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Signal Recognition Particle Binds to Ribosome-bound Signal Sequences with Fluorescence-detected Subnanomolar Affinity That Does Not Diminish as the Nascent Chain Lengthens*
The binding of signal recognition particle (SRP) to ribosome-bound signal sequences has been characterized directly and quantitatively using fluorescence spectroscopy. A fluorescent probe wasExpand
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Identification of a membrane-spanning domain of the thiol-activated pore-forming toxin Clostridium perfringens perfringolysin O: an alpha-helical to beta-sheet transition identified by fluorescence
Clostridium perfringens perfringolysin O (PFO or theta-toxin) is a cytolytic toxin that binds to cholesterol-containing membranes and then self-associates to spontaneously form aqueous pores ofExpand
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Redefining cholesterol's role in the mechanism of the cholesterol-dependent cytolysins
The cholesterol-dependent cytolysins (CDCs) constitute a large family of pore-forming toxins that function exclusively on cholesterol-containing membranes. A detailed analysis of the various stagesExpand
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Sequential triage of transmembrane segments by Sec61α during biogenesis of a native multispanning membrane protein
During polytopic protein biogenesis, the Sec61 translocon must rapidly orient and integrate multiple transmembrane segments (TMs) into the endoplasmic reticulum membrane. To understand this process,Expand
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Cotranslational protein integration into the ER membrane is mediated by the binding of nascent chains to translocon proteins.
During cotranslational protein integration into the ER membrane, each transmembrane (TM) segment moves laterally through the translocon to reach the lipid bilayer. Photocrosslinking studies revealExpand
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The mechanism of pore assembly for a cholesterol-dependent cytolysin: formation of a large prepore complex precedes the insertion of the transmembrane beta-hairpins.
Perfringolysin O (PFO) is a member of the cholesterol-dependent cytolysin (CDC) family of membrane-penetrating toxins. The CDCs form large homooligomers (estimated to be comprised of up to 50 CDCExpand
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Membrane-dependent conformational changes initiate cholesterol-dependent cytolysin oligomerization and intersubunit β-strand alignment
Cholesterol-dependent cytolysins are bacterial protein toxins that bind to cholesterol-containing membranes, form oligomeric complexes and insert into the bilayer to create large aqueous pores.Expand
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Assembly and Topography of the Prepore Complex in Cholesterol-dependent Cytolysins*
Cholesterol-dependent cytolysins are a family of poreforming proteins that have been shown to be virulence factors for a large number of pathogenic bacteria. The mechanism of pore formation for theseExpand
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How Interaction of Perfringolysin O with Membranes Is Controlled by Sterol Structure, Lipid Structure, and Physiological Low pH
Perfringolysin O (PFO) is a sterol-dependent, pore-forming cytolysin. To understand the molecular basis of PFO membrane interaction, we studied its dependence upon sterol and lipid structure andExpand
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Cotranslational Membrane Protein Biogenesis at the Endoplasmic Reticulum*
In eukaryotic cells, most polypeptides destined to become membrane proteins are initially integrated into the membrane of the endoplasmic reticulum (ER) before being sorted to the location at whichExpand
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