Two Hrd1p homologues in the yeast Yarrowia lipolytica which act in different pathways

Autor: Jean-Marie Beckerich, A. Babour, Anita Boisramé, M. Chasles
Přispěvatelé: Microbiologie et Génétique Moléculaire (MGM), Institut National de la Recherche Agronomique (INRA)-Institut National Agronomique Paris-Grignon (INA P-G)-Centre National de la Recherche Scientifique (CNRS), Institut National Agronomique Paris Grignon (INAPG)
Jazyk: angličtina
Rok vydání: 2006
Předmět:
Zdroj: Molecular Genetics and Genomics
Molecular Genetics and Genomics, Springer Verlag, 2006, 275, pp.242-250
Molecular Genetics and Genomics, Springer Verlag, 2006, 275 (3), pp.242-250. ⟨10.1007/s00438-005-0084-6⟩
ISSN: 1617-4615
1617-4623
DOI: 10.1007/s00438-005-0084-6⟩
Popis: International audience; The endoplasmic reticulum associated degradation (ERAD) is a process widespread in eukaryotes that enable cells to get rid of unfolded or unassembled polypeptides which jam the endoplasmic reticulum compartment. In order to improve understanding of the initial steps of the secretory pathway and their relationship, we focused on components of the ERAD ubiquitylation machinery in the yeast Yarrowia lipolytica. Two Hrd1p homologues, Hrd1p and Hrh1p, were identified in Y. lipolytica. A study of the fate of the heterologous CPY* reporter protein showed that YlHrd1p is involved in the elimination of this misfolded polypeptide, while YlHrh1p is not. Moreover, the different phenotypic pattern displayed by Deltahrd1 and Deltahrh1 cells suggests that the two putative E3 enzymes function in separate ways. Our results bring some evidence of a coupling between the ERAD pathway and the co-translational translocation process and show that studies in Y. lipolytica can give new insights into events that take place in the ER.
Databáze: OpenAIRE
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