ROLE OF THE UBIQUITIN PROTEASOME SYSTEM IN REGULATED PROTEIN-DEGRADATION IN SACCHAROMYCES-CEREVISIAE/

Citation
Se. Smith et al., ROLE OF THE UBIQUITIN PROTEASOME SYSTEM IN REGULATED PROTEIN-DEGRADATION IN SACCHAROMYCES-CEREVISIAE/, Biological chemistry, 377(7-8), 1996, pp. 437-446
Citations number
108
Categorie Soggetti
Biology
Journal title
ISSN journal
14316730
Volume
377
Issue
7-8
Year of publication
1996
Pages
437 - 446
Database
ISI
SICI code
1431-6730(1996)377:7-8<437:ROTUPS>2.0.ZU;2-T
Abstract
Selective degradation of proteins in eukaryotes is mediated primarily by the ubiquitin system in conjunction with the 26S proteasome. The ye ast Saccharomyces cerevisiae has proved a powerful model system to stu dy protein degradation in vivo. Biochemical and genetic studies comple mented by the sequence analysis of the entire yeast genome have identi fied more than 70 genes presumed to function in the ubiquitin/proteaso me system. Moreover, a number of physiological substrates of the ubiqu itin system have been identified in yeast which are key regulatory pro teins involved in the control of the cell cycle and transcription. In this review we will describe the enzymes effecting ubiquitin-protein c onjugation and degradation. In addition we will discuss several target s of this system and describe the cellular functions mediated by this pathway.