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  • 1
    Electronic Resource
    Electronic Resource
    Cytokinins, abscisic acid and light affect accumulation of chloroplast proteins in Lupinus luteus cotyledons without notable effect on steady-state mRNA levels (1994)
    Springer
    Planta 194 (1994), S. 318-327 
    Details
    ISSN: 1432-2048
    Keywords: Abscisic acid ; Chloroplast proteins ; Cytokinin ; Gene expression ; Lupinus ; Photosynthesis (Light regulation)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Etiolated lupine (Lupinus luteus L.) cotyledons respond in a highly sensitive manner to phytohormones and light. The effects of cytokinin, abscisic acid, gibberellic acid (GA3) and indolylacetic acid (IAA) have been studied at the ultrastructural, steady-state mRNA and protein levels using 15 gene-specific probes for plastid proteins and corresponding antisera. No effect was noted with GA3 and IAA. As in other systems, N6-benzylaminopurine (BAP) and abscisic acid (ABA) operated antagonistically. In both instances, the steady-state mRNA levels remained relatively unaffected for plastid-encoded polypeptides, but not for those nuclear-encoded genes that could be tested. On the other hand, synthesis and accumulation of proteins of nuclear and plastid origin varied significantly. Cytokinin strongly promoted the accumulation of cytochrome b 559 and subunit IV of the cytochrome b/f complex, while little effect was observed for cytochrome b 6, the β subunit of the chloroplast ATP synthase or the large subunit of ribulose-1,5-bisphosphate carboxylase. In etiolated seedlings the level of chlorophyll-binding proteins (the 43-kDa chlorophyll a protein of photosystem II and subunits I a, b of photosystem I) was below the level of detectability. Their accumulation in light was promoted by cytokinin and inhibited by ABA though to different extents. Cytochrome b 559 and the 33-kDa polypeptide of the water-oxidizing complex were not detectable in water-(control) and ABA-treated cotyledons. Cytokinin induced the synthesis of these proteins, even in darkness. These results indicate a protein-specific response to phytohormones, which can differ even for polypeptides belonging to the same membrane complex. They also suggest different modes of interaction between hormones and light, quite different phytohormone action in the two compartments, and demonstrate that phytohormones influence the biogenesis of the thylakoid membrane mainly posttranscriptionally.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00197531
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  • 2
    Electronic Resource
    Electronic Resource
    Nucleotide sequence of cDNA clones encoding the complete precursor for subunit delta of thylakoid-located ATP synthase from spinach (1988)
    Springer
    Plant molecular biology 10 (1988), S. 323-330 
    Details
    ISSN: 1573-5028
    Keywords: chloroplast ATP synthase ; subunit delta ; cDNA nucleotide sequence ; transit peptide ; spinach
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The nucleotide sequence of the entire nuclear-encoded precursor for subunit delta of the ATP synthase from spinach thylakoid membranes was determined by cDNA sequencing. Appropriate recombinant DNAs were selected from pBR322 and lambda gt11 libraries made from polyadenylated RNA of greening spinach seedlings. The mature protein consists of 187 amino acid residues corresponding to a molecular weight of 20468. The precursor protein (257 amino acid residues; M r=27676) is probably processed between a Met-Val bond. The predicted secondary structure of the transit sequence (70 residues; 7.2 kDa) resembles that of the Rieske Fe/S polypeptide, but shows little similarity with those of stromal or luminal proteins. The comparison of the chloroplast delta amino acid sequence with the published delta sequences from respiratory ATP synthases of bacterial and mitochondrial sources and from the thylakoid ATP synthase of the cyanobacterium Synechococcus suggests substantial divergence at the genic level although structural elements appear to be remarkably conserved.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00029882
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  • 3
    Electronic Resource
    Electronic Resource
    Nucleotide sequence of cDNA clones encoding the complete “33 kDa” precursor protein associated with the photosynthetic oxygen-evolving complex from spinach (1987)
    Springer
    Molecular genetics and genomics 207 (1987), S. 288-293 
    Details
    ISSN: 1617-4623
    Keywords: Photosynthetic oxygen evolution ; “33 kDa” protein ; cDNA nucleotide sequence ; Transit peptide ; Spinach
