The Saccharomyces cerevisiae ubiquitin-proteasome system

被引:23
|
作者
Hochstrasser, M [1 ]
Johnson, PR [1 ]
Arendt, CS [1 ]
Amerik, AY [1 ]
Swaminathan, S [1 ]
Swanson, R [1 ]
Li, SJ [1 ]
Laney, J [1 ]
Pals-Rylaarsdam, R [1 ]
Nowak, J [1 ]
Connerly, PL [1 ]
机构
[1] Univ Chicago, Dept Biochem & Mol Biol, Chicago, IL 60637 USA
关键词
yeast; ubiquitin; proteasome; proteolysis; mating type;
D O I
10.1098/rstb.1999.0495
中图分类号
Q [生物科学];
学科分类号
07 ; 0710 ; 09 ;
摘要
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, MAT alpha 2. The alpha 2 protein is polyubiquitinated and rapidly degraded in alpha-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 alpha 2. Interestingly, degradation of alpha 2 is blocked in a/alpha-diploid cells by heterodimer formation between the alpha 2 and al homeodomain proteins. The data suggest that degradation signals may overlap protein-protein interaction surfaces, allowing a straightforward steric mechanism for regulated degradation. Analysis of alpha 2 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.
引用
收藏
页码:1513 / 1522
页数:10
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