1996 |
Medientyp: | academicJournal |
ISSN: | 0031-9317 (print) |
DOI: | 10.1111/j.1399-3054.1996.tb00456.x |
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