The bacterial translocon SecYEG opens upon ribosome binding. 2013

Denis G Knyazev, and Alexander Lents, and Eberhard Krause, and Nicole Ollinger, and Christine Siligan, and Daniel Papinski, and Lukas Winter, and Andreas Horner, and Peter Pohl
Institute of Biophysics, Johannes Kepler University Linz, A-4020 Linz, Austria.

In co-translational translocation, the ribosome funnel and the channel of the protein translocation complex SecYEG are aligned. For the nascent chain to enter the channel immediately after synthesis, a yet unidentified signal triggers displacement of the SecYEG sealing plug from the pore. Here, we show that ribosome binding to the resting SecYEG channel triggers this conformational transition. The purified and reconstituted SecYEG channel opens to form a large ion-conducting channel, which has the conductivity of the plug deletion mutant. The number of ion-conducting channels inserted into the planar bilayer per fusion event roughly equals the number of SecYEG channels counted by fluorescence correlation spectroscopy in a single proteoliposome. Thus, the open probability of the channel must be close to unity. To prevent the otherwise lethal proton leak, a closed post-translational conformation of the SecYEG complex bound to a ribosome must exist.

UI MeSH Term Description Entries
D007473 Ion Channels Gated, ion-selective glycoproteins that traverse membranes. The stimulus for ION CHANNEL GATING can be due to a variety of stimuli such as LIGANDS, a TRANSMEMBRANE POTENTIAL DIFFERENCE, mechanical deformation or through INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS. Membrane Channels,Ion Channel,Ionic Channel,Ionic Channels,Membrane Channel,Channel, Ion,Channel, Ionic,Channel, Membrane,Channels, Ion,Channels, Ionic,Channels, Membrane
D008051 Lipid Bilayers Layers of lipid molecules which are two molecules thick. Bilayer systems are frequently studied as models of biological membranes. Bilayers, Lipid,Bilayer, Lipid,Lipid Bilayer
D008563 Membrane Lipids Lipids, predominantly phospholipids, cholesterol and small amounts of glycolipids found in membranes including cellular and intracellular membranes. These lipids may be arranged in bilayers in the membranes with integral proteins between the layers and peripheral proteins attached to the outside. Membrane lipids are required for active transport, several enzymatic activities and membrane formation. Cell Membrane Lipid,Cell Membrane Lipids,Membrane Lipid,Lipid, Cell Membrane,Lipid, Membrane,Lipids, Cell Membrane,Lipids, Membrane,Membrane Lipid, Cell,Membrane Lipids, Cell
D008565 Membrane Proteins Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors. Cell Membrane Protein,Cell Membrane Proteins,Cell Surface Protein,Cell Surface Proteins,Integral Membrane Proteins,Membrane-Associated Protein,Surface Protein,Surface Proteins,Integral Membrane Protein,Membrane Protein,Membrane-Associated Proteins,Membrane Associated Protein,Membrane Associated Proteins,Membrane Protein, Cell,Membrane Protein, Integral,Membrane Proteins, Integral,Protein, Cell Membrane,Protein, Cell Surface,Protein, Integral Membrane,Protein, Membrane,Protein, Membrane-Associated,Protein, Surface,Proteins, Cell Membrane,Proteins, Cell Surface,Proteins, Integral Membrane,Proteins, Membrane,Proteins, Membrane-Associated,Proteins, Surface,Surface Protein, Cell
D009154 Mutation Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations. Mutations
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D000069816 SEC Translocation Channels Universally conserved multiprotein complexes that form the protein transport channel of the general secretory (SEC) pathway. The SEC translocase is present in all bacteria, archaea, and eukaryotes. It is in the ENDOPLASMIC RETICULUM membrane of eukaryotic cells, in the THYLAKOID MEMBRANE in CHLOROPLASTS and in some protozoa in the INNER MITOCHONDRIAL MEMBRANE. SEC Translocation Channel,SEC Translocon,SEC61 Translocation Channel,Sec Protein Translocation System,SecYEG Protein,SecYEG Translocation Channel,SEC Complexes,SEC Translocase,SEC Translocons,SEC61 Protein,SEC61 Proteins,SEC61 Translocase,SEC61 Translocation Channels,SEC61 Translocon,Sec Protein Translocation Systems,Sec61 Complex,Sec61 Protein Translocation System,SecY Translocase,SecYEG Complex,SecYEG Complexes,SecYEG Protein Translocation System,SecYEG Proteins,SecYEG Translocation Channels,SecYEG Translocon,Channel, SEC Translocation,Channel, SEC61 Translocation,Channel, SecYEG Translocation,Channels, SEC Translocation,Channels, SEC61 Translocation,Channels, SecYEG Translocation,Complex, Sec61,Complex, SecYEG,Complexes, SEC,Complexes, SecYEG,Protein, SEC61,Protein, SecYEG,Proteins, SEC61,Proteins, SecYEG,Translocase, SEC,Translocase, SEC61,Translocase, SecY,Translocation Channel, SEC,Translocation Channel, SEC61,Translocation Channel, SecYEG,Translocation Channels, SEC,Translocation Channels, SEC61,Translocation Channels, SecYEG,Translocon, SEC,Translocon, SEC61,Translocon, SecYEG,Translocons, SEC
D012270 Ribosomes Multicomponent ribonucleoprotein structures found in the CYTOPLASM of all cells, and in MITOCHONDRIA, and PLASTIDS. They function in PROTEIN BIOSYNTHESIS via GENETIC TRANSLATION. Ribosome
D013050 Spectrometry, Fluorescence Measurement of the intensity and quality of fluorescence. Fluorescence Spectrophotometry,Fluorescence Spectroscopy,Spectrofluorometry,Fluorescence Spectrometry,Spectrophotometry, Fluorescence,Spectroscopy, Fluorescence
D015640 Ion Channel Gating The opening and closing of ion channels due to a stimulus. The stimulus can be a change in membrane potential (voltage-gated), drugs or chemical transmitters (ligand-gated), or a mechanical deformation. Gating is thought to involve conformational changes of the ion channel which alters selective permeability. Gating, Ion Channel,Gatings, Ion Channel,Ion Channel Gatings

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