Biological nitrogen fixation: primary structure of the Rhizobium trifolii iron protein gene.
Biological nitrogen fixation in the Rhizobium-legume symbiosis is dependent on the induction of a bacterially-encoded enzyme complex, nitrogenase. To examine the organization and expression of the genes encoding the components of nitrogenase in this complex system, these genes have been isolated from the legume symbiont Rhizobium trifolii by molecular cloning. DNA sequence analysis of the entire nifH gene (encoding the Fe-protein component of nitrogenase) and of the amino-terminal 141 codons of the nifD gene (encoding the alpha-subunit of the Mo-Fe protein) indicates that these genes are linked on a single operon in this strain. The Fe-protein amino acid sequence shares considerable homology with the sequence from other organisms, in particular the related organism Rhizobium meliloti (90% homology). The nif structural genes are preceded by a DNA sequence which is repeated at least three times in the Rhizobium trifolii genome.
D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D004262:DNA Restriction Enzymes; D005288:Ferredoxins / Q000235:genetics*; D005796:Genes; D008667:Metalloproteins / Q000235:genetics*; D008983:Molybdoferredoxin / Q000235:genetics*; D009586:Nitrogen Fixation; D009591:Nitrogenase / Q000235:genetics; D019159:Nonheme Iron Proteins; D009693:Nucleic Acid Hybridization; D010957:Plasmids; D012231:Rhizobium / Q000235:genetics*
D005288:Ferredoxins; D008667:Metalloproteins; D008983:Molybdoferredoxin; D019159:Nonheme Iron Proteins; D009591:Nitrogenase; D004262:DNA Restriction Enzymes