The signal sequence of the p62 protein of Semliki Forest virus is involved in initiation but not in completing chain translocation

The glycosylation of the translocated p62-hybrid and its effect on the apparent size of the protein was shown in an experiment where a short peptide (Asn-Leu-Thr), which competes for N-linked glycosylation, was included during translation. Apparently only unglycosylated faster migrating p62-dhfr hybrids were formed in these conditions although chain translocation took place conferring protease resistance (Fig. 2, lanes 5-7) . Additional analyses (lanes 8-10) illustrate that a control peptide (Asn-Leu-aThr) which cannot serve as an acceptor site for N-linked glycosylation, had no effect on the glycosylation of the p62-reporter hybrids when tested in an analogous way.