Journal article

Gpi17p does not stably interact with other subunits of glycosylphosphatidylinositol transamidase in Saccharomyces cerevisiae

  • Zhu, Yonghua Unit of Biochemistry, Department of Medicine, University of Fribourg, Switzerland
  • Fraering, Patrick Unit of Biochemistry, Department of Medicine, University of Fribourg, Switzerland - Center for Neurologic Diseases, Brigham and Women's Hospital and Harvard Medical School, Boston, USA
  • Vionnet, Christine Unit of Biochemistry, Department of Medicine, University of Fribourg, Switzerland
  • Conzelmann, Andreas Unit of Biochemistry, Department of Medicine, University of Fribourg, Switzerland
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    25.05.2005
Published in:
  • Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids. - 2005, vol. 1735(1), p. 79
English Homologues of Gpi8p, Gaa1p, Gpi16p, Gpi17p, and Cdc91p are essential components of the GPI transamidase complex that adds glycosylphosphatidylinositols (GPIs 1) to newly synthesized proteins in the ER. In mammalian cells, these five subunits remain stably associated with each other in detergent. In yeast, we find no stable stoichiometric association of Gpi17p with the Gpi8p–Gpi16p–Gaa1p core... Show more…
Faculty
Faculté des sciences et de médecine
Department
Département de Biologie
Language
  • English
Classification
Biology
License
License undefined
Identifiers
Persistent URL
https://folia.unifr.ch/unifr/documents/299945