Inducible System for the Utilization of β-Glucosides in <i>Escherichia coli</i> I. Active Transport and Utilization of β-Glucosides
-
- S. Schaefler
- Department of Microbiology, New York University Medical Center, New York, New York
書誌事項
- 公開日
- 1967-01
- 権利情報
-
- https://journals.asm.org/non-commercial-tdm-license
- DOI
-
- 10.1128/jb.93.1.254-263.1967
- 公開者
- American Society for Microbiology
この論文をさがす
説明
<jats:p> Wild-type <jats:italic>Escherichia coli</jats:italic> strains (β- <jats:italic>gl</jats:italic> <jats:sup>−</jats:sup> ) do not split β-glucosides, but inducible mutants (β- <jats:italic>gl</jats:italic> <jats:sup>+</jats:sup> ) can be isolated which do so. This inducible system consists of a β-glucoside permease and an aryl β-glucoside splitting enzyme. Both can be induced by aryl and alkyl β-glucosides. In β- <jats:italic>gl</jats:italic> <jats:sup>−</jats:sup> and noninduced β- <jats:italic>gl</jats:italic> <jats:sup>+</jats:sup> cells, C <jats:sup>14</jats:sup> -labeled thioethyl β-glucoside (TEG) is taken up by a constitutive permease, apparently identical with a glucose permease (GP). This permease has a high affinity for α-methyl glucoside and a low affinity for aryl β-glucosides. No accumulation of TEG occurs in a β- <jats:italic>gl</jats:italic> <jats:sup>−</jats:sup> strain lacking glucose permease (GP <jats:sup>−</jats:sup> ). In induced β- <jats:italic>gl</jats:italic> <jats:sup>+</jats:sup> strains, there appears a second β-glucoside permease with low affinity for α-methyl glucoside and high affinity for aryl β-glucosides. Autoradiography shows that TEG is accumulated by the β-glucoside permease and glucose permease in two different forms (one being identical with TEG, the other probably phosphorylated TEG). In GP <jats:sup>+</jats:sup> β- <jats:italic>gl</jats:italic> <jats:sup>+</jats:sup> strains with high GP activity, alkyl β-glucosides induce the enzyme and the β-glucoside permease after a prolonged induction lag, and they competitively inhibit the induction by aryl β-glucosides. The induction lag and competition do not exist in GP <jats:sup>−</jats:sup> β- <jats:italic>gl</jats:italic> <jats:sup>+</jats:sup> strains. It is assumed that phosphorylated alkyl and thioalkyl β-glucosides inhibit the induction, and that this inhibition is responsible for the induction lag. </jats:p>
収録刊行物
-
- Journal of Bacteriology
-
Journal of Bacteriology 93 (1), 254-263, 1967-01
American Society for Microbiology