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 == | ||
| + | {{LitSignificance}} | ||
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| + | == Materials and Methods Used == | ||
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| + | ==Phenotype Annotations== | ||
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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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| + | ==Notes== | ||
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| + | ==References== | ||
| + | {{RefHelp}} | ||
| + | <references/> | ||
Revision as of 13:57, 30 March 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 | |
| Keywords |
Biological Transport; Chromatography, DEAE-Cellulose; Chromosome Mapping; Histidine; Mutation; Protein Binding; Salmonella typhimurium; Tritium |
| edit table |
Main Points of the Paper
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Materials and Methods Used
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Phenotype Annotations
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| Species | Taxon ID | Strain | Gene (if known) | OMP | Phenotype | Details | Evidence | Notes |
|---|---|---|---|---|---|---|---|---|
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Notes
References
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