Periplasmic secretion of native ovalbumin without signal cleavage in Escherichia coli.
In Escherichia coli cells carrying wild-type ovalbumin cDNA, some of the recombinant protein was secreted into the periplasmic space. In contrast, a signal-region mutant form of ovalbumin (deletion, Gly1 to Ala39) was not detected in the periplasm despite being synthesized at the same level as the wild-type protein. Chemical and spectroscopic analyses showed that periplasmic ovalbumin assumes a conformation indistinguishable from that of native egg white ovalbumin. We concluded that a process resembling the secretion of ovalbumin process in the oviduct occurs also in bacteria.
Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Uji, Kyoto 611-0011, Japan.
Yasuhiro
Y
Arii
Nobuyuki
N
Takahashi
Masaaki
M
Hirose
D002942:Circular Dichroism; D018076:DNA, Complementary / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D017353:Gene Deletion; D010047:Ovalbumin / Q000235:genetics* / Q000378:metabolism*; D019897:Periplasm / Q000378:metabolism*; D021382:Protein Sorting Signals; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D013050:Spectrometry, Fluorescence; D014364:Tryptophan / Q000737:chemistry
D018076:DNA, Complementary; D021382:Protein Sorting Signals; D011994:Recombinant Proteins; D014364:Tryptophan; D010047:Ovalbumin