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Signal peptides open protein-conducting channels in E. coli

scientific article published on May 1992

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Europe PubMed Central

3 November 2017

Signal peptides open protein-conducting channels in E. coli (English)

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3 November 2017

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Blobel G

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Simon SM

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1 May 1992

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Europe PubMed Central

3 November 2017

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677-684

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Protein translocation across the endoplasmic reticulum. I. Detection in the microsomal membrane of a receptor for the signal recognition particle

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SecB functions as a cytosolic signal recognition factor for protein export in E. coli.

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Fusion of phospholipid vesicles with a planar membrane depends on the membrane permeability of the solute used to create the osmotic pressure

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Endogenously synthesized peptide with an endoplasmic reticulum signal sequence sensitizes antigen processing mutant cells to class I-restricted cell-mediated lysis

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[13] Bacterial Membranes

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Translocation of proteins across the endoplasmic reticulum. II. Signal recognition protein (SRP) mediates the selective binding to microsomal membranes of in-vitro-assembled polysomes synthesizing secretory protein

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Conformations of signal peptides induced by lipids suggest initial steps in protein export

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Modulation of folding pathways of exported proteins by the leader sequence

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Unity in function in the absence of consensus in sequence: role of leader peptides in export

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Co-translational membrane integration of calcium pump protein without signal sequence cleavage.

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Reconstitution of Cell Membrane Structure in vitro and its Transformation into an Excitable System

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A membrane component essential for vectorial translocation of nascent proteins across the endoplasmic reticulum: requirements for its extraction and reassociation with the membrane

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Fusion of phospholipid vesicles with planar phospholipid bilayer membranes. I. Discharge of vesicular contents across the planar membrane

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Induction of non-bilayer lipid structures by functional signal peptides

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Stop-transfer regions do not halt translocation of proteins into chloroplasts.

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Translocation of proteins across the endoplasmic reticulum. I. Signal recognition protein (SRP) binds to in-vitro-assembled polysomes synthesizing secretory protein

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A protein-conducting channel in the endoplasmic reticulum.

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Ribonucleoparticle-independent import of proteins into mammalian microsomes involves a membrane protein which is sensitive to chemical alkylation.

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The signal recognition particle receptor mediates the GTP-dependent displacement of SRP from the signal sequence of the nascent polypeptide

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Production and ultrastructure of lysozyme and ethylenediaminetetraacetate-lysozyme spheroplasts of Escherichia coli

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The signal sequence of nascent preprolactin interacts with the 54K polypeptide of the signal recognition particle

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10.1016/0092-8674(92)90231-Z

1 reference

stated in

Europe PubMed Central

3 November 2017

1 reference

Europe PubMed Central

PubMed ID

1375130

retrieved

3 November 2017

(Q42602564)

Signal peptides open protein-conducting channels in E. coli

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