Oligomeric Rings of the Sec61p Complex Induced by Ligands Required for Protein Translocation
Identifieur interne : 003F38 ( Main/Exploration ); précédent : 003F37; suivant : 003F39Oligomeric Rings of the Sec61p Complex Induced by Ligands Required for Protein Translocation
Auteurs : Dorit Hanein [États-Unis] ; Kent E. S Matlack [États-Unis] ; Berit Jungnickel [États-Unis] ; Kathrin Plath [États-Unis, Allemagne] ; Kai-Uwe Kalies [Allemagne] ; Kenneth R. Miller [États-Unis] ; Tom A. Rapoport [États-Unis] ; Christopher W. Akey [États-Unis]Source :
- Cell [ 0092-8674 ] ; 1996.
English descriptors
- Teeft :
- Average diameter, Bilayer, Biol, Blobel, Canine, Cell biol, Central pore, Corresponding averages, Cotranslational, Cotranslational pathway, Cotranslational translocation, Cytoplasmic surface, Data sets, Electron microscopy, Endoplasmic, Endoplasmic reticulum, Endoplasmic reticulum membrane, Experimental procedures, Fracture, Freeze fracture, Gating, Gorlich, Hartmann, Heptameric, Heterotrimers, Image processing, Individual particles, Inset, Intramembranous particles, Jungnickel, Kalies, Koac, Large numbers, Lipid, Lipid bilayer, Magnesium acetate, Membrane, Membrane proteins, Microscopy, Microsome, Morphology, Nascent, Nascent chain, Native membranes, Negative stain, Oligomer, Oligomeric, Oligomeric rings, Oligomerization, Oligomers, Panzner, Pathway, Phospholipid bilayer, Pmol, Polypeptide, Pore, Posttranslational, Posttranslational pathway, Posttranslational protein transport, Posttranslational translocation, Posttranslational transport, Protein translocation, Protein transport, Proteoliposomes, Proteoliposomes reconstituted, Quasipentagonal, Quasipentagonal appearance, Quasipentagonal morphology, Rapoport, Reconstituted, Reconstituted membranes, Reconstituted proteoliposomes, Reconstitution, Reticulum, Ribosome, Ring structures, Rings, Rotary shadowing, Rough endoplasmic reticulum, Same buffer, Signal sequence, Subunit, Translocating, Translocation, Unstained specimens, Yeast, Yeast ribosomes.
Abstract
Abstract: The heterotrimeric Sec61p complex is a major component of the protein-conducting channel of the endoplasmic reticulum (ER) membrane, associating with either ribosomes or the Sec62/63 complex to perform co- and posttranslational transport, respectively. We show by electron microscopy that purified mammalian and yeast Sec61p complexes in detergent form cylindrical oligomers with a diameter of ∼85 Å and a central pore of ∼20 Å. Each oligomer contains 3–4 heterotrimers. Similar ring structures are seen in reconstituted proteoliposomes and native membranes. Oligomer formation by the reconstituted Sec61p complex is stimulated by its association with ribosomes or the Sec62/63p complex. We propose that these cylindrical oligomers represent protein-conducting channels of the ER, formed by ligands specific for co- and posttranslational transport.
