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Journal Article

Yeast ubiquitin-conjugating enzymes involved in selective protein degradation are essential for cell viability

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Seufert,  W
Jentsch Group, Friedrich Miescher Laboratory, Max Planck Society;

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Jentsch,  S
Jentsch Group, Friedrich Miescher Laboratory, Max Planck Society;

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Citation

Seufert, W., & Jentsch, S. (1991). Yeast ubiquitin-conjugating enzymes involved in selective protein degradation are essential for cell viability. Acta Biologica Hungarica, 42(1-3), 27-37.


Cite as: https://hdl.handle.net/21.11116/0000-000C-033F-B
Abstract
Ubiquitin-mediated proteolysis is a major pathway for selective protein degradation in eukaryotic cells. This proteolysis pathway involves the processive covalent attachment of ubiquitin to proteolytic substrates and their subsequent degradation by a specific ATP-dependent protease complex. We have cloned the genes and characterized the function of ubiquitin-conjugating enzymes (UBCs) from the yeast Saccharomyces cerevisiae. UBC1, UBC4 and UBC5 enzymes were found to mediate selective degradation of short-lived and abnormal proteins. These enzymes have overlapping functions and constitute a UBC subfamily essential for growth. UBC1 is specifically required at early stages of growth after germination of spores. UBC4 and UBC5 enzymes generate high molecular weight ubiquitin-protein conjugates and comprise a major ubiquitin-conjugation activity in yeast cells. Moreover, these enzymes are central components of the cellular stress response.