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  • Plastoglobuli composition  (2)
  • psaC  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Planta 163 (1985), S. 91-96 
    ISSN: 1432-2048
    Keywords: Chloroplast senescence ; Fagus ; Leaf lipid ; Plastoglobuli composition
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The lipid composition of whole leaves and isolated plastoglobul of beech (Fagus sylvatica) has been studied during four natural autumnal senescence stages. Chlorophylls, glycolipids, and phospholipids were extensively degraded in leaves. About 20% of the glycolipids found in leaves during summer, however, remained in the last stage of leaf senescence. Triacylglycerols, also detected in large amounts in summer leaves, were hydrolyzed during senescence. The content of free fatty acids derived from degradation of glycerolipids therefore increased. The total carotenoid and prenyl quinone content was largely unchanged during senescence, except during the last stage investigated, but the reduced forms of prenyl quinones decreased while the oxidized prenyl quinones increased. Plastoglobuli isolated from summer leaves mainly contained triacylglycerols, plastohydroquinone, and α-tocopherol. The triacylglycerol content declined in plastoglobuli during senescence. Most of the triacylglycerols must be located outside the plastoglobuli throughout the stages investigated. Carotenoids liberated from thylakoids were esterified and increasingly deposited in plastoglobuli during senescence. In the last senescence stage, carotenoid esters were the main component of plastoglobuli. Prenyl quinones were also transferred into plastoglobuli. Reduced prenyl quinones were sucessively oxidized during senescence and plastoquinone (oxidized) was the predominant prenyl quinone in plastoglobuli isolated from the last senescence stage. The carotenoid and prenyl quinone distribution was identical in leaves and plastoglobuli during late senescence. The main constituents of thylakoids, glycolipids and proteins, were not deposited in plastoglobuli and therefore did not play an important role in plastoglobuli metabolism.
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Planta 163 (1985), S. 201-207 
    ISSN: 1432-2048
    Keywords: Plastoglobuli composition ; Spinacia ; Fagus ; Sarothamnus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Plastoglobuli have been isolated and purified from chloroplasts of beech and spinach leaves and from broom flower chromoplasts by a repeated floating-gradient technique. The main components in plastoglobuli isolated from chloroplasts were triacylglycerols and lipophilic prenyl quinones, mainly plastohydroquinone and α-tocopherol. The corresponding oxidized prenyl quinones, plastoquinone (ox), α-tocoquinone, and the phylloquinone vitamin K1, were detected in trace amounts. Plastoglobuli isolated from chromoplasts contained large amounts of carotenoid esters. Triacylglycerols constituted two-thirds of the content of these plastoglobuli. The total prenyl quinone content was low in chromoplast plastoglobuli. Plastoquinone (ox) was the major prenyl quinone constituent. Plastoglobuli contained small amounts of chlorophylls, carotenoids (with the exception of chromoplast plastoglobuli), glycolipids, and proteins due to adsorption phenomena during the isolation process; however, increasing purification of the plastoglobuli fractions resulted in an exponential decline of these components. Adsorption of thylakoid lipids onto the plastoglobuli during the isolation process was demonstrated using an artificial globuli system. Therefore, pigments, glyco- and phospholipids, and proteins were regarded as thylakoid contaminations and not as actual constituents of plastoglobuli.
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Plant molecular biology 20 (1992), S. 997-1001 
    ISSN: 1573-5028
    Keywords: Synechocystis sp. PCC6803 ; photosystem I ; iron-sulfur protein ; psaC
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The psaC gene encodes the 9 kDa protein subunit of photosystem I that carries the iron-sulfur centers FA and FB. The paper describes the sequence and transcription analysis of a second psaC gene (psaC2) from Synechocystis sp. PCC6803. The psaC2 gene is transcribed into an abundant monocistronic mRNA. The deduced amino acid sequence of PSI-C2 is very similar to the protein sequences from two other cyanobacteria (Synechococcus sp. PCC7002 and Nostoc sp. PCC8009). In contrast, the recently isolated psaC1 gene is not transcribed and the PSI-C1 amino acid sequence shows the highest similarity to the proteins from higher plants.
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  • 4
    ISSN: 1573-5028
    Keywords: Synechocystis sp. PCC6803 ; NAD(P)H-plastoquinone oxidoreductase ; ndhA ; ndhI ; ndhG ; ndhE ; ndhE ; ndhD ; psaC
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The plastid DNA of higher plants contains eleven reading frames that are homologous to subunits of the mitochondrial NADH-ubiquinone oxidoreductase (complex I). The genes are expressed, but a plastid NAD(P)H dehydrogenase has not yet been isolated and the function of the enzyme in plastid metabolism is unknown. Cyanobacteria also contain a NADH dehydrogenase that is homologous to the mitochondrial complex I. The enzyme is sensitive to rotenone and is located on the cytoplasmic and the thylakoid membrane. We report here the sequence of five subunits (ndhA,-I, G,-E and -D) of the NADH dehydrogenase from the unicellular cyanobacterium Synechocystis sp. PCC6803. As in plastid DNA, the genes ndh(A-I-G-E) are clustered and probably constitute an operon. The ndhD gene is associated with a gene encoding an iron-sulphur protein of photosystem I (psaC) as in plastid DNA. In contrast to the situation in plastids, psaC and ndhD are not cotranscribed but transcribed from opposite strands. The deduced amino acid sequence of the cyanobacterial polypeptides is more similar to the corresponding plastid (40–68% identity) than to the corresponding mitochondrial subunits (17–39% identity). Thus, the cyanobacterial NADH-dehydrogenase provides a prokaryotic model system which is more suitable to genetic analysis than the enzyme of plastids.
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