Oligomeric rings of the Sec61p complex induced by ligands required for protein translocation

Dorit Hanein*, Kent E.S. Matlack, Berit Jungnickel, Kathrin Plath, Kai Uwe Kalies, Kenneth R. Miller, Tom A. Rapoport, Christopher W. Akey

*Corresponding author for this work
274 Citations (Scopus)


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 ~85Å 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 post-translational transport.

Original languageEnglish
Issue number4
Pages (from-to)721-732
Number of pages12
Publication statusPublished - 15.01.1996

Research Areas and Centers

  • Academic Focus: Center for Infection and Inflammation Research (ZIEL)


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