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Several cDNA clones encoding the “33 kDa” protein associated with the photosynthetic water oxidation activity of spinach were sequenced. A 1208 bp insert of one of the clones encodes the entire 331 amino acid residues of the precursor protein including 84 amino acids (8.5 kDa) of the amino-terminal transit peptide, 49 bp of the 5′ and 111 bp of the 3′ untranslated segment of the mRNA. The 3′ poly(A) tail starts 19 bp downstream from a putative polyadenylation signal, TATAAA. The hydrophilic mature protein consists of 247 amino acid residues corresponding to an Mr of 26.5 kDa, which is 6.5 kDa smaller than the value determined by SDS-polyacrylamide gel electrophoresis (33–34 kDa), and shows a certain degree of conservation with the putative Mn-complexing active sites of bacterial Mn-dependent superoxide dismutases. The anatomy of the unusually long transit sequence is discussed with regard to current concepts of protein import into and protein routein within the organelle.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00331591
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  • 4
    Electronic Resource
    Electronic Resource
    The complete amino-acid sequence of the rieske FeS-precursor protein from spinach chloroplasts deduced from cDNA analysis (1987)
    Springer
    Molecular genetics and genomics 210 (1987), S. 171-177 
    Details
    ISSN: 1617-4623
    Keywords: Photosynthesis ; Rieske iron-sulfur precursor protein ; cDNA nucleotide sequence ; Transit peptide ; Spinach
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Summary Several cDNA clones encoding the entire Rieske FeS-precursor protein of the chloroplast cytochrome b 6 f-complex have been isolated by high density plaque immunoscreening of a phage lambda gt11 cDNA expression library, made from poly A+-RNA of spinach seedlings. The identity of the cDNAs has been confirmed by N-terminal amino acid sequencing of the purified protein. The nucleotide sequence indicates a protein of 247 amino acid residues including a putative transit sequence of 68 amino acids corresponding to molecular masses of 26.3 kDa (precursor) and 18.8 kDa (mature protein; 179 amino acid residues). Alignteins of the sequence with sequences from Rieske FeS-proteins of respiratory electron transport chains, two of bacterial and three of mitochondrial origin, shows little sequence homology, but remarkable similarity in secondary structure including a putative N-terminal transmembrane segment of about 25 residues and the peptides CTHLGCV and CPCHGS in the C-terminal region of the protein that are involved in the binding of the Fe2S2-cluster.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00337775
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  • 5
    Electronic Resource
    Electronic Resource
    Cytokinin stimulates and abscisic acid inhibits greening of etiolated Lupinus luteus cotyledons by affecting the expression of the light-sensitive protochlorophyllide oxidoreductase (1998)
    Springer
    Molecular genetics and genomics 259 (1998), S. 21-28 
    Details
    ISSN: 1617-4623
    Keywords: Key words Abscisic acid ; Cytokinin ; Plastid biogenesis ; Protochlorophyllide oxidoreductase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Plastid biogenesis in etiolated lupine (Lupinus luteus L.) cotyledons is highly sensitive to cytokinins and abscisic acid. In the presence of the synthetic cytokinin N6-benzylaminopurine, greening and plastid biogenesis is substantially promoted as compared to untreated controls, whereas abscisic acid has an inhibitory effect. Faster greening in cytokinin-treated cotyledons is accompanied by a higher level and slower degradation of the light-sensitive protochlorophyllide-oxidoreductase (POR); while ABA has the opposite effect. The phytohormones appear to modulate POR gene expression, since the steady-state levels of POR mRNA, as well as transcripts of other nuclear genes for plastid proteins, are strongly increased by cytokinin and reduced by abscisic acid treatment. When etiolated lupine cotyledons were illuminated with far-red light prior to phytohormone application, the POR level substantially decreased; this was accompanied by the loss of the phytohormone's effect on greening. Based on these findings it is concluded that the level of POR and the integrity of the prolamellar body is crucial for cytokinin- and abscisic acid-controlled greening following transfer of etiolated lupine cotyledons into the light.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/PL00008626
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