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 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.
Anba
J
J
Baty
D
D
Lloubès
R
R
Pagès
J M
JM
Joseph-Liauzun
E
E
Shire
D
D
Roskam
W
W
Lazdunski
C
C
D001426:Bacterial Proteins / Q000235:genetics; D001692:Biological Transport; D002352:Carrier Proteins / Q000235:genetics; D003488:Cyanogen Bromide; D004926:Escherichia coli; D005822:Genetic Vectors; D013006:Growth Hormone / Q000235:genetics*; D006801:Humans; D008715:Methionine; D008970:Molecular Weight; D028044:Phosphate-Binding Proteins; D011401:Promoter Regions, Genetic; D011499:Protein Processing, Post-Translational; D011993:Recombinant Fusion Proteins
D001426:Bacterial Proteins; D002352:Carrier Proteins; D028044:Phosphate-Binding Proteins; D011993:Recombinant Fusion Proteins; D013006:Growth Hormone; D008715:Methionine; D003488:Cyanogen Bromide