Url:
DOI: 10.1016/S0092-8674(00)81391-4
Affiliations:
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S Matlack</name></author><author><name sortKey="Jungnickel, Berit" sort="Jungnickel, Berit" uniqKey="Jungnickel B" first="Berit" last="Jungnickel">Berit Jungnickel</name></author><author><name sortKey="Plath, Kathrin" sort="Plath, Kathrin" uniqKey="Plath K" first="Kathrin" last="Plath">Kathrin Plath</name></author><author><name sortKey="Kalies, Kai Uwe" sort="Kalies, Kai Uwe" uniqKey="Kalies K" first="Kai-Uwe" last="Kalies">Kai-Uwe Kalies</name></author><author><name sortKey="Miller, Kenneth R" sort="Miller, Kenneth R" uniqKey="Miller K" first="Kenneth R" last="Miller">Kenneth R. Miller</name></author><author><name sortKey="Rapoport, Tom A" sort="Rapoport, Tom A" uniqKey="Rapoport T" first="Tom A" last="Rapoport">Tom A. Rapoport</name></author><author><name sortKey="Akey, Christopher W" sort="Akey, Christopher W" uniqKey="Akey C" first="Christopher W" last="Akey">Christopher W. 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S Matlack</name><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115</wicri:regionArea><wicri:noRegion>Massachusetts 02115</wicri:noRegion></affiliation></author><author><name sortKey="Jungnickel, Berit" sort="Jungnickel, Berit" uniqKey="Jungnickel B" first="Berit" last="Jungnickel">Berit Jungnickel</name><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115</wicri:regionArea><wicri:noRegion>Massachusetts 02115</wicri:noRegion></affiliation></author><author><name sortKey="Plath, Kathrin" sort="Plath, Kathrin" uniqKey="Plath K" first="Kathrin" last="Plath">Kathrin Plath</name><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115</wicri:regionArea><wicri:noRegion>Massachusetts 02115</wicri:noRegion></affiliation><affiliation wicri:level="3"><country xml:lang="fr">Allemagne</country><wicri:regionArea>Max Delbrueck Center for Molecular Medicine, Robert Roessle Str. 10, 13122 Berlin-Buch</wicri:regionArea><placeName><region type="land" nuts="3">Berlin</region><settlement type="city">Berlin</settlement></placeName></affiliation></author><author><name sortKey="Kalies, Kai Uwe" sort="Kalies, Kai Uwe" uniqKey="Kalies K" first="Kai-Uwe" last="Kalies">Kai-Uwe Kalies</name><affiliation wicri:level="3"><country xml:lang="fr">Allemagne</country><wicri:regionArea>Max Delbrueck Center for Molecular Medicine, Robert Roessle Str. 10, 13122 Berlin-Buch</wicri:regionArea><placeName><region type="land" nuts="3">Berlin</region><settlement type="city">Berlin</settlement></placeName></affiliation></author><author><name sortKey="Miller, Kenneth R" sort="Miller, Kenneth R" uniqKey="Miller K" first="Kenneth R" last="Miller">Kenneth R. 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Akey</name><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biophysics, Boston University School of Medicine, Boston, Massashusetts 02218-2394</wicri:regionArea><wicri:noRegion>Massashusetts 02218-2394</wicri:noRegion></affiliation><affiliation></affiliation><affiliation wicri:level="1"><country wicri:rule="url">États-Unis</country></affiliation></author></analytic><monogr></monogr><series><title level="j">Cell</title><title level="j" type="abbrev">CELL</title><idno type="ISSN">0092-8674</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1996">1996</date><biblScope unit="volume">87</biblScope><biblScope unit="issue">4</biblScope><biblScope unit="page" from="721">721</biblScope><biblScope unit="page" to="732">732</biblScope></imprint><idno type="ISSN">0092-8674</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0092-8674</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Average diameter</term><term>Bilayer</term><term>Biol</term><term>Blobel</term><term>Canine</term><term>Cell biol</term><term>Central pore</term><term>Corresponding averages</term><term>Cotranslational</term><term>Cotranslational pathway</term><term>Cotranslational translocation</term><term>Cytoplasmic surface</term><term>Data sets</term><term>Electron microscopy</term><term>Endoplasmic</term><term>Endoplasmic reticulum</term><term>Endoplasmic reticulum membrane</term><term>Experimental procedures</term><term>Fracture</term><term>Freeze fracture</term><term>Gating</term><term>Gorlich</term><term>Hartmann</term><term>Heptameric</term><term>Heterotrimers</term><term>Image processing</term><term>Individual