Proteins in the early golgi compartment of Saccharomyces cerevisiae immunoisolated by Sed5p.
The yeast tSNARE Sed5p is considered to mainly reside in the early Golgi compartment at the steady state of its intracellular cycling. To better understand this compartment, we immunoisolated a membrane subfraction having Sed5p on the surface (the Sed5 vesicles). Immunoblot studies showed that considerable portions (20-30%) of the Golgi ... mannosyltransferases (Mnt1p, Van1p, and Mnn9p) were simultaneously recovered while the late Golgi (Kex2p) or endoplasmic reticulum (Sec71p) proteins were almost excluded. The N-terminal sequences of the polypeptides detectable by Coomassie blue staining indicated that the prominent components of the Sed5 vesicles include Anp1p, Emp24p, Erv25p, Erp1p, Ypt52p, and a putative membrane protein of unknown function (Yml067c).
Mesh Terms:
Carrier Proteins, Electrophoresis, Polyacrylamide Gel, Fungal Proteins, Golgi Apparatus, Immunoblotting, Mannosyltransferases, Membrane Proteins, Qa-SNARE Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Sequence Analysis, Protein, Vesicular Transport Proteins, rab GTP-Binding Proteins, rab5 GTP-Binding Proteins
Carrier Proteins, Electrophoresis, Polyacrylamide Gel, Fungal Proteins, Golgi Apparatus, Immunoblotting, Mannosyltransferases, Membrane Proteins, Qa-SNARE Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Sequence Analysis, Protein, Vesicular Transport Proteins, rab GTP-Binding Proteins, rab5 GTP-Binding Proteins
FEBS Lett.
Date: Mar. 10, 2000
PubMed ID: 10713261
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