Secretion into the bacterial periplasmic space of chicken ovalbumin synthesized in Escherichia coli.
Ovalbumin is secreted by the tubular gland cells without cleavage of a signal sequence at the N-terminus. In Escherichia coli strains which produce a chicken ovalbumin-like protein (OLP) from a plasmid-cloned gene, the OLP is synthesized on membrane-bound polysomes and secreted without cleavage into the periplasmic space. In contrast, a deleted protein, which lacks 126 amino acids in the N-terminal half, is not secreted and is synthesized from free polysomes. Our results are compatible with the presence, in the N-terminal half of the molecule, of a signal sequence necessary for the transport across the membrane.
D000818:Animals; D001692:Biological Transport; D002462:Cell Membrane / Q000378:metabolism; D002645:Chickens / Q000235:genetics; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics / Q000648:ultrastructure; D010047:Ovalbumin / Q000235:genetics* / Q000378:metabolism; D010957:Plasmids; D011132:Polyribosomes / Q000378:metabolism
D010047:Ovalbumin