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  • Articles  (17)
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  • Articles  (17)
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  • 11
    Electronic Resource
    Electronic Resource
    Plastid genes and parasitic plants (1991)
    [s.l.] : Nature Publishing Group
    Nature 350 (1991), S. 664-664 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] SIR - Howe and Smith! have provided one explanation for the retention of a plastid genome in achlorophyllous Epifagus virgi-niana, as reported by dePamphilis and Palmer2. But porphyrin biosynthesis is not the only significant metabolic activity restricted to plastids; the biosynthetic pathways for ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/350664a0
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  • 12
    Electronic Resource
    Electronic Resource
    Molecular analysis of barley mutants deficient in chloroplast glutamine synthetase (1990)
    Springer
    Plant molecular biology 14 (1990), S. 297-311 
    Details
    ISSN: 1573-5028
    Keywords: cDNA sequence ; chloroplast protein ; glutamine synthetase ; Hordeum vulgare L. ; mRNA ; mutants
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A barley leaf cDNA library has been screened with two oligonucleotide probes designed to hybridize to conserved sequences in glutamine synthetase (GS) genes from higher plants. Two GS cDNA clones were identified as hybridizing strongly to one or both probes. The larger clone (pcHvGS6) contained a 1.6 kb insert which was shown by primer extension analysis to be an almost full-length cDNA. Both clones were more closely related to cDNAs for the chloroplast form of GS (GS2) from pea and Phaseolus vulgaris than to cDNAs for the cytosolic form (GS1). A sequence identicalto an N-terminal sequence determined from a purified preparation of the mature GS2 polypeptide (NH2-XLGPETTGVIQRMQQ) was found in the pcHvGS6-encoded polypeptide at residues 46–61, indicating a pre-sequence of at least 45 amino acids. The pre-sequence has only limited sequence homology to the pre-sequences of pea and P. vulgaris GS2 subunits, but is similarly rich in basic residues and possesses some of the structural features common to the targeting sequences of other chloroplast proteins. The molecular lesions responsible for the GS2-deficient phenotypes of eight photorespiratory mutants of barley were investigated using a gene-specific probe from pcHvGS6 to assay for GS2 mRNA, and an anti-GS antiserum to assay for GS2 protein. Three classes of mutants were identified: class I, in which absence of cross-reacting material was correlated with low or undetectable levels of GS2 mRNA; class II, which had normal or increased levels of GS2 mRNA but very little GS2 protein; and class III, which had significant amounts of GS2 protein but little or no GS2 activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00028767
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  • 13
    Electronic Resource
    Electronic Resource
    The development of NAD(P)H-dependent and ferredoxin-dependent glutamate synthase in greening barley and pea leaves (1982)
    Springer
    Planta 154 (1982), S. 473-476 
    Details
    ISSN: 1432-2048
    Keywords: Ferredoxin ; Glutamate synthase ; Greening (leaves) ; Hordeum ; Pisum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The activity of NAD(P)H-dependent glutamate synthase (E.C. 1.4.1.14) has been demonstrated in extracts from etiolated shoots of pea (Pisum sativum L.) and barley (Hordeum vulgare L.). This activity does not significantly alter upon greening of the etiolated shoots, and is at a similar level in light-grown material. Ferredoxin-dependent glutamate synthase (E.C. 1.4.7.1) has low activity in etiolated shoots but increases rapidly on greening. In light grown leaves ferredoxin-dependent activity is 30–40-fold higher than NAD(P)H-dependent activity. It is not considered that the NAD(P)H-dependent glutamate synthase plays an important role in ammonia assimilation in the photosynthetic tissue of higher plants.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01267816
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  • 14
    Electronic Resource
    Electronic Resource
    Cloning and sequence analysis of a cDNA for barley ferredoxin-dependent glutamate synthase and molecular analysis of photorespiratory mutants deficient in the enzyme (1993)
    Springer
    Planta 189 (1993), S. 475-483 
    Details
    ISSN: 1432-2048
    Keywords: Amidotransferase ; Amino-terminal sequences ; Chromosomal assignment ; Glutamate synthase ; Hordeum (mutants) ; Photorespiration mutants (barley) ; Polymerase chain reaction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The NH2-terminal sequences of ferredoxin-dependent glutamate synthase (Fd-GOGAT; EC 1.4.7.1) purified from barley (Hordeum vulgare L.) and Chlamydomonas reinhardtii (Dangeard), and of a barley peptide, were determined and the barley sequences were used to design oligonucleotide primers for the polymerase chain reaction. A specific 1.3-kilobase (kb) cDNA fragment specifying the NH2-terminal one-third of the mature barley polypeptide, was amplified, cloned and sequenced. The NH2-terminus of plant Fd-GOGAT is highly conserved and homologous to the NH2-terminus of the heavy subunit of Escherichia coli NADPH-GOGAT. Based on sequence homologies, we tentatively identified the NH2-terminal region of Fd-GOGAT as the glutamine-amidotransferase domain, which is related to the