Plant delta-aminolevulinic acid dehydratase. Expression in soybean root nodules and evidence for a bacterial lineage of the Alad gene.
We isolated a soybean (Glycine max) cDNA encoding the heme and chlorophyll synthesis enzyme delta-aminolevulinic acid (ALA) dehydratase by functional complementation of an Escherichia coli hemB mutant, and we designated the gene Alad. ALA dehydratase was strongly expressed in nodules but not in uninfected roots, although Alad mRNA was only 2- to 3-fold greater in the symbiotic tissue. Light was not essential for expression of Alad in leaves of dark-grown etiolated plantlets as discerned by mRNA, protein, and enzyme activity levels; hence, its expression in subterranean nodules was not unique in that regard. The data show that soybean can metabolize the ALA it synthesizes in nodules, which argues in favor of tetrapyrrole formation by the plant host in that organ. Molecular phylogenetic analysis of ALA dehydratases from 11 organisms indicated that plant and bacterial enzymes have a common lineage not shared by animals and yeast. We suggest that plant ALA dehydratase is descended from the bacterial endosymbiont ancestor of chloroplasts and that the Alad gene was transferred to the nucleus during plant evolution.
Department of Biochemistry, State University of New York at Buffalo 14214.
C M
CM
Kaczor
M W
MW
Smith
I
I
Sangwan
M R
MR
O'Brian
D000595:Amino Acid Sequence; D000818:Animals; D001419:Bacteria / Q000201:enzymology / Q000235:genetics; D001483:Base Sequence; D015342:DNA Probes; D005798:Genes, Bacterial; D017343:Genes, Plant; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D010802:Phylogeny; D010944:Plants / Q000201:enzymology / Q000235:genetics; D000623:Porphobilinogen Synthase / Q000096:biosynthesis / Q000235:genetics*; D012333:RNA, Messenger / Q000096:biosynthesis / Q000378:metabolism; D013025:Glycine max / Q000201:enzymology* / Q000235:genetics*
D015342:DNA Probes; D012333:RNA, Messenger; D000623:Porphobilinogen Synthase