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  • 1
    Publication Date: 1997-08-15
    Description: 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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Matlack, K E -- Plath, K -- Misselwitz, B -- Rapoport, T A -- GM54238-02/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Aug 15;277(5328):938-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9252322" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Biological Transport ; Cross-Linking Reagents ; Cytosol/metabolism ; Detergents ; Digitonin ; Endoplasmic Reticulum/metabolism ; Fungal Proteins/*metabolism ; HSP70 Heat-Shock Proteins/*metabolism ; *Heat-Shock Proteins ; Lipid Bilayers ; Liposomes/metabolism ; Membrane Proteins/*metabolism ; *Membrane Transport Proteins ; Protein Precursors/*metabolism ; Protein Sorting Signals/metabolism ; Proteolipids/metabolism ; RNA, Transfer/metabolism ; *Saccharomyces cerevisiae Proteins ; Solubility ; Succinimides
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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