particles</term><term>Inset</term><term>Intramembranous particles</term><term>Jungnickel</term><term>Kalies</term><term>Koac</term><term>Large numbers</term><term>Lipid</term><term>Lipid bilayer</term><term>Magnesium acetate</term><term>Membrane</term><term>Membrane proteins</term><term>Microscopy</term><term>Microsome</term><term>Morphology</term><term>Nascent</term><term>Nascent chain</term><term>Native membranes</term><term>Negative stain</term><term>Oligomer</term><term>Oligomeric</term><term>Oligomeric rings</term><term>Oligomerization</term><term>Oligomers</term><term>Panzner</term><term>Pathway</term><term>Phospholipid bilayer</term><term>Pmol</term><term>Polypeptide</term><term>Pore</term><term>Posttranslational</term><term>Posttranslational pathway</term><term>Posttranslational protein transport</term><term>Posttranslational translocation</term><term>Posttranslational transport</term><term>Protein translocation</term><term>Protein transport</term><term>Proteoliposomes</term><term>Proteoliposomes reconstituted</term><term>Quasipentagonal</term><term>Quasipentagonal appearance</term><term>Quasipentagonal morphology</term><term>Rapoport</term><term>Reconstituted</term><term>Reconstituted membranes</term><term>Reconstituted proteoliposomes</term><term>Reconstitution</term><term>Reticulum</term><term>Ribosome</term><term>Ring structures</term><term>Rings</term><term>Rotary shadowing</term><term>Rough endoplasmic reticulum</term><term>Same buffer</term><term>Signal sequence</term><term>Subunit</term><term>Translocating</term><term>Translocation</term><term>Unstained specimens</term><term>Yeast</term><term>Yeast ribosomes</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The heterotrimeric Sec61p complex is a major component of the protein-conducting channel of the endoplasmic reticulum (ER) membrane, associating with either ribosomes or the Sec62/63 complex to perform co- and posttranslational transport, respectively. We show by electron microscopy that purified mammalian and yeast Sec61p complexes in detergent form cylindrical oligomers with a diameter of ∼85 Å and a central pore of ∼20 Å. Each oligomer contains 3–4 heterotrimers. Similar ring structures are seen in reconstituted proteoliposomes and native membranes. Oligomer formation by the reconstituted Sec61p complex is stimulated by its association with ribosomes or the Sec62/63p complex. We propose that these cylindrical oligomers represent protein-conducting channels of the ER, formed by ligands specific for co- and posttranslational transport.</div></front></TEI><affiliations><list><country><li>Allemagne</li><li>États-Unis</li></country><region><li>Berlin</li><li>Rhode Island</li></region><settlement><li>Berlin</li><li>Providence (Rhode Island)</li></settlement><orgName><li>Université Brown</li></orgName></list><tree><country name="États-Unis"><noRegion><name sortKey="Hanein, Dorit" sort="Hanein, Dorit" uniqKey="Hanein D" first="Dorit" last="Hanein">Dorit Hanein</name></noRegion><name sortKey="Akey, Christopher W" sort="Akey, Christopher W" uniqKey="Akey C" first="Christopher W" last="Akey">Christopher W. Akey</name><name sortKey="Akey, Christopher W" sort="Akey, Christopher W" uniqKey="Akey C" first="Christopher W" last="Akey">Christopher W. Akey</name><name sortKey="Jungnickel, Berit" sort="Jungnickel, Berit" uniqKey="Jungnickel B" first="Berit" last="Jungnickel">Berit Jungnickel</name><name sortKey="Matlack, Kent E S" sort="Matlack, Kent E S" uniqKey="Matlack K" first="Kent E. S" last="Matlack">Kent E. S Matlack</name><name sortKey="Miller, Kenneth R" sort="Miller, Kenneth R" uniqKey="Miller K" first="Kenneth R" last="Miller">Kenneth R. Miller</name><name sortKey="Plath, Kathrin" sort="Plath, Kathrin" uniqKey="Plath K" first="Kathrin" last="Plath">Kathrin Plath</name><name sortKey="Rapoport, Tom A" sort="Rapoport, Tom A" uniqKey="Rapoport T" first="Tom A" last="Rapoport">Tom A. Rapoport</name></country><country name="Allemagne"><region name="Berlin"><name sortKey="Plath, Kathrin" sort="Plath, Kathrin" uniqKey="Plath K" first="Kathrin" last="Plath">Kathrin Plath</name></region><name sortKey="Kalies, Kai Uwe" sort="Kalies, Kai Uwe" uniqKey="Kalies K" first="Kai-Uwe" last="Kalies">Kai-Uwe Kalies</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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