Publikationsdatum:
1997-08-15
Beschreibung:
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〉
Schlagwort(e):
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
Digitale ISSN:
1095-9203
Thema:
Biologie
,
Chemie und Pharmazie
,
Informatik
,
Medizin
,
Allgemeine Naturwissenschaft
,
Physik
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