Expression vector promoting the synthesis and export of the human growth-hormone-releasing factor in Escherichia coli

We have studied the synthesis, processing and export of human growth-hormone-releasing factor (hGRF) in Escherichia coli transformed with a plasmid constructed for the expression of hGRF as a hybrid protein. A DNA fragment containing the entire sequence of phosphate-binding protein gene ( phoS) is f...

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Veröffentlicht in:Gene 1987, Vol.53 (2), p.219-226
Hauptverfasser: Anba, Jamila, Baty, Daniel, Lloubès, Roland, Pagès, Jean-Marie, Joseph-Liauzun, Evelyne, Shire, David, Roskam, Willem, Lazdunski, Claude
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Sprache:eng
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Zusammenfassung:We have studied the synthesis, processing and export of human growth-hormone-releasing factor (hGRF) in Escherichia coli transformed with a plasmid constructed for the expression of hGRF as a hybrid protein. A DNA fragment containing the entire sequence of phosphate-binding protein gene ( phoS) is fused to a modified hGRF-coding sequence ( phoS-mhGRF). The hybrid protein, PhoS-mhGRF, was recovered in the supernatant fluid after spheroplasting treatment indicating correct export to the periplasmic space. Pulse-chase experiments demonstrated that the hybrid protein was similarly processed as the PhoS precursor.
ISSN:0378-1119
1879-0038
DOI:10.1016/0378-1119(87)90010-2