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Identification and Characterization of a Membrane Component Essential for the Translocation of Nascent Proteins across the Membrane of the Endoplasmic Reticulum

Meyer, David I. ; Dobberstein, Bernhard

In: THE JOURNAL OF CELL BIOLOGY , 87 (1980), pp. 503-508

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When rough microsomes are subjected to limited proteolysis and high salt, a soluble fraction can be separated from the membrane . Neither fraction alone is capable of vectorially translocating nascent peptides . When the soluble extract is recombined with the residual membrane fraction, translocating activity is restored . Standard biochemical techniques were used to identify and characterize the active component derived by treating rough microsomes with elastase and high salt. The active factor is a peptide fragment with an apparent molecular weight of 60,000. It represents the cytoplasmic domain of a larger membrane protein. The fragment is basic and has at least one accessible sulfhydryl group. These characteristics facilitated its purification and identification as a membrane component required for translocation of nascent peptides across microsomal membranes.

Item Type: Article
Journal or Publication Title: THE JOURNAL OF CELL BIOLOGY
Volume: 87
Date Deposited: 17 Jun 2008 17:01
Date: 1980
Page Range: pp. 503-508
Faculties / Institutes: Service facilities > Center for Molecular Biology Heidelberg
Subjects: 570 Life sciences
Schriftenreihe ID: Works by Bernhard Dobberstein
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