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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 19 (1980), S. 4875-4883 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 20 (1981), S. 5080-5087 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular evolution 30 (1990), S. 26-35 
    ISSN: 1432-1432
    Keywords: Cytosine methylation ; Vascular plants ; Nonvascular plants ; rDNA
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary CpNpG and CpG methylation was surveyed in a range of vascular and nonvascular plants to determine firstly when CpNpG methylation evolved and secondly whether the two methylation systems found in higher plants were likely to be under common or separate control. Although both systems exist in a wide range of vascular plant taxa, the nonvascular plant taxa appear to contain only CpNpG methylation and this in only very limited amounts. The data suggest that both systems may have evolved at the same time and that speciation involved loss of one or the other methylation system or the evolution of differentiation stage-specific control systems.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Photosynthesis research 14 (1987), S. 3-13 
    ISSN: 1573-5079
    Keywords: Arabidopsis thaliana ; photorespiration ; mutant
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Phosphoglycolate phosphatase was partially purified from leaves of Nicotiana rustica using ion exchange and chromatofocusing columns. The native molecular weight of the enzyme was determined to be about 58 kD from Ferguson plots, with a subunit size of about 32 kD. The native enzyme is thus likely to be a dimer. A polyclonal antibody prepared against the LDS denatured enzyme cross reacted with proteins from Nicotiana tabacum, Glycine max, Spinacea oleracea and Arabidopsis thaniana. There was little or no reaction with an Arabidopsis mutant lacking phosphoglycolate phosphatase activity, indicating a much reduced level of phosphoglycolate phosphatase protein in the mutant.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1573-5028
    Keywords: Arabidopsis thaliana ; signal recognition particle ; protein secretion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The first step in the routing of newly synthesized proteins into the secretory pathway is the binding of the nascent signal sequence to the signal recognition particle. The mammalian signal recognition particle is a complex consisting of 6 proteins and a single 7S RNA molecule. Signal recognition particle-like complexes have been described from wheat and maize but none of the protein components have yet been described from any plant species. Here we report the cloning and characterization of an Arabidopsis thaliana gene encoding the 54 kDa protein subunit of the signal recognition particle. This is the first report of a SRP-54 sequence for any plant species and the first genomic sequence for any multicellular organism.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1573-5028
    Keywords: Zea mays ; thiamine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Thiamine or vitamin B-1, is an essential constituent of all cells since it is a cofactor for two enzyme complexes involved in the citric acid cycle, pyruvate dehydrogenase and α-ketoglutarate dehydrogenase. Thiamine is synthesized by plants, but it is a dietary requirement for humans and other animals. The biosynthetic pathway for thiamine in plants has not been well characterized and none of the enzymes involved have been isolated. Here we report the cloning and characterization of two cDNAs representing members of the maize thi1 gene family encoding an enzyme of the thiamine biosynthetic pathway. This assignment was made based on sequence homology to a yeast thiamine biosynthetic gene and by functional complementation of a yeast strain in which the endogenous gene was inactivated. Using immunoblot analysis, the thi1 gene product was found to be located in a plastid membrane fraction. RNA gel blot analysis of various tissues and developmental stages indicated thi1 expression was differentially regulated in a manner consistent with what is known about thiamine synthesis in plants. This is the first report of cDNAs encoding proteins involved in thiamine biosynthesis for any plant species.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Chichester [u.a.] : Wiley-Blackwell
    Developmental Genetics 8 (1987), S. 475-493 
    ISSN: 0192-253X
    Keywords: methylation ; Adh1 ; Zea ; Arabidopsis ; transformed DNA ; CpG-rich islands ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Higher plant DNA is extensively methylated, but the two methylated sequences (CpG and CpNpG) show different characteristics. Using sequence analysis techniques, we demonstrate that while CpG methylation follows the existing models for cytosine methylation in animals, CpNpG methylation does not. Although there is evidence to support the suggestion that the low CpG frequency has arisen from deaminational conversion of 5-methylcytosine to thymidine, there appears to be no comparable conversion of 5-methylcytosine in the CpNpG configuration. It therefore appears that between the evolution of CpG and CpNpG cytosine methylation systems, a mechanism evolved for the correction of C→T conversion, probably using the methylated strand to direct the repair in the correct direction.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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