In recombinant protein production, is glycosylation of the protein product affected solely by choice of expression host, or does choice of vector (e.g. pUC18/19 {Escherichia coli} vector vs pPICZ A, B, C {yeast} vector) affect glycosylation (wheteher it occours or to what degree)? If I use an E. coli expression vector in yeast, will my resultant protein be glycosylated?
Yes since you are using the vector to express your protein only, while glycosylation happens in the Golgi of the system you are using which is in that case the yeast.
Since the protein glycosylation system is not present in E. coli, the protein will not be glycosylated when expressed in E. coli. If the protein has the correct signals for glycosylation in yeast, AND is expressed in yeast (can E. coli expression vectors be used in yeast?), then it should be glycosylated. The nature of the glycosylation will likely be different than in the native species, if that species is not yeast.
In addition to using an expression host capable of protein glycosylation, your expression construct needs to comprise a secretion/membrane insertion signal sequence to get glycosylated, as glycosylation takes place in the ER and golgi. Cytoplasmically expressed proteins do not get glycosylated.
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