Two Hrd1p homologues in the yeast Yarrowia lipolytica which act in different pathways
Autor: | Jean-Marie Beckerich, A. Babour, Anita Boisramé, M. Chasles |
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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: |
[SDV]Life Sciences [q-bio]
Molecular Sequence Data Fluorescent Antibody Technique Yarrowia Endoplasmic-reticulum-associated protein degradation Biology Fungal Proteins 03 medical and health sciences 0302 clinical medicine Genetics ERAD pathway Secretion Amino Acid Sequence PROTEASOME Molecular Biology Secretory pathway DNA Primers 030304 developmental biology CHAPERONE 0303 health sciences UBIQUITYLATION Base Sequence Sequence Homology Amino Acid Endoplasmic reticulum HRD1 PROTEIN [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biology General Medicine ERAD biology.organism_classification Yeast YARROWIA LIPOLYTICA Cell biology [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology Biochemistry SECRETION 030217 neurology & neurosurgery Function (biology) |
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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