Abstract
An Escherichia coli heme-requiring, heme-permeable mutant had no detectable 5-aminolevulinate dehydratase or porphobilinogen deaminase activities. The gene which complemented this mutation was cloned to a high-copy-number plasmid, and porphobilinogen deaminase activity was restored to normal levels, but the synthesis of 5-aminolevulinate dehydratase increased 20- to 30-fold. A maxicell procedure confirmed that the gene cloned was hemB.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Alleles
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Chromosome Mapping
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Cloning, Molecular
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Escherichia coli / enzymology
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Escherichia coli / genetics*
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Genes, Bacterial*
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Heme / biosynthesis
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Heme / genetics*
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Hydroxymethylbilane Synthase / biosynthesis
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Hydroxymethylbilane Synthase / genetics
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Mutation
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Plasmids
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Porphobilinogen Synthase / biosynthesis
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Porphobilinogen Synthase / genetics*
Substances
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Heme
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Hydroxymethylbilane Synthase
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Porphobilinogen Synthase