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Vol. 11, Issue 11, 3859-3871, November 2000

Sec62p, A Component of the Endoplasmic Reticulum Protein Translocation Machinery, Contains Multiple Binding Sites for the Sec-Complex

Sandra Wittke, Martin Dünnwald, and Nils Johnsson*

Max-Delbrück-Laboratorium, D-50829 Köln, Germany

SEC62 encodes an essential component of the Sec-complex that is responsible for posttranslational protein translocation across the membrane of the endoplasmic reticulum in Saccharomyces cerevisiae. The specific role of Sec62p in translocation was not known and difficult to identify because it is part of an oligomeric protein complex in the endoplasmic reticulum membrane. An in vivo competition assay allowed us to characterize and dissect physical and functional interactions between Sec62p and components of the Sec-complex. We could show that Sec62p binds via its cytosolic N- and C-terminal domains to the Sec-complex. The N-terminal domain, which harbors the major interaction site, binds directly to the last 14 residues of Sec63p. The C-terminal binding site of Sec62p is less important for complex stability, but adjoins the region in Sec62p that might be involved in signal sequence recognition.

* Corresponding author. E-mail address: johnsson{at}mpiz-koeln.mpg.de.

Molecular Biology of the Cell
Vol. 11, 3859-3871, November 2000
Copyright © 2000 by The American Society for Cell Biology


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