| Autor: |
Opekarová, Miroslava, Robl, Ingrid, Graßl, Renate, Tanner, Widmar |
| Zdroj: |
FEMS Microbiology Letters; May 1999, Vol. 174 Issue: 1 p65-72, 8p |
| Abstrakt: |
To study the effect of sterols on the activity of the eukaryotic plasma membrane transporter, the hexose‐proton symporter HUP1 from the unicellular alga Chlorella kessleriwas expressed in Escherichia coli, a prokaryotic microorganism containing virtually no sterols. Under certain conditions, the recombinant protein was partially active in this prokaryotic organism. The heterologously produced HUP1p was purified from membrane fractions of E. coliand reconstituted in an in vitro system. The presence of ergosterol during solubilization, purification and reconstitution resulted in an increased activity of the reconstituted protein. Its activity, however, was 5–6 times lower as compared to the activity of HUP1p produced in Saccharomyces cerevisiaemembranes and solubilized, purified, and reconstituted under the same conditions as above. |
| Databáze: |
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