Difference between revisions of "PMID:4920090"

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{|  id="U4d937d0755fed"  class=" tableEdit PMID_info_table" 
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!align=left  |Citation
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'''Ames, GF and Lever, J'''  (1970) Components of histidine transport: histidine-binding proteins and hisP protein.''Proc. Natl. Acad. Sci. U.S.A.'' '''66''':1096-103
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!align=left  |Abstract
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The high-affinity (K(m) = 3 x 10(-8) M) transport system for histidine in Salmonella typhimurium has been resolved into three components: J, K, and P. J, which is a histidine-binding protein released by osmotic shock, is specified by the hisJ gene: hisJ mutants lack the binding protein and are defective in histidine transport. Another class of mutants-dhuA, which is closely linked to hisJ-has five times the normal level of binding protein and has an increased rate of histidine transport. P, which is a protein specified by the hisP gene, is required for J binding protein to be operative in transport. hisP mutants, though defective in transport, have normal levels of J binding protein. K, a third transport component, works in parallel to J, and also requires the P protein in order to be operative in transport. A second histidine-binding protein has been found but its relation to K is unclear. hisJ, dhuA, and hisP have been mapped and are in a cluster (near purF) on the S. typhimurium chromosome.
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!align=left  |Links
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=4920090 PubMed]
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!align=left  |Keywords
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Biological Transport; Chromatography, DEAE-Cellulose; Chromosome Mapping; Histidine; Mutation; Protein Binding; Salmonella typhimurium; Tritium
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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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{|  id="C4d937d0758fd8"  class=" tableEdit PMID_Phenotype_table" 
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!|Species!!Taxon ID!!Strain!!Gene (if known)!!OMP!!Phenotype!!Details!!Evidence!!Notes
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''Salmonella enterica'' spp. Typhimurium
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TA831
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''hisF645''
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no growth on D-histidine
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Growth
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Plating Assay
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Table 1
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''Salmonella enterica'' spp. Typhimurium
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TA831
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''hisF645''
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*increased sensitivity to HIPA
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*decreased resistance to HIPA
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Sensitivity to
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HIPA is an inhibitory histidine analog
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Table 1
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''Salmonella enterica'' spp. Typhimurium
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TA1014
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''dhuA1''
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*increased sensitivity to HIPA
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*decreased resistance to HIPA
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Sensitivity to
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HIPA is an inhibitory histidine analog
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Table 1
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''Salmonella enterica'' spp. Typhimurium
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TA1653
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''hisJ5601''
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*decreased uptake of histidine
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Metabolic Activity
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Lineweaver-Burk plot
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Biochemical Assay
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Figure 2
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''Salmonella enterica'' spp. Typhimurium
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TA1195
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''hisP5503''
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*decreased rate of uptake/transport- histidine
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*decreased rate of histidine uptake/transport
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Metabolic Activity
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Lineweaver-Burk plot
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Biochemical Assay
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Figure 2
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''Salmonella enterica'' spp. Typhimurium
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''hisP1661''
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* decreased rate of uptake/transport- histidine
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* decreased rate of histidine uptake/transport
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Metabolic Activity
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Lineweaver-Burk plot
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Biochemical Assay
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Figure 2
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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]]
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[[Category:To Be Converted]]

Latest revision as of 12:09, 22 June 2011

Citation

Ames, GF and Lever, J (1970) Components of histidine transport: histidine-binding proteins and hisP protein.Proc. Natl. Acad. Sci. U.S.A. 66:1096-103

Abstract

The high-affinity (K(m) = 3 x 10(-8) M) transport system for histidine in Salmonella typhimurium has been resolved into three components: J, K, and P. J, which is a histidine-binding protein released by osmotic shock, is specified by the hisJ gene: hisJ mutants lack the binding protein and are defective in histidine transport. Another class of mutants-dhuA, which is closely linked to hisJ-has five times the normal level of binding protein and has an increased rate of histidine transport. P, which is a protein specified by the hisP gene, is required for J binding protein to be operative in transport. hisP mutants, though defective in transport, have normal levels of J binding protein. K, a third transport component, works in parallel to J, and also requires the P protein in order to be operative in transport. A second histidine-binding protein has been found but its relation to K is unclear. hisJ, dhuA, and hisP have been mapped and are in a cluster (near purF) on the S. typhimurium chromosome.

Links

PubMed

Keywords

Biological Transport; Chromatography, DEAE-Cellulose; Chromosome Mapping; Histidine; Mutation; Protein Binding; Salmonella typhimurium; Tritium

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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>

Species Taxon ID Strain Gene (if known) OMP Phenotype Details Evidence Notes

Salmonella enterica spp. Typhimurium

TA831

hisF645

no growth on D-histidine

Growth

Plating Assay

Table 1

Salmonella enterica spp. Typhimurium

TA831

hisF645

  • increased sensitivity to HIPA
  • decreased resistance to HIPA

Sensitivity to

HIPA is an inhibitory histidine analog

Table 1

Salmonella enterica spp. Typhimurium

TA1014

dhuA1

  • increased sensitivity to HIPA
  • decreased resistance to HIPA

Sensitivity to

HIPA is an inhibitory histidine analog

Table 1

Salmonella enterica spp. Typhimurium

TA1653

hisJ5601

  • decreased uptake of histidine

Metabolic Activity

Lineweaver-Burk plot

Biochemical Assay

Figure 2

Salmonella enterica spp. Typhimurium

TA1195

hisP5503

  • decreased rate of uptake/transport- histidine
  • decreased rate of histidine uptake/transport

Metabolic Activity

Lineweaver-Burk plot

Biochemical Assay

Figure 2

Salmonella enterica spp. Typhimurium

hisP1661

  • decreased rate of uptake/transport- histidine
  • decreased rate of histidine uptake/transport

Metabolic Activity

Lineweaver-Burk plot

Biochemical Assay

Figure 2

edit table

</protect>

Notes

References

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

Retrieved from "http://bcbp-ftq4xm2.biobio.tamu.edu/omp/dev/index.php?title=PMID:4920090&oldid=5233"