Sgf1p, a new component of the Sec34p/Sec35p complex.
Here we report the identification of SGF1 as a high-copy suppressor of the sec35-1 mutant. SGF1 encodes an essential hydrophilic protein of approximately 100 kDa. Using the yeast two-hybrid system and coprecipitation studies, we demonstrate that Sgf1p is a new subunit of the multiprotein Sec34p/Sec35p complex. Reduced levels of Sgf1p ... lead to the accumulation of a variety of membranes as well as a kinetic block in endoplasmic reticulum to Golgi traffic. Immunofluorescence studies demonstrate that Sec34p is found throughout the Golgi, with a high concentration on early Golgi. Although an earlier study suggested that Sec34p (Grd20p) is not required for protein secretion, we show here that the sec34-2 and sec35-1 mutations lead to a pleiotropic block in the secretion of all proteins into the growth medium.
Mesh Terms:
Adaptor Proteins, Vesicular Transport, Base Sequence, Carrier Proteins, Cell Compartmentation, Cell Membrane, DNA Primers, Fluorescent Antibody Technique, Golgi Apparatus, Membrane Proteins, Microscopy, Electron, Open Reading Frames, Protein Transport, Saccharomyces cerevisiae Proteins, Two-Hybrid System Techniques, Vesicular Transport Proteins
Adaptor Proteins, Vesicular Transport, Base Sequence, Carrier Proteins, Cell Compartmentation, Cell Membrane, DNA Primers, Fluorescent Antibody Technique, Golgi Apparatus, Membrane Proteins, Microscopy, Electron, Open Reading Frames, Protein Transport, Saccharomyces cerevisiae Proteins, Two-Hybrid System Techniques, Vesicular Transport Proteins
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Date: Nov. 01, 2001
PubMed ID: 11733049
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