Role of a ubiquitin-conjugating enzyme in degradation of S- and M-phase cyclins.
Seufert, Wolfgang; Futcher, Bruce; Jentsch, Stefan
[Letter]
Nature.
373(6509):78-81, January 5, 1995.
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Cell cycle progression in eukaryotes is controlled by the p34 sup cdc2/CDC28 protein kinase and its short-lived, phase-specific regulatory subunits called cyclins [1,2]. In Xenopus oocytes, degradation of M-phase (B-type) cyclins is required for exit from mitosis and is mediated by the ubiquitin-dependent proteolytic system [3]. Here we show that B-type-cyclin degradation in yeast involves an essential nuclear ubiquitin-conjugating enzyme, UBC9. Repression of UBC9 