Difference between revisions of "PMID:4344919"

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'''Friedberg, I'''  (1972) Localization of phosphoglucose isomerase in Escherichia coli and its relation to the induction of the hexose phosphate transport system.''J. Bacteriol.'' '''112''':1201-5
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!align=left  |Abstract
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The localization of phosphoglucose isomerase (PGI) was studied in relation to the induction of hexose phosphate uptake in Escherichia coli. The uptake system is induced only by extracellular glucose-6-phosphate (G6P); there is no induction by intracellular G6P. Fructose-6-phosphate (F6P) is an indirect inducer, and isomerization of F6P to G6P must occur before induction. PGI has been considered to be an internal enzyme; therefore, uptake of F6P by noninduced cells and leakage of the G6P formed would be required for induction. In this study, it was concluded that part of the PGI activity is located in the cell surface because: (i) uninduced, intact cells are able to convert F6P to G6P, whereas the activity of G6P dehydrogenase is not detectable; (ii) when cells are subjected to osmotic shock, about 10% of the PGI activity is found in the shock fluid; and (iii) sorbitol-6-phosphate (S6P) inhibits both PGI activity of whole cells and the induction of hexose phosphate transport system by F6P. S6P was not taken by intact cells. The data indicate that the isomerization of F6P to G6P can take place on the cell surface, and this explains the indirect induction of hexose phosphate transport by F6P.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=4344919 PubMed]
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!align=left  |Keywords
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Biological Transport; Cell Membrane; Enzyme Induction; Escherichia coli; Fructosephosphates; Galactosidases; Glucosephosphate Dehydrogenase; Glucosephosphates; Glyceraldehyde-3-Phosphate Dehydrogenases; Hexosephosphates; Isomerases; Osmosis; Phosphoric Diester Hydrolases; Pyrophosphatases; Spheroplasts
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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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{| border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"  id="C4fa452c16bd03"  class=" tableEdit Phenotype_Table_2" 
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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:
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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: ''pgi''
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*Genotype of Experimental Strain : ''pgi''
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*Reference Condition:
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OMP:0006058
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increased resistance to aminoglycoside
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ECO:0000182
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in vitro culture assay data
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fosfomycin + fructose-6-phosphate resistance
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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]]

Latest revision as of 17:06, 16 June 2014

Citation

Friedberg, I (1972) Localization of phosphoglucose isomerase in Escherichia coli and its relation to the induction of the hexose phosphate transport system.J. Bacteriol. 112:1201-5

Abstract

The localization of phosphoglucose isomerase (PGI) was studied in relation to the induction of hexose phosphate uptake in Escherichia coli. The uptake system is induced only by extracellular glucose-6-phosphate (G6P); there is no induction by intracellular G6P. Fructose-6-phosphate (F6P) is an indirect inducer, and isomerization of F6P to G6P must occur before induction. PGI has been considered to be an internal enzyme; therefore, uptake of F6P by noninduced cells and leakage of the G6P formed would be required for induction. In this study, it was concluded that part of the PGI activity is located in the cell surface because: (i) uninduced, intact cells are able to convert F6P to G6P, whereas the activity of G6P dehydrogenase is not detectable; (ii) when cells are subjected to osmotic shock, about 10% of the PGI activity is found in the shock fluid; and (iii) sorbitol-6-phosphate (S6P) inhibits both PGI activity of whole cells and the induction of hexose phosphate transport system by F6P. S6P was not taken by intact cells. The data indicate that the isomerization of F6P to G6P can take place on the cell surface, and this explains the indirect induction of hexose phosphate transport by F6P.

Links

PubMed

Keywords

Biological Transport; Cell Membrane; Enzyme Induction; Escherichia coli; Fructosephosphates; Galactosidases; Glucosephosphate Dehydrogenase; Glucosephosphates; Glyceraldehyde-3-Phosphate Dehydrogenases; Hexosephosphates; Isomerases; Osmosis; Phosphoric Diester Hydrolases; Pyrophosphatases; Spheroplasts

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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

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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

a mutation or genetic difference within a strain

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

OMP:0006058

increased resistance to aminoglycoside

ECO:0000182

in vitro culture assay data

fosfomycin + fructose-6-phosphate resistance


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Notes

References

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