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• W1516481845 abstract "Ubiquitin-Proteasome System (UPS) mediated proteolysis of an array of cellular proteins plays an important role in many basic physiological processes. Among these are control of cell cycle and division, differentiation and development, response to stress, transcriptional regulation, circadian rhythms, regulation of the immune and inflammatory responses, and biogenesis of organelles. Some of the well-known substrates of this system are cell cycle regulators such as cyclins, cyclin dependent kinase inhibitors, and proteins involved in sister chromatid separation, tumor suppressors, as well as transcriptional activators and their inhibitors [Glickman, 2002; Hilt, 2004; Wolf, D.H, 2004]. Due to these facts, identification and characterization of new substrates of the ubiquitin-proteasome system is important to reveal its cellular functions. For this purpose a high expression lethality [HEL] screen had been developed [Ledig, 1996; Velten, 1996, Velten, 2000]. This screen was based on the hypothesis that overexpression of a protein whose degradation by the ubiquitin-proteasome system is required for viability or growth, will cause a strong growth defect in cells where proteasome function is impaired, as for instance in pre1-1 pre4-1 mutants. An unknown protein originally designated as Hel48 now commonly termed as Far10 was identified, [Velten, 2000; Kemp and Sprague, Jr., 2003]. In this work cycloheximide chase experiments were undertaken to prove that Far10 is a novel substrate of the proteasome. Far10 expressed from its endogenous promoter on the chromosome either as N-terminally 19Myc tagged or as C-terminally 3Ha-tagged version was rapidly degraded in wild type cells and stabilized in pre1-1 pre4-1 proteosome mutants. Based on the ability of HA-tagged Far10 to cause lethality it was concluded that the tagged version of this protein is functional. Therefore the degradation rates seen with different tagged versions are supposed to be as wild type. The identical behavior of N-terminally and C-terminally tagged Far10 strongly support this idea. Regulatory proteolysis is an important mechanism for major cell cycle transitions such as the initiation of DNA replication, separation of sister chromatids and exit from mitosis [Jan-Michael Peters, 1998; Hilt, 2004]. APC, an ubiquitin-protein ligase, consisting of 12 known subunits in Saccharomyces cerevisiae is essential for ubiquitindependent proteolysis during mitosis [Harper et al., 2002; Jan-Michael Peters, 2002]. It" @default.
• W1516481845 created "2016-06-24" @default.
• W1516481845 creator A5032425966 @default.
• W1516481845 date "2005-01-01" @default.
• W1516481845 modified "2023-09-24" @default.
• W1516481845 title "The novel proteasomal substrate Far10 contributes to control of mitotic exit in yeast" @default.
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• W1516481845 doi "https://doi.org/10.18419/opus-794" @default.
• W1516481845 hasPublicationYear "2005" @default.
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