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  • NAD(P)H-plastoquinone-oxidoreductase  (2)
  • psaC  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Studies on the expression of NDH-H, a subunit of the NAD(P)H-plastoquinone-oxidoreductase of higher-plant chloroplasts (1993)
    Springer
    Planta 190 (1993), S. 25-31 
    Details
    ISSN: 1432-2048
    Keywords: NAD(P)H-plastoquinone-oxidoreductase ; ndhH gene ; Plastid DNA
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The plastid genomes of higher plants contain eleven reading frames (ndhA-K) that are homologous to genes encoding subunits of the mitochondrial NADH-ubiquinone-oxidoreductase (complex I). The carboxyterminal end of the NDH-H subunit from rice (Oryza sativa L.) was expressed as a fusion protein in Escherichia coli and antibodies against the fusion protein were generated in rabbits. The antibody was used to study the expression of NDH-H, and the following results were obtained: (i) NDH-H is expressed in mono- and dicotyledonous plants, (ii) NDH-H is localized on the stroma lamellae of the thylakoid membrane and (iii) NDH-H is expressed in etioplasts. Together with the finding that two other ndh genes (ndhI and ndhK) are expressed in plastids, these results point to the existence of an NAD(P)H-plastoquinone-oxidoreductase on the thylakoid membrane. The possible function of the enzyme in plastids is discussed and it is suggested that it works in balancing the ATP/ADP and the NADPH/NADP ratios during changing external (i.e. light) or internal (i.e. ATP and NADPH demands of biosynthetic pathways of the plastid) conditions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00195671
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  • 2
    Electronic Resource
    Electronic Resource
    Differential expression of plastome-encoded ndh genes in mesophyll and bundle-sheath chloroplasts of the C4 plant Sorghum bicolor indicates that the complex I-homologous NAD(P)H-plastoquinone oxidoreductase is involved in cyclic electron transport (1996)
    Springer
    Planta 199 (1996), S. 276-281 
    Details
    ISSN: 1432-2048
    Keywords: C4 photosynthesis ; Cyclic electron transport ; NAD(P)H-plastoquinone-oxidoreductase ; Sorghum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Cyanobacteria and plastids harbor a putative NAD(P)H- or ferredoxin-plastoquinone oxidoreductase that is homologous to the NADH-ubiquinone oxidoreductase (complex I) of mitochondria and eubacteria. The enzyme is a multimeric protein complex that consists of at least 11 subunits (NDH-A-K) and is localized in the stroma lamellae of the thylakoid membrane system. We investigated the expression of the different subunits of the enzyme in mesophyll and bundle-sheath chloroplasts of Sorghum bicolor [L.] Moench, a C4 plant of the NADP-malic enzyme type. The relative amounts of the subunits NDH-H, -J and -K were strongly increased in bundle-sheath plastids as compared to mesophyll plastids. This increase was accompanied by enhanced transcript levels for all subunits except NDH-I. Because the main function of the protein complexes in the thylakoid membranes of bundle-sheath chloroplasts (photosystem I, cytochrome b 6/f-complex and ATPase) is the generation of ATP for CO2 fixation via cyclic electron transport, we conclude that the NAD(P)H/ferredoxin-plastoquinone oxidoreductase is an essential component of the cyclic electron-transport pathway in chloroplasts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00196569
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  • 3
    Electronic Resource
    Electronic Resource
    Identification of a second psaC gene in the cyanobacterium Synechocystis sp. PCC6803 (1992)
    Springer
    Plant molecular biology 20 (1992), S. 997-1001 
    Details
    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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00027170
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  • 4
    Electronic Resource
    Electronic Resource
    Cloning and transcription analysis of the ndh(A-I-G-E) gene cluster and the ndhD gene of the cyanobacterium Synechocystis sp. PCC6803 (1992)
    Springer
    Plant molecular biology 20 (1992), S. 1097-1110 
    Details
    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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00028896
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