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  • 1
    Electronic Resource
    Electronic Resource
    Components of chlorophyll biosynthesis in a barley albina mutant unable to synthesize δ-aminolevulinic acid by utilizing the transfer RNA for glutamic acid (1992)
    Springer
    Planta 188 (1992), S. 19-27 
    Details
    ISSN: 1432-2048
    Keywords: Hordeum (chlorophyll biosynthesis) ; Chlorophyll biosynthesis ; Gene regulation ; Mutant (barley) ; Protochlorophyllide oxidoreductase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Components of chlorophyll biosynthesis were investigated in the plastid-ribosome-deficient albostrians mutant of barley (Hordeum vulgare L.). Compared with green leaves, white leaves lacked chloroplast tRNAGlu and 16S ribosomal RNA, but contained a much higher level of the mRNA for glutamate 1-semialdehyde aminotransferase. Substantial amounts of protochlorophyllide were accumulated when the mutant was incubated in a solution of δ-aminolevulinic acid. The level of protochlorophyllide oxidoreductase mRNA (PCOR, EC 1.6.99.1.) in etiolated albostrians plants reached only about 50% of the level in wild-type plants. In addition the content of PCOR protein and the activity of chlorophyll synthetase were distinctly lower than in the wild-type. Mutant and wild-type barley seedlings which were grown under a daily light/dark regime and were therefore nonetiolated both possessed PCOR mRNA. The data presented may help explain the albino phenotype of this mutant. The results are discussed in relation to biosynthesis of tetrapyrrols in higher plants, regulation of chlorophyll biosynthesis and the action of a plastidderived signal involved in the expression of certain nuclear genes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00198935
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Investigations on the apoprotein of phycocyanin from Cyanidium caldarium (1983)
    Springer
    Archives of microbiology 135 (1983), S. 30-35 
    Details
    ISSN: 1432-072X
    Keywords: Rhodophyta ; Cyanidium caldarium ; Biliprotein ; Levulinic acid ; δ-aminolevulinic acid incorporation ; Phycocyanin apoprotein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Cultures of the unicellular red alga Cyanidium caldarium were transferred from heterotrophic growth conditions to photoautotrophic growth. During photoautotrophic growth, the biliprotein phycocyanin is synthesized de novo. In the presence of 2–5 mM/l levulinic acid which inhibits the biosynthesis of tetrapyrrole chromophores, phycocyanin biosynthesis is suppressed by a factor of 29. Immunoprecipitation yields small amounts of “apoprotein” i.e. phycocyanin which lacks all or part of its chromophore(s). In various experiments the ratio apoprotein/residual holoprotein (phycocyanin) was determined as 2–6 to one. Incubation with [3H]leucine leads to labelled immunoprecitable material: apoprotein (18,300–19,600 Mr) and larger poly-peptides (50,000–52,000 Mr) of unknown nature. The apoprotein was separated from residual phycocyanin by chromatography on DEAE-cellulose and preparative isoelectric focusing (IEF). The significance of the results for further studies on the last steps of phycocyanin biosynthesis is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00419478
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Components of chlorophyll biosynthesis in a barley albina mutant unable to synthesize δ-aminolevulinic acid by utilizing the transfer RNA for glutamic acid (1992)
    Springer
    Planta 188 (1992), S. 19-27 
    Details
    ISSN: 1432-2048
    Keywords: Hordeum (chlorophyll biosynthesis) ; Chlorophyll biosynthesis ; Gene regulation ; Mutant (barley) ; Protochlorophyllide oxidoreductase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Components of chlorophyll biosynthesis were investigated in the plastid-ribosome-deficientalbostrians mutant of barley (Hordeum vulgare L.). Compared with green leaves, white leaves lacked chloroplast tRNAGlu and 16S ribosomal RNA, but contained a much higher level of the mRNA for glutamate 1-semialdehyde aminotransferase. Substantial amounts of protochlorophyllide were accumulated when the mutant was incubated in a solution of δ-aminolevulinic acid. The level of protochlorophyllide oxidoreductase mRNA (PCOR, EC 1.6.99.1.) in etiolatedalbostrians plants reached only about 50% of the level in wild-type plants. In addition the content of PCOR protein and the activity of chlorophyll synthetase were distinctly lower than in the wild-type. Mutant and wild-type barley seedlings which were grown under a daily light/dark regime and were therefore nonetiolated both possessed PCOR mRNA. The data presented may help explain the albino phenotype of this mutant. The results are discussed in relation to biosynthesis of tetrapyrrols in higher plants, regulation of chlorophyll biosynthesis and the action of a plastidderived signal involved in the expression of certain nuclear genes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01160708
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
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