corresponding domain of the purF-type amidotransferases. The Fd-GOGAT cDNA clone, and polyclonal antibodies raised against the barley enzyme, were used to analyse four Fd-GOGAT-deficient photorespiratory mutants. Three mutants (RPr 82/1, RPr 82/9 and RPr 84/82) had no detectable Fd-GOGAT protein in leaves, while the fourth (RPr 84/42) had a small amount of cross-reacting material. Hybridization to Northern blots of total leaf RNA revealed that both RPr 82/9 and RPr 84/82 were indistinguishable from the parental line (Maris Mink), having normal amounts of a 5.7-kb mRNA species. On the other hand, RPr 82/2 and RPr 84/42 each contained two distinct hybridizing RNA species, one of which was larger than 5.7 kb, the other smaller. Using a set of wheat-barley telosomic addition lines we have assigned the Fd-GOGAT structural locus to the short arm of chromosome 2.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00198209
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  • 15
    Electronic Resource
    Electronic Resource
    Biochemical characterisation of Nicotiana plumbaginifolia auxotrophs that require branched-chain amino acids (1986)
    Springer
    Plant cell reports 5 (1986), S. 223-226 
    Details
    ISSN: 1432-203X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The biochemical lesions in six amino acid-requiring auxotrophic lines of Nicotiana plumbaginifolia have been investigated, by means of feeding experiments with [14C] and unlabelled substrates, and enzyme analysis. Three of the lines require isoleucine for growth, are unable to synthesise 2-oxobutyrate in vivo and have no detectable threonine dehydratase (E.C.4.2.1.16) in vitro. The other three lines require (isoleucine + valine), accumulate [14C] dihydroxymethylvalerate when fed [14C]-L-threonine, and contain no detectable dihydroxyacid dehydratase (E.C.4.2.1.9).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00269125
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  • 16
    Electronic Resource
    Electronic Resource
    The value of mutants unable to carry out photorespiration (1988)
    Springer
    Photosynthesis research 16 (1988), S. 155-176 
    Details
    ISSN: 1573-5079
    Keywords: Hordeum ; mutants ; nitrogen metabolism ; photosynthesis ; photorespiration ; Pisum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Manipulation of the CO2 concentration of the atmosphere allows the selection of photorespiratory mutants from populations of seeds treated with powerful mutagens such as sodium azide. So far, barley lines deficient in activity of phosphoglycolate phosphatase, catalase, the glycine to serine conversion, glutamine synthetase, glutamate synthase, 2-oxoglutarate uptake and serine: glyoxylate aminotransferase have been isolated. In addition one line of pea lacking glutamate synthase activity and one barley line containing reduced levels of Rubisco are available. The characteristics of these mutations are described and compared with similar mutants isolated from populations of Arabidopsis. As yet, no mutant lacking glutamine synthetase activity has been isolated from Arabidopsis and possible reasons for this difference between barley and Arabidopsis are discussed. The value of these mutant plants in the elucidation of the mechanism of photorespiration and its relationships with CO2 fixation and amino acid metabolism are highlighted.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00039491
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  • 17
    Electronic Resource
    Electronic Resource
    Characteristics of a photorespiratory mutant of barley (Hordeum vulgare L.) deficient in phosphogly collate phosphatase (1987)
    Springer
    Photosynthesis research 11 (1987), S. 89-96 
    Details
    ISSN: 1573-5079
    Keywords: photosynthesis ; photorespiration ; barley ; mutants ; phosphoglycollate ; phosphatase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A barley mutant RPr84/90 has been isolated by selecting for plants which grow poorly in natural air, but normally in air enriched to 0.8% CO2. After 5 minutes of photosynthesis in air containing14CO2 this mutant incorporated 26% of the14C carbon into phosphoglycollate, a compound not normally labelled in wild type (cv. Maris Mink) leaves. The activity of phosphoglycollate phosphatase (EC 3.1.1.18) was 1.2 nkat mg−1 protein at 30°C in RPr 84/90 compared to 19.2 nkat mg−1 protein in the wild-type leaves. Phosphoglycollate phosphatase activity was not detected after protein separation by electrophoresis of leaf extracts from the mutant on polyacrylamide gels; on linear 5% acrylamide gels three bands with enzyme activity were separated from extracts of wild type plants. Gradient gel electrophoresis followed by activity staining showed two bands in Maris Mink tracks of MW 86,000 and 96,000, but no bands in 84/90. This is the first report of isozymes of phosphoglycollate phosphatase in barley which were absent in the mutant extracts. Our results confirm an earlier report of isozymes of this phosphatase in Phaseolus vulgaris [18]. The photosynthetic rate of RPr 84/90 in 1% O2, 350 μl CO2 l−1 was 9–12 mg CO2 dm−2 h−1 at 20°C, whereas the wild-type rate was 27–29 mg CO2 dm−2 h−1 at 20°C. In 21% O2, 350 μl CO2 l−1 the rate was 2–3 mg CO2 dm−2 h−1 in the mutant and 20 mg CO2 dm−2 h−1 in the wild type. Genetic analysis has shown that the mutation segregates as a single recessive nuclear gene.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00117676
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