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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1991-2-20
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pubmed:databankReference |
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pubmed:abstractText |
Ethylmethane sulfonate-induced mutants of several Escherichia coli strains that required delta-aminolevulinic acid (ALA) for growth were isolated by penicillin enrichment or by selection for respiratory-defective strains resistant to the aminoglycoside antibiotic kanamycin. Three classes of mutants were obtained. Two-thirds of the strains were mutants in hemA. Representative of a third of the mutations was the hem-201 mutation. This mutation was mapped to min 8.6 to 8.7. Complementation of the auxotrophic phenotype by wild-type DNA from the corresponding phage 8F10 allowed the isolation of the gene. DNA sequence analysis revealed that the hem-201 gene encoded ALA dehydratase and was similar to a known hemB gene of E. coli. Complementation studies of hem-201 and hemB1 mutant strains with various hem-201 gene subfragments showed that hem-201 and the previously reported hemB1 mutation are in the same gene and that no other gene is required to complement the hem-201 mutant. ALA-forming activity from glutamate could not be detected by in vitro or in vivo assays. Extracts of hem-201 cells had drastically reduced ALA dehydratase levels, while cells transformed with the plasmid-encoded wild-type gene possessed highly elevated enzyme levels. The ALA requirement for growth, the lack of any ALA-forming enzymatic activity, and greatly reduced ALA dehydratase activity of the hem-201 strain suggest that a diffusible product of an enzyme in the heme biosynthetic pathway after ALA formation is involved in positive regulation of ALA biosynthesis. In contrast to the hem-201 mutant, previously isolated hemB mutants were not ALA auxotrophs and had no detectable ALA dehydratase activity.(ABSTRACT TRUNCATED AT 250 WORDS)
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1987138-16662960,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1987138-170364,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1987138-2110138,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1987138-2188943,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1987138-2194094,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1987138-2282139,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1987138-2303495,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1987138-2407234,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1987138-2407729,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1987138-2464127,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1987138-2511063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1987138-2544564,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1987138-2548996,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1987138-2651407,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1987138-2656410,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1987138-2656630,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1987138-2664454,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1987138-2664455,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1987138-271968,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1987138-2789025,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1987138-2900830,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/1987138-3038334,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1987138-3049558,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1987138-3075378,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/1987138-3321068,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/1987138-4860913,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1987138-4877132,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1987138-4882033,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1987138-4911544,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1987138-4965055,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1987138-4999072,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1987138-5338813,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1987138-5340314,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1987138-6262434,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1987138-6295879,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1987138-6376471
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0021-9193
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
173
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pubmed:geneSymbol |
hemA,
hemB
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
94-100
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pubmed:dateRevised |
2010-9-9
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pubmed:meshHeading |
pubmed-meshheading:1987138-Aminolevulinic Acid,
pubmed-meshheading:1987138-Base Sequence,
pubmed-meshheading:1987138-DNA, Bacterial,
pubmed-meshheading:1987138-Escherichia coli,
pubmed-meshheading:1987138-Ethyl Methanesulfonate,
pubmed-meshheading:1987138-Genes, Bacterial,
pubmed-meshheading:1987138-Genetic Complementation Test,
pubmed-meshheading:1987138-Genotype,
pubmed-meshheading:1987138-Molecular Sequence Data,
pubmed-meshheading:1987138-Mutation,
pubmed-meshheading:1987138-Plasmids,
pubmed-meshheading:1987138-Porphobilinogen Synthase,
pubmed-meshheading:1987138-Transduction, Genetic
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pubmed:year |
1991
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pubmed:articleTitle |
delta-Aminolevulinic acid dehydratase deficiency can cause delta-aminolevulinate auxotrophy in Escherichia coli.
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pubmed:affiliation |
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06511.
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