DOI: 10.1091/mbc.e06-03-0200. The Plug Domain of Yeast Sec61p Is Important for Efficient Protein Translocation, but Is Not Essential for Cell Viability

The Plug Domain of Yeast Sec61p Is Important for Efficient Protein Translocation, but Is Not Essential for Cell Viability

10.1091/mbc.e06-03-0200

Crossref journal-article

American Society for Cell Biology (ASCB)

Molecular Biology of the Cell (1076)

Abstract

The Sec61/SecY translocon mediates translocation of proteins across the membrane and integration of membrane proteins into the lipid bilayer. The structure of the translocon revealed a plug domain blocking the pore on the lumenal side. It was proposed to be important for gating the protein conducting channel and for maintaining the permeability barrier in its unoccupied state. Here, we analyzed in yeast the effect of introducing destabilizing point mutations in the plug domain or of its partial or complete deletion. Unexpectedly, even when the entire plug domain was deleted, cells were viable without growth phenotype. They showed an effect on signal sequence orientation of diagnostic signal-anchor proteins, a minor defect in cotranslational and a significant deficiency in posttranslational translocation. Steady-state levels of the mutant protein were reduced, and when coexpressed with wild-type Sec61p, the mutant lacking the plug competed poorly for complex partners. The results suggest that the plug is unlikely to be important for sealing the translocation pore in yeast but that it plays a role in stabilizing Sec61p during translocon formation.

Bibliography

Junne, T., Schwede, T., Goder, V., & Spiess, M. (2006). The Plug Domain of Yeast Sec61p Is Important for Efficient Protein Translocation, but Is Not Essential for Cell Viability. Molecular Biology of the Cell, 17(9), 4063â4068.

Authors 4

Tina Junne (first)
Torsten Schwede (additional)
Veit Goder (additional)
Martin Spiess (additional)

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Dates

Type	When
Created	19 years, 1 month ago (July 6, 2006, 4:53 a.m.)
Deposited	5 years, 4 months ago (April 16, 2020, 2:04 a.m.)
Indexed	3 months, 2 weeks ago (May 16, 2025, 8:44 a.m.)
Issued	19 years ago (Sept. 1, 2006)
Published	19 years ago (Sept. 1, 2006)
Published Print	19 years ago (Sept. 1, 2006)

Funders 0

None

BibTeX

@article{Junne_2006, title={The Plug Domain of Yeast Sec61p Is Important for Efficient Protein Translocation, but Is Not Essential for Cell Viability}, volume={17}, ISSN={1939-4586}, url={http://dx.doi.org/10.1091/mbc.e06-03-0200}, DOI={10.1091/mbc.e06-03-0200}, number={9}, journal={Molecular Biology of the Cell}, publisher={American Society for Cell Biology (ASCB)}, author={Junne, Tina and Schwede, Torsten and Goder, Veit and Spiess, Martin}, editor={Gilmore, Reid}, year={2006}, month=sep, pages={4063–4068} }

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  "abstract": "<jats:p>The Sec61/SecY translocon mediates translocation of proteins across the membrane and integration of membrane proteins into the lipid bilayer. The structure of the translocon revealed a plug domain blocking the pore on the lumenal side. It was proposed to be important for gating the protein conducting channel and for maintaining the permeability barrier in its unoccupied state. Here, we analyzed in yeast the effect of introducing destabilizing point mutations in the plug domain or of its partial or complete deletion. Unexpectedly, even when the entire plug domain was deleted, cells were viable without growth phenotype. They showed an effect on signal sequence orientation of diagnostic signal-anchor proteins, a minor defect in cotranslational and a significant deficiency in posttranslational translocation. Steady-state levels of the mutant protein were reduced, and when coexpressed with wild-type Sec61p, the mutant lacking the plug competed poorly for complex partners. The results suggest that the plug is unlikely to be important for sealing the translocation pore in yeast but that it plays a role in stabilizing Sec61p during translocon formation.</jats:p>",
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