id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-300796-rmjv56ia	nan	The signal sequence of the p62 protein of Semliki Forest virus is involved in initiation but not in completing chain translocation	1990-09-01		.txt	text/plain	8031	405	57	In this work we show that the p62 protein of Semliki Forest virus contains an uncleaved signal sequence at its NH2-terminus and that this becomes glycosylated early during synthesis and translocation of the p62 polypeptide. As the glycosylation of the signal sequence most likely occurs after its release from the ER membrane our results suggest that this region has no role in completing the transfer process. Furthermore, the p62-reporter hybrid should be translocated across microsomal membranes and possibly glycosylated at Asn~3 of the p62 sequence if the 40 residues long NH2-terminal p62 peptide carries a signal sequence. This must involve Asn~3 of the p62 peptide as it is part of the only potential glycosylation site on the hybrid polypeptides (Garoff et al., 1980 ; references on dhfr sequence in legend to Fig. 1) , Finally, we can also conclude that the p62 signal sequence does not provide a stable membrane anchor to the translocated chain.	./cache/cord-300796-rmjv56ia.txt	./txt/cord-300796-rmjv56ia.txt