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Vol. 13, Issue 7, 2223-2232, July 2002

Recognition of a Subset of Signal Sequences by Ssh1p, a Sec61p-related Protein in the Membrane of Endoplasmic Reticulum of Yeast Saccharomyces cerevisiae

Sandra Wittke, Martin Dünnwald,^* Markus Albertsen, and Nils Johnsson^§

Max-Delbrück-Laboratorium, 50829 Cologne, Germany

Ssh1p of Saccharomyces cerevisiae is related in sequence to Sec61p, a general receptor for signal sequences and the major subunit of the channel that guides proteins across the membrane of the endoplasmic reticulum. The split-ubiquitin technique was used to determine whether Ssh1p serves as an additional receptor for signal sequences in vivo. We measured the interactions between the N_ub-labeled Ssh1p and C_ub-translocation substrates bearing four different signal sequences. The so-determined interaction profile of Ssh1p was compared with the signal sequence interaction profile of the correspondingly modified N_ub-Sec61p. The assay reveals interactions of Ssh1p with the signal sequences of Kar2p and invertase, whereas Sec61p additionally interacts with the signal sequences of Mf1 and carboxypeptidase Y. The measured physical proximity between Ssh1p and the -subunit of the signal sequence recognition particle receptor confirms our hypothesis that Ssh1p is directly involved in the cotranslational translocation of proteins across the membrane of the endoplasmic reticulum.

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Corresponding author. E-mail address: nils.johnsson{at}itg.fzk.de.

Present addresses: ^*Whitehead Institute, Nine Cambridge Center, Cambridge, MA 02142-1479; Department of Biochemistry, University of Cologne, Zülpicher Straße 47, 50674 Cologne, Germany; ^§Forschungszentrum Karlsruhe, Institute of Genetics, Postfach 3640, 76021 Karlsruhe, Germany.

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Molecular Biology of the Cell
Vol. 13, 2223-2232, July 2002
Copyright © 2002 by The American Society for Cell Biology

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