Biochemical and genetic comparison of two nitrate reductase-deficient pea mutants disturbed in the cofactor.
Two nitrate reductase (NaR)-deficient mutants of pea (Pisum sativum L.), E1 and A300, both disturbed in the molybdenum cofactor function and isolated, respectively, from cv Rondo and cv Juneau, were tested for allelism and were compared in biochemical and growth characteristics. The F1 plants of the cross E1 X A300 possessed NaR and xanthine dehydrogenase (XDH) activities comparable to those of the wild types, indicating that these mutants belong to different complementation groups, representing two different loci. Therefore, mutant E1 represents, besides mutant A300 and the allelic mutants A317 and A334, a third locus governing NaR and is assigned the gene destignation nar 3. In comparison with the wild types, cytochrome c reductase activity was increased in both mutants. The mutants had different cytochrome c reductase distribution patterns, indicating that mutant A300 could be disturbed in the ability to dimerize NaR apoprotein monomers, and mutant E1 in the catalytic function of the molybdenum cofactor. In growth characteristics studied, A300 did not differ from the wild types, whereas fully grown leaves of mutant E1 became necrotic in soil and in liquid media containing nitrate.
Jacobsen
E
E
Schaart
J G
JG
Warner
R L
RL
D003067:Coenzymes; D007887:Fabaceae / Q000235:genetics*; D008667:Metalloproteins / Q000172:deficiency*; D000090006:Molybdenum Cofactors; D009154:Mutation; D009245:NADH Dehydrogenase / Q000378:metabolism; D050901:Nitrate Reductase; D009565:Nitrate Reductases / Q000172:deficiency*; D010946:Plants, Medicinal; D011621:Pteridines / Q000172:deficiency*; D014968:Xanthine Dehydrogenase / Q000378:metabolism
D003067:Coenzymes; D008667:Metalloproteins; D000090006:Molybdenum Cofactors; D009245:NADH Dehydrogenase; D050901:Nitrate Reductase; D009565:Nitrate Reductases; D011621:Pteridines; D014968:Xanthine Dehydrogenase; C022261:molybdopterin