Difference between revisions of "PMID:355237"

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{|  id="W4f9f024c7cc12"  class=" tableEdit PMID_info_table" 
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'''Miller, CG and Schwartz, G'''  (1978) Peptidase-deficient mutants of Escherichia coli.''J. Bacteriol.'' '''135''':603-11
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!align=left  |Abstract
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Mutant derivatives of Escherichia coli K-12 deficient in several peptidases have been obtained. Mutants lacking a naphthylamidase, peptidase N, were isolated by screening for colonies unable to hydrolyze L-alanine beta-naphthylamide. Other mutants were isolated using positive selections for resistance to valine peptides. Mutants lacking peptidase A, a broad-specificity aminopeptidase, were obtained by selection for resistance to L-valyl-L-leucine amide. Mutants lacking a dipeptidase, peptidase D, were isolated from a pepN pepA strain by selection for resistance to L-valyl-glycine. Starting with a pepN pepA pepD strain, selection for resistance to L-valyl-glycyl-glycine or several other valine peptides produced mutants deficient in another aminopeptidase, peptidase B. Mutants resistant to L-valyl-L-proline lack peptidase Q, an activity capable of rapid hydrolysis of X-proline dipeptides. Using these selection procedures, a strain (CM89) lacking five different peptidases has been isolated. Although still sensitive to valine, this strain is resistant to a variety of valine di- and tripeptides. The ability of this strain to use peptides as sources of amino acids is much more restricted than that of wild-type E. coli strains. Strains containing only one of the five peptidases missing in CM89 have been constructed by transduction. The peptide utilization profiles of these strains show that each of the five peptidases can function during growth in the catabolism of peptides.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=355237 PubMed]
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!align=left  |Keywords
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Alleles; Aminopeptidases; Escherichia coli; Genes; Mutation; Peptide Hydrolases; Peptides; Transduction, Genetic
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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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!|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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a mutation or genetic difference within a strain
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*Taxon: Escherichia coli
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*Strain: K-12
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*Substrain: CM89
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*NCBI Taxon ID: [http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&id=83333&lvl=3&lin=f&keep=1&srchmode=1&unlock 83333]
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*Genotype of Reference Strain: ''pepQ''
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*Genotype of Experimental Strain : ''pepQ''
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*Reference Condition:
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Resistant to toxic, valine containing peptide
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a mutation or genetic difference within a strain
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*Taxon: Escherichia coli
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*Strain: K-12
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*Substrain: CM89
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*NCBI Taxon ID: [http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&id=83333&lvl=3&lin=f&keep=1&srchmode=1&unlock 83333]
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*Genotype of Reference Strain: ''pepN''
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*Genotype of Experimental Strain : ''pepN''
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*Reference Condition:
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Resistant to toxic, valine containing peptide
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==Notes==
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==References==
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{{RefHelp}}
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<references/>
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[[Category:Publication]] [[Category:Papers referenced in the LaRossa chapter]] [[Category:LaRossa citations that need review]]

Latest revision as of 13:43, 4 May 2012

Citation

Miller, CG and Schwartz, G (1978) Peptidase-deficient mutants of Escherichia coli.J. Bacteriol. 135:603-11

Abstract

Mutant derivatives of Escherichia coli K-12 deficient in several peptidases have been obtained. Mutants lacking a naphthylamidase, peptidase N, were isolated by screening for colonies unable to hydrolyze L-alanine beta-naphthylamide. Other mutants were isolated using positive selections for resistance to valine peptides. Mutants lacking peptidase A, a broad-specificity aminopeptidase, were obtained by selection for resistance to L-valyl-L-leucine amide. Mutants lacking a dipeptidase, peptidase D, were isolated from a pepN pepA strain by selection for resistance to L-valyl-glycine. Starting with a pepN pepA pepD strain, selection for resistance to L-valyl-glycyl-glycine or several other valine peptides produced mutants deficient in another aminopeptidase, peptidase B. Mutants resistant to L-valyl-L-proline lack peptidase Q, an activity capable of rapid hydrolysis of X-proline dipeptides. Using these selection procedures, a strain (CM89) lacking five different peptidases has been isolated. Although still sensitive to valine, this strain is resistant to a variety of valine di- and tripeptides. The ability of this strain to use peptides as sources of amino acids is much more restricted than that of wild-type E. coli strains. Strains containing only one of the five peptidases missing in CM89 have been constructed by transduction. The peptide utilization profiles of these strains show that each of the five peptidases can function during growth in the catabolism of peptides.

Links

PubMed

Keywords

Alleles; Aminopeptidases; Escherichia coli; Genes; Mutation; Peptide Hydrolases; Peptides; Transduction, Genetic

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Main Points of the Paper

Please summarize the main points of the paper.

Materials and Methods Used

Please list the materials and methods used in this paper (strains, plasmids, antibodies, etc).

Phenotype Annotations

See Help:AnnotationTable for details on how to edit this table.
<protect>

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

a mutation or genetic difference within a strain

  • Taxon: Escherichia coli
  • Strain: K-12
  • Substrain: CM89
  • NCBI Taxon ID: 83333
  • Genotype of Reference Strain: pepQ
  • Genotype of Experimental Strain : pepQ
  • Reference Condition:

Resistant to toxic, valine containing peptide

a mutation or genetic difference within a strain

  • Taxon: Escherichia coli
  • Strain: K-12
  • Substrain: CM89
  • NCBI Taxon ID: 83333
  • Genotype of Reference Strain: pepN
  • Genotype of Experimental Strain : pepN
  • Reference Condition:

Resistant to toxic, valine containing peptide


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</protect>

Notes

References

See Help:References for how to manage references in omp dev.

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