Cloning of the Escherichia coli K-12 hemB gene.
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.
Li
J M
JM
Department of Biochemistry, City College, City University of New York, New York 10031.
Umanoff
H
H
Proenca
R
R
Russell
C S
CS
Cosloy
S D
SD
D000483:Alleles; D002874:Chromosome Mapping; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics*; D005798:Genes, Bacterial; D006418:Heme / Q000096:biosynthesis / Q000235:genetics*; D011163:Hydroxymethylbilane Synthase / Q000096:biosynthesis / Q000235:genetics; D009154:Mutation; D010957:Plasmids; D000623:Porphobilinogen Synthase / Q000096:biosynthesis / Q000235:genetics*
D006418:Heme; D011163:Hydroxymethylbilane Synthase; D000623:Porphobilinogen Synthase