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Carbon and nitrogen metabolism in barley (Hordeum vulgareL.) mutants lacking ferredoxin-dependent glutamate synthase

โœ Scribed by A. C. Kendall; R. M. Wallsgrove; N. P. Hall; J. C. Turner; P. J. Lea


Publisher
Springer-Verlag
Year
1986
Tongue
English
Weight
941 KB
Volume
168
Category
Article
ISSN
0032-0935

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โœฆ Synopsis


Five mutant lines of barley (Hordeum vulgare L.), which are only able to grow at elevated levels of CO2, contain less than 5% of the wildtype activity of ferredoxin-dependent glutamate synthase (EC 1.4.7.1). Two of these lines (RPr 82/1 and RPr 82/9) have been studied in detail. Leaves and roots of both lines contain normal activities of NADH-dependent glutamate synthase (EC 1.4.1.14) and the other enzymes of ammonia assimilation. Under conditions that minimise photorespiration, both mutants fix CO2 at normal rates; on transfer to air, the rates drop rapidly to 15% of the wild-type. Incorporation of 14CO2 into sugar phosphates and glycollate is increased under such conditions, whilst incorporation of radioactivity into serine, glycine, glycerate and sucrose is decreased; continuous exposure to air leads to an accumulation of 14C in malate. The concentrations of malate, glutamine, asparagine and ammonia are all high in air, whilst aspartate, alanine, glutamate, glycine and serine are low, by comparison with the wild-type parent line (cv. Maris Mink), under the same conditions. The metabolism of [~4C]glutamate and [14C]glutamine by leaves of the mutants indicates a very much reduced ability to convert glutamine to glutamate. Genetic analysis has shown that the mutation in RPr 82/9 segregates as a single recessive nuclear gene.


๐Ÿ“œ SIMILAR VOLUMES


Carbon and nitrogen metabolism in a barl
โœ R. M. Wallsgrove; A. C. Kendall; N. P. Hall; J. C. Turner; P. J. Lea ๐Ÿ“‚ Article ๐Ÿ“… 1986 ๐Ÿ› Springer-Verlag ๐ŸŒ English โš– 536 KB

A mutant line, RPr79/2, of barley (Hordeum vulgare L. cv. Maris Mink) has been isolated that has an apparent defect in photorespiratory nitrogen metabolism. The metabolism of 14C-labelled glutamine, glutamate and 2-oxoglutarate indicates that the mutant has a greatly reduced ability to synthesise gl