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      Proteins in the early golgi compartment of Saccharomyces cerevisiae immunoisolated by Sed5p.

      Febs Letters
      Carrier Proteins, analysis, metabolism, Electrophoresis, Polyacrylamide Gel, Fungal Proteins, Golgi Apparatus, Immunoblotting, Mannosyltransferases, Membrane Proteins, Qa-SNARE Proteins, Saccharomyces cerevisiae, ultrastructure, Saccharomyces cerevisiae Proteins, Sequence Analysis, Protein, Vesicular Transport Proteins, rab GTP-Binding Proteins, rab5 GTP-Binding Proteins

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          Abstract

          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).

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