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A more recent version of this article appeared on July 1, 2002
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Submitted on October 26, 2001
Revised on March 4, 2002
Accepted on April 19, 2002
1 Max-Delbrück-Laboratorium, Carl-von-Linné-Weg 10, 50829 Köln, Germany
* Corresponding author. E-mail address: nils.johnsson{at}itg.fzk.de.
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 Nub-labeled Ssh1p and Cub-translocation substrates bearing four different signal sequences. The so determined interaction profile of Ssh1p was compared to the signal sequence interaction profile of the correspondingly modified Nub-Sec61p. The assay reveals interactions of Ssh1p with the signal sequences of Kar2p and invertase, whereas Sec61p additionally interacts with the signal sequences of Mf
1 and CPY. The measured physical proximity between Ssh1p and the ß-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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