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  • 1
    ISSN: 1432-2242
    Keywords: Arabidopsis thaliana ; Chlorate resistance ; Nitrate reductase deficiency ; Suspension cultures ; M2-seeds
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Cell suspensions of diploid Arabidopsis thaliana were screened for resistance to chlorate on a medium with ammonium nitrate as the nitrogen source, and after plating on filters to increase the plating efficiency. Thirty-nine lines were selected, four of which were still resistant after two years of subculturing on non-selective medium. Of the latter lines three were nitrate reductase deficient but exhibited some residual nitrate reductase activity; the fourth line showed a high level of enzyme activity. Screening M2-seeds for callus production on selective medium with amino acids as the nitrogen source and chlorate revealed resistant calli in 17 out of 483 M2-groups. Nine well-growing lines, all but one (G3) exhibiting no detectable in vivo nitrate reductase activity, were classified as defective in the cofactor. Two lines (G1 and G3) could be analysed genetically at the plant level. Chlorate resistance was monogenic and recessive. Sucrose gradient fractionation of callus extracts of G1 revealed that a complete enzyme molecule can be assembled. Nitrate reductase activity in G1 could partly be restored by excess molybdenum. It is suggested that G1 is disturbed in the catalytic properties of the cofactor. It appeared that G1 is neither allelic with another molybdenum repairable mutant (B73) nor with another cofactor mutant (B25). Wilting of intact G1 plants could be ascribed to non-closing stomata.
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Theoretical and applied genetics 64 (1982), S. 83-90 
    ISSN: 1432-2242
    Keywords: Arabidopsis thaliana ; Mutant ; Chlorateresistance ; Nitrate reductase ; Cytochrome-c reductase ; Xanthine dehydrogenase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Chlorate resistant mutants of Arabidopsis thaliana were isolated, of which 10 exhibited a lowered nitrate reductase activity and 51 were chlorate-resistant because of an impaired uptake of chlorate. The 51 mutants of this type are all affected in the same gene. The mutants with a lowered nitrate reductase activity fall into 7 different complementation groups. Three of these mutants grow poorly on media with nitrate as the sole nitrogen source, while the others apparently can reduce sufficient nitrate to bring about growth. In all cases a low nitrate reductase activity coincides with an enhanced nitrite reductase activity. After sucrose gradient centrifugation of wildtype extracts nitrate reductase is found at the 8S position, whereas cytochrome-c reductase is found both at 4 and 8S positions. It is suggested that the functional nitrate reductase is a complex consisting of 4S subunits showing cytochrome-c reductase activity and a Mo-bearing cofactor. All mutants except B25 are capable of assembling the 4S subunits into complexes which for most mutants have a lower S value and exhibit a lower nitrate reductase activity than the wildtype complexes. Since the mutants B25 and B73 exhibit a low xanthine dehydrogenase activity, the Mo-bearing cofactor is probably less available in these mutants than in the wildtype. B73 appears to be the only mutant which is partly repaired by excessive Mo. The possible role of several genes is discussed.
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Theoretical and applied genetics 61 (1982), S. 263-271 
    ISSN: 1432-2242
    Keywords: Arabidopsis thaliana ; Suppressor ; Nitrate reductase deficient mutant
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Revertants of B25, a nitrate reductase-deficient mutant of Arabidopsis thaliana (L.) Heinh, were isolated with a high frequency. All 7 independently arisen revertants were mutations in the same suppressor gene su, which is unlinked to the originally mutated gene rgn. The mutant character shows up both in growth on nitrate as the sole nitrogen source and in susceptibility to chlorate. When judged for these properties the mutant alleles are either dominant for both, recessive for both or dominant for growth on nitrate and recessive for the effect of chlorate, when compared to the wildtype allele. Whereas the original mutant B25 exhibits no or very little nitrate reductase activity, the activities of the revenants were in the range of 0.4 to 1.5 of the wildtype activity. Physiological characteristics of nitrate reductase from the revertants are the same as those from the wildtype. Probably rgn is not the structural gene for nitrate reductase. The ability to assemble the nitrate reductase complex from its subunits, which was absent in mutant B25, appears to have been restored in the revertants.
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