Difference between revisions of "PMID:9829935"

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{|  id="Q511bdcee7252d"  class=" tableEdit PMID_info_table" 
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'''Hussein, MJ , Green, JM  and Nichols, BP '''  (1998) Characterization of mutations that allow p-aminobenzoyl-glutamate utilization by Escherichia coli. ''J. Bacteriol.'' '''180''':6260-8
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!align=left  |Abstract
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An Escherichia coli strain deficient in p-aminobenzoate synthesis was mutagenized, and derivatives were selected for growth on folic acid. Supplementation was shown to be due to p-aminobenzoyl-glutamate present as a breakdown product in commercial folic acid preparations. Two classes of mutations characterized by the minimum concentration of p-aminobenzoyl-glutamate that could support growth were obtained. Both classes of mutations were genetically and physically mapped to about 30 min on the E. coli chromosome. A cloned wild-type gene from this region, abgT (formerly ydaH) could confer a similar p-aminobenzoyl-glutamate utilization phenotype on the parental strain. Interruption of abgT on the plasmid or on the chromosome of the mutant strain resulted in a loss of the phenotype. abgT was the third gene in an apparent operon containing abgA, abgB, abgT, and possibly ogt and might be regulated by a divergently transcribed LysR-type regulator encoded by abgR. Two different single-base-pair mutations that gave rise to the p-aminobenzoyl-glutamate utilization phenotype lay in the abgR-abgA intercistronic region and appeared to allow the expression of abgT. The second class of mutation was due to a tandem duplication of abgB and abgT fused to fnr. The abgA and abgB gene products were homologous to one another and to a family of aminoacyl aminohydrolases. p-Aminobenzoyl-glutamate hydrolysis could be detected in extracts from several of the mutant strains, but intact abgA and abgB were not essential for p-aminobenzoyl-glutamate utilization when abgT was supplied in trans.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=9829935 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC107711 PMC107711]
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!align=left  |Keywords
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Amino Acid Sequence; Base Sequence; Chromosome Mapping; Cloning, Molecular; DNA, Bacterial/genetics; Dihydropteroate Synthase/metabolism; Escherichia coli/genetics; Escherichia coli/growth & development; Escherichia coli/metabolism; Folic Acid/metabolism; Gene Duplication; Genes, Bacterial; Glutamates/metabolism; Hydrolysis; Molecular Sequence Data; Mutation; Phenotype
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==Main Points of the Paper ==
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{{LitSignificance}}
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== Materials and Methods Used ==
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{{LitMaterials}}
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==Phenotype Annotations==
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{{AnnotationTableHelp}}
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==Notes==
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==References==
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[[Category:Publication]]

Revision as of 13:35, 13 February 2013

Citation

Hussein, MJ , Green, JM and Nichols, BP (1998) Characterization of mutations that allow p-aminobenzoyl-glutamate utilization by Escherichia coli. J. Bacteriol. 180:6260-8

Abstract

An Escherichia coli strain deficient in p-aminobenzoate synthesis was mutagenized, and derivatives were selected for growth on folic acid. Supplementation was shown to be due to p-aminobenzoyl-glutamate present as a breakdown product in commercial folic acid preparations. Two classes of mutations characterized by the minimum concentration of p-aminobenzoyl-glutamate that could support growth were obtained. Both classes of mutations were genetically and physically mapped to about 30 min on the E. coli chromosome. A cloned wild-type gene from this region, abgT (formerly ydaH) could confer a similar p-aminobenzoyl-glutamate utilization phenotype on the parental strain. Interruption of abgT on the plasmid or on the chromosome of the mutant strain resulted in a loss of the phenotype. abgT was the third gene in an apparent operon containing abgA, abgB, abgT, and possibly ogt and might be regulated by a divergently transcribed LysR-type regulator encoded by abgR. Two different single-base-pair mutations that gave rise to the p-aminobenzoyl-glutamate utilization phenotype lay in the abgR-abgA intercistronic region and appeared to allow the expression of abgT. The second class of mutation was due to a tandem duplication of abgB and abgT fused to fnr. The abgA and abgB gene products were homologous to one another and to a family of aminoacyl aminohydrolases. p-Aminobenzoyl-glutamate hydrolysis could be detected in extracts from several of the mutant strains, but intact abgA and abgB were not essential for p-aminobenzoyl-glutamate utilization when abgT was supplied in trans.

Links

PubMed PMC107711

Keywords

Amino Acid Sequence; Base Sequence; Chromosome Mapping; Cloning, Molecular; DNA, Bacterial/genetics; Dihydropteroate Synthase/metabolism; Escherichia coli/genetics; Escherichia coli/growth & development; Escherichia coli/metabolism; Folic Acid/metabolism; Gene Duplication; Genes, Bacterial; Glutamates/metabolism; Hydrolysis; Molecular Sequence Data; Mutation; Phenotype

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Main Points of the Paper

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Materials and Methods Used

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Phenotype Annotations

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<protect>

Phenotype of Taxon Information Genotype Information (if known) Condition Information OMP ID OMP Term Name ECO ID ECO Term Name Notes Status
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</protect>

Notes

References

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