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doi:10.22028/D291-31223
Titel: | The N-terminus of Sec61p plays key roles in ER protein import and ERAD |
VerfasserIn: | Elia, Francesco Yadhanapudi, Lalitha Tretter, Thomas Römisch, Karin |
Sprache: | Englisch |
Titel: | PLOS ONE |
Bandnummer: | 14 |
Heft: | 4 |
Verlag/Plattform: | PLOS |
Erscheinungsjahr: | 2019 |
DDC-Sachgruppe: | 500 Naturwissenschaften |
Dokumenttyp: | Journalartikel / Zeitschriftenartikel |
Abstract: | Sec61p is the channel-forming subunit of the heterotrimeric Sec61 complex that mediates co-translational protein import into the endoplasmic reticulum (ER). In yeast, proteins can also be post-translationally translocated by the hetero-heptameric Sec complex, composed of the Sec61 and the Sec63 complexes. The Sec61 channel is also a candidate for the dislocation channel for misfolded proteins from the ER to the cytosol during ER-associated degradation (ERAD). The structure of the Sec61 complex is highly conserved, but the roles of its N-terminal acetylation and its amphipathic N-terminal helix are unknown so far. To gain insight into the function of the Sec61p N-terminus, we mutated its N-acetylation site, deleted its amphipathic helix, or both the helix and the N-acetylation site. Mutation of the N-acetylation site on its own had no effect on protein import into the ER in intact cells, but resulted in an ERAD defect. Yeast expressing sec61 without the N-terminal amphipathic helix displayed severe growth defects and had profound defects in post-translational protein import into the ER. Nevertheless the formation of the hetero-heptameric Sec complex was not affected. Instead, the lack of the N-terminal amphipathic helix compromised the integrity of the heterotrimeric Sec61 complex. We conclude that the N-terminal helix of Sec61p is required for post-translational protein import into the ER and Sec61 complex stability, whereas N-terminal acetylation of Sec61p plays a role in ERAD. |
DOI der Erstveröffentlichung: | 10.1371/journal.pone.0215950 |
Link zu diesem Datensatz: | urn:nbn:de:bsz:291--ds-312239 hdl:20.500.11880/29269 http://dx.doi.org/10.22028/D291-31223 |
ISSN: | 1932-6203 |
Datum des Eintrags: | 17-Jun-2020 |
Fakultät: | NT - Naturwissenschaftlich- Technische Fakultät |
Fachrichtung: | NT - Biowissenschaften |
Professur: | NT - Prof. Dr. Karin Römisch |
Sammlung: | SciDok - Der Wissenschaftsserver der Universität des Saarlandes |
Dateien zu diesem Datensatz:
Datei | Beschreibung | Größe | Format | |
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journal.pone.0215950.pdf | The N-terminus of Sec61p plays key roles in ER protein import and ERAD | 1,57 MB | Adobe PDF | Öffnen/Anzeigen |
Diese Ressource wurde unter folgender Copyright-Bestimmung veröffentlicht: Lizenz von Creative Commons