ER translocation intermediates are adjacent to a nonglycosylated 34-kD integral membrane protein.

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ER translocation intermediates are adjacent to a nonglycosylated 34-kD integral membrane protein

We have used the homobifunctional cross-linking reagent disuccinimidyl suberate (DSS) to identify proteins that are adjacent to nascent polypeptides undergoing translocations across mammalian rough ER. Translocation intermediates were assembled by supplementing cell free translations of truncated mRNAs with the signal recognition particle (SRP) and microsomal membrane vesicles. Two prominent cr...

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Protein translocation across the endoplasmic reticulum membrane: identification by photocross-linking of a 39-kD integral membrane glycoprotein as part of a putative translocation tunnel

The molecular environment of secretory proteins during translocation across the ER membrane was examined by photocross-linking. Nascent preprolactin chains of various lengths, synthesized by in vitro translation of truncated messenger RNAs in the presence of N epsilon-(5-azido-2-nitrobenzoyl)-Lys-tRNA, signal recognition particle, and microsomal membranes, were used to position photoreactive pr...

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Protein Translocation across the Endoplasmic Reticulum Membrane: Identification by Photocross-Lknking of a 39-kD Integral Membrane Glycoprotein as Part of a Putative Translocation Tunnel

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SED5 encodes a 39-kD integral membrane protein required for vesicular transport between the ER and the Golgi complex

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ژورنال

عنوان ژورنال: Journal of Cell Biology

سال: 1991

ISSN: 0021-9525,1540-8140

DOI: 10.1083/jcb.114.1.21