Phenotypic reversion of nitrogenase in pleiotropic mutants of Rhizobium meliloti.
In two out of three pleiotropic mutants of Rhizobium meliloti, defective in nitrate reductase induced by amino acid utilization in vegetative bacteria and in symbiotic nitrogen fixation, nitrogenase activity could be restored completely by purines and partially by the amino acids L-glutamate, L-aspartate, L-glutamine, and L-asparagine. The compounds restoring effectiveness in nitrogen fixation did not restore nitrate reductase activity in vegetative bacteria. The restoration of effectiveness supports our earlier conclusion that the mutation is not in the structural gene for a suggested common subunit of nitrogenase and nitrate reductase.
D000596:Amino Acids / Q000494:pharmacology; D009154:Mutation; D009565:Nitrate Reductases / Q000378:metabolism; D009586:Nitrogen Fixation; D009591:Nitrogenase / Q000235:genetics / Q000378:metabolism*; D010641:Phenotype; D011687:Purines / Q000494:pharmacology; D012231:Rhizobium / Q000201:enzymology* / Q000235:genetics; D012988:Soil Microbiology; D013559:Symbiosis
D000596:Amino Acids; D011687:Purines; D009591:Nitrogenase; D009565:Nitrate Reductases