QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) All Versions of this Article: 01-10-0518v1 13/7/2223    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Wittke, S. Articles by Johnsson, N. Search for Related Content PubMed PubMed Citation Articles by Wittke, S. Articles by Johnsson, N.

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.

---

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.

---

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

This article has been cited by other articles:

				T. Becker, S. Bhushan, A. Jarasch, J.-P. Armache, S. Funes, F. Jossinet, J. Gumbart, T. Mielke, O. Berninghausen, K. Schulten, et al. Structure of Monomeric Yeast and Mammalian Sec61 Complexes Interacting with the Translating Ribosome Science, December 4, 2009; 326(5958): 1369 - 1373. [Abstract] [Full Text] [PDF]

				M. B. Metzger and S. Michaelis Analysis of Quality Control Substrates in Distinct Cellular Compartments Reveals a Unique Role for Rpn4p in Tolerating Misfolded Membrane Proteins Mol. Biol. Cell, February 1, 2009; 20(3): 1006 - 1019. [Abstract] [Full Text] [PDF]

				A. Varshavsky Discovery of Cellular Regulation by Protein Degradation J. Biol. Chem., December 12, 2008; 283(50): 34469 - 34489. [Full Text] [PDF]

				R. S. Hegde and S.-W. Kang The concept of translocational regulation J. Cell Biol., July 28, 2008; 182(2): 225 - 232. [Abstract] [Full Text] [PDF]

				Y. Jiang, Z. Cheng, E. C. Mandon, and R. Gilmore An interaction between the SRP receptor and the translocon is critical during cotranslational protein translocation J. Cell Biol., March 24, 2008; 180(6): 1149 - 1161. [Abstract] [Full Text] [PDF]

				A. Yan and W. J. Lennarz Two oligosaccharyl transferase complexes exist in yeast and associate with two different translocons Glycobiology, December 1, 2005; 15(12): 1407 - 1415. [Abstract] [Full Text] [PDF]

				J. P. Miller, R. S. Lo, A. Ben-Hur, C. Desmarais, I. Stagljar, W. S. Noble, and S. Fields Large-scale identification of yeast integral membrane protein interactions PNAS, August 23, 2005; 102(34): 12123 - 12128. [Abstract] [Full Text] [PDF]

				M. Chavan, A. Yan, and W. J. Lennarz Subunits of the Translocon Interact with Components of the Oligosaccharyl Transferase Complex J. Biol. Chem., June 17, 2005; 280(24): 22917 - 22924. [Abstract] [Full Text] [PDF]

				X. Wang and N. Johnsson Protein kinase CK2 phosphorylates Sec63p to stimulate the assembly of the endoplasmic reticulum protein translocation apparatus J. Cell Sci., February 15, 2005; 118(4): 723 - 732. [Abstract] [Full Text] [PDF]

				Z. Cheng, Y. Jiang, E. C. Mandon, and R. Gilmore Identification of cytoplasmic residues of Sec61p involved in ribosome binding and cotranslational translocation J. Cell Biol., January 3, 2005; 168(1): 67 - 77. [Abstract] [Full Text] [PDF]

				C. G. Levine, D. Mitra, A. Sharma, C. L. Smith, and R. S. Hegde The Efficiency of Protein Compartmentalization into the Secretory Pathway Mol. Biol. Cell, January 1, 2005; 16(1): 279 - 291. [Abstract] [Full Text] [PDF]

				E. L. Snapp, G. A. Reinhart, B. A. Bogert, J. Lippincott-Schwartz, and R. S. Hegde The organization of engaged and quiescent translocons in the endoplasmic reticulum of mammalian cells J. Cell Biol., March 29, 2004; 164(7): 997 - 1007. [Abstract] [Full Text] [PDF]

				J. Helmers, D. Schmidt, J. S. Glavy, G. Blobel, and T. Schwartz The {beta}-Subunit of the Protein-conducting Channel of the Endoplasmic Reticulum Functions as the Guanine Nucleotide Exchange Factor for the {beta}-Subunit of the Signal Recognition Particle Receptor J. Biol. Chem., June 20, 2003; 278(26): 23686 - 23690. [Abstract] [Full Text] [PDF]