Protein transport by purified yeast Sec complex and Kar2p without membranes.
Posttranslational protein translocation across the endoplasmic reticulum membrane of yeast requires a seven-component transmembrane complex (the Sec complex) in collaboration with the lumenal Kar2 protein (Kar2p). A translocation substrate was initially bound to the cytosolic face of the purified Sec complex in a signal-sequence-dependent but Kar2p- and nucleotide-independent manner. In ... a subsequent reaction, in which Kar2p interacted with the lumenal face of the Sec complex and hydrolyzed adenosine triphosphate, the substrate moved through a channel formed by the Sec complex and was released at the lumenal end. Movement through the channel occurred in detergent solution in the absence of a lipid bilayer.
Mesh Terms:
Adenosine Triphosphate, Biological Transport, Cross-Linking Reagents, Cytosol, Detergents, Digitonin, Endoplasmic Reticulum, Fungal Proteins, HSP70 Heat-Shock Proteins, Heat-Shock Proteins, Lipid Bilayers, Liposomes, Membrane Proteins, Membrane Transport Proteins, Protein Precursors, Protein Sorting Signals, Proteolipids, RNA, Transfer, Saccharomyces cerevisiae Proteins, Solubility, Succinimides
Adenosine Triphosphate, Biological Transport, Cross-Linking Reagents, Cytosol, Detergents, Digitonin, Endoplasmic Reticulum, Fungal Proteins, HSP70 Heat-Shock Proteins, Heat-Shock Proteins, Lipid Bilayers, Liposomes, Membrane Proteins, Membrane Transport Proteins, Protein Precursors, Protein Sorting Signals, Proteolipids, RNA, Transfer, Saccharomyces cerevisiae Proteins, Solubility, Succinimides
Science
Date: Aug. 15, 1997
PubMed ID: 9252322
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