The Saccharomyces cerevisiae ubiquitin-proteasome system

Mark Hochstrasser, Phoebe R. Johnson, Cassandra S. Arendt, Alexander Yu Amerik, Sowmya Swaminathan, Robert Swanson, Shyr Jiann Li, Jeffrey D Laney, Robin Pals-Rylaarsdam, Jonathan Nowak, Pamela L. Connerly

Research output: Contribution to journalArticle

22 Citations (Scopus)

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 in a/α-diploid cells by heterodimer formation between the α2 and a1 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 dynamic in vivo, and our studies of yeast de-ubiquitinating enzymes illustrate how such enzymes can facilitate the proteolysis of diverse substrates.

Original languageEnglish (US)
Pages (from-to)1513-1522
Number of pages10
JournalPhilosophical transactions of the Royal Society of London. Series B: Biological sciences
Volume354
Issue number1389
StatePublished - Sep 29 1999
Externally publishedYes

Fingerprint

proteasome endopeptidase complex
Proteasome Endopeptidase Complex
ubiquitin
Ubiquitin
Yeast
Saccharomyces cerevisiae
Yeasts
Proteolysis
Degradation
protein
degradation
yeast
yeasts
proteolysis
Ubiquitin-Conjugating Enzymes
Homeodomain Proteins
enzyme
Proteins
Ubiquitination
Haploidy

Keywords

  • Mating type
  • Proteasome
  • Proteolysis
  • Ubiquitin
  • Yeast

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)
  • Agricultural and Biological Sciences (miscellaneous)

Cite this

Hochstrasser, M., Johnson, P. R., Arendt, C. S., Amerik, A. Y., Swaminathan, S., Swanson, R., ... Connerly, P. L. (1999). The Saccharomyces cerevisiae ubiquitin-proteasome system. Philosophical transactions of the Royal Society of London. Series B: Biological sciences, 354(1389), 1513-1522.

The Saccharomyces cerevisiae ubiquitin-proteasome system. / Hochstrasser, Mark; Johnson, Phoebe R.; Arendt, Cassandra S.; Amerik, Alexander Yu; Swaminathan, Sowmya; Swanson, Robert; Li, Shyr Jiann; Laney, Jeffrey D; Pals-Rylaarsdam, Robin; Nowak, Jonathan; Connerly, Pamela L.

In: Philosophical transactions of the Royal Society of London. Series B: Biological sciences, Vol. 354, No. 1389, 29.09.1999, p. 1513-1522.

Research output: Contribution to journalArticle

Hochstrasser, M, Johnson, PR, Arendt, CS, Amerik, AY, Swaminathan, S, Swanson, R, Li, SJ, Laney, JD, Pals-Rylaarsdam, R, Nowak, J & Connerly, PL 1999, 'The Saccharomyces cerevisiae ubiquitin-proteasome system', Philosophical transactions of the Royal Society of London. Series B: Biological sciences, vol. 354, no. 1389, pp. 1513-1522.
Hochstrasser M, Johnson PR, Arendt CS, Amerik AY, Swaminathan S, Swanson R et al. The Saccharomyces cerevisiae ubiquitin-proteasome system. Philosophical transactions of the Royal Society of London. Series B: Biological sciences. 1999 Sep 29;354(1389):1513-1522.
Hochstrasser, Mark ; Johnson, Phoebe R. ; Arendt, Cassandra S. ; Amerik, Alexander Yu ; Swaminathan, Sowmya ; Swanson, Robert ; Li, Shyr Jiann ; Laney, Jeffrey D ; Pals-Rylaarsdam, Robin ; Nowak, Jonathan ; Connerly, Pamela L. / The Saccharomyces cerevisiae ubiquitin-proteasome system. In: Philosophical transactions of the Royal Society of London. Series B: Biological sciences. 1999 ; Vol. 354, No. 1389. pp. 1513-1522.
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