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- Title
The Yeast Ubiquitin Protease, Ubp3p, Promotes Protein Stability.
- Authors
Brew, Christine T.; Huffaker, Tim C.
- Abstract
Stulp is a microtubule-associated protein required for spindle assembly. In this article we show that the temperature-sensitive stul-5 allele is synthetically lethal in combination with ubp3, gim1-gim5, and kem1 mutations. The primary focus of this article is on the stul-5 ubp3 interaction. Ubp3 is a deubiquitination enzyme and a member of a large family of cysteine proteases that cleave ubiquitin moieties from protein substrates. UBP3 is the only one of 16 UBP genes in yeast whose loss is synthetically lethal with stul-5. Stu1p levels in stul-5 cells are several-fold lower than the levels in wild-type cells and the stul-5 temperature sensitivity can be rescued by additional copies of stul-5. These results indicate that the priming, effect of the stul-5 mutation is to make the protein less stable. The levels of Stulp are even lower in ubp3Δ stu1-45 cells, suggesting that Ubp3p plays a role in promoting protein stability. We also found that ubp3Δ produces growth defects in combination with mutations in other genes that decrease protein stability. Overall, these data support the idea that Ubp3p has a general role in the reversal of protein ubiquitination.
- Subjects
TUBULINS; CYSTEINE proteinases; UBIQUITIN
- Publication
Genetics, 2002, Vol 162, Issue 3, p1079
- ISSN
0016-6731
- Publication type
Article
- DOI
10.1093/genetics/162.3.1079