DOI: 10.1098/rstb.1999.0495. The Saccharomyces cerevisiae ubiquitin

The Saccharomyces cerevisiae ubiquitin–proteasome system

10.1098/rstb.1999.0495

Crossref journal-article

The Royal Society

Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences (175)

Abstract

Our studies of the yeast ubiquitin-proteasome pathway have uncovered a number of general principles that govern substrate selectivity and proteolysis in this complex system. Much of the work has focused on the destruction of a yeast transcription factor, MATα2. The α2 protein is polyubiquitinated and rapidly degraded in α–haploid cells. One pathway of proteolytic targeting, which depends on two distinct endoplasmic reticulum–localized ubiquitin–conjugating enzymes, recognizes the hydrophobic face of an amphipathic helix in α2. Interestingly, degradation of α2 is blocked ina/α–diploid cells by heterodimer formation between the α2 anda1 homeodomain proteins. The data suggest that degradation signals may overlap protein–protein interaction surfaces, allowing a straightforward steric mechanism for regulated degradation. Analysis of α2 degradation led to the identification of both 20S and 26S proteasome subunits, and several key features of proteasome assembly and active–site formation were subsequently uncovered. Finally, it has become clear that protein (poly)ubiquitination is highly dynamicin vivo, and our studies of yeast de–ubiquitinating enzymes illustrate how such enzymes can facilitate the proteolysis of diverse substrates.

Bibliography

Hochstrasser, M., Johnson, P. R., Arendt, C. S., Amerik, A. Y., Swaminathan, S., Swanson, R., Li, S., Laney, J., Pals-Rylaarsdam, R., Nowak, J., & Connerly, P. L. (1999). The Saccharomyces cerevisiae ubiquitinâproteasome system. Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences, 354(1389), 1513â1522.

Authors 11

M. Hochstrasser (first)
P. R. Johnson (additional)
C. S. Arendt (additional)
A. Y. Amerik (additional)
S. Swaminathan (additional)
R. Swanson (additional)
S. Li (additional)
J. Laney (additional)
R. Pals-Rylaarsdam (additional)
J. Nowak (additional)
P. L. Connerly (additional)

References 39 Referenced 26

Dates

Type	When
Created	23 years, 1 month ago (July 26, 2002, 7:55 p.m.)
Deposited	2 years, 4 months ago (April 23, 2023, 1:37 a.m.)
Indexed	11 months, 2 weeks ago (Sept. 15, 2024, 5:40 p.m.)
Issued	25 years, 11 months ago (Sept. 29, 1999)
Published	25 years, 11 months ago (Sept. 29, 1999)
Published Online	25 years, 11 months ago (Sept. 29, 1999)
Published Print	25 years, 11 months ago (Sept. 29, 1999)

Funders 0

None

BibTeX

@article{Hochstrasser_1999, title={The Saccharomyces cerevisiae ubiquitin–proteasome system}, volume={354}, ISSN={1471-2970}, url={http://dx.doi.org/10.1098/rstb.1999.0495}, DOI={10.1098/rstb.1999.0495}, number={1389}, journal={Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences}, publisher={The Royal Society}, author={Hochstrasser, M. and Johnson, P. R. and Arendt, C. S. and Amerik, A. Y. and Swaminathan, S. and Swanson, R. and Li, S. and Laney, J. and Pals-Rylaarsdam, R. and Nowak, J. and Connerly, P. L.}, editor={Hunt, R. T. and Nasmyth, K. A. and Diffley, J.}, year={1999}, month=sep, pages={1513–1522} }

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