Pult, Frauke ; Fallah, Ghada ; Braam, Ursula ; Detro-Dassen, Silvia ; Niculescu, Cristina ; Laube, Bodo ; Schmalzing, Günther (2011)
Robust post-translocational N-glycosylation at the extreme C-terminus of membrane and secreted proteins in Xenopus laevis oocytes and HEK293 cells.
In: Glycobiology, 21 (9)
Artikel, Bibliographie
Kurzbeschreibung (Abstract)
N-glycosylation is normally a co-translational process that occurs as soon as a nascent and unfolded polypeptide chain has emerged approximately 12 residues into the lumen of the endoplasmic reticulum (ER). Here, we describe the efficient utilisation of an N-glycosylation site engineered within the luminal extreme C-terminal residues of distinct integral membrane glycoproteins, a native ER resident protein, and an engineered secreted protein. This N-glycan addition required that the acceptor asparagine within an Asn-Trp-Ser sequon be located at least four residues away from the C-terminus of the polypeptide and, in the case of membrane proteins, at least 13 residues away from the lumenal side of the transmembrane segment. Pulse-chase assays revealed that the natural N-glycans of the proteins studied were attached co-translationally, whereas C-terminal N-glycosylation occurred post-translocationally within a time frame of hours in Xenopus laevis oocytes and minutes in HEK293 cells. In oocyte and HEK cell expression systems, affinity tag-driven C-terminal N-glycosylation may facilitate the determination of orientation of the C-terminal tail of membrane proteins relative to the membrane.
| Typ des Eintrags: | Artikel |
|---|---|
| Erschienen: | 2011 |
| Autor(en): | Pult, Frauke ; Fallah, Ghada ; Braam, Ursula ; Detro-Dassen, Silvia ; Niculescu, Cristina ; Laube, Bodo ; Schmalzing, Günther |
| Art des Eintrags: | Bibliographie |
| Titel: | Robust post-translocational N-glycosylation at the extreme C-terminus of membrane and secreted proteins in Xenopus laevis oocytes and HEK293 cells. |
| Sprache: | Englisch |
| Publikationsjahr: | 2011 |
| Titel der Zeitschrift, Zeitung oder Schriftenreihe: | Glycobiology |
| Jahrgang/Volume einer Zeitschrift: | 21 |
| (Heft-)Nummer: | 9 |
| Kurzbeschreibung (Abstract): | N-glycosylation is normally a co-translational process that occurs as soon as a nascent and unfolded polypeptide chain has emerged approximately 12 residues into the lumen of the endoplasmic reticulum (ER). Here, we describe the efficient utilisation of an N-glycosylation site engineered within the luminal extreme C-terminal residues of distinct integral membrane glycoproteins, a native ER resident protein, and an engineered secreted protein. This N-glycan addition required that the acceptor asparagine within an Asn-Trp-Ser sequon be located at least four residues away from the C-terminus of the polypeptide and, in the case of membrane proteins, at least 13 residues away from the lumenal side of the transmembrane segment. Pulse-chase assays revealed that the natural N-glycans of the proteins studied were attached co-translationally, whereas C-terminal N-glycosylation occurred post-translocationally within a time frame of hours in Xenopus laevis oocytes and minutes in HEK293 cells. In oocyte and HEK cell expression systems, affinity tag-driven C-terminal N-glycosylation may facilitate the determination of orientation of the C-terminal tail of membrane proteins relative to the membrane. |
| Fachbereich(e)/-gebiet(e): | 10 Fachbereich Biologie 10 Fachbereich Biologie > Neurophysiologie und neurosensorische Systeme ?? fb10_zoologie ?? |
| Hinterlegungsdatum: | 11 Apr 2011 09:08 |
| Letzte Änderung: | 05 Mär 2019 06:48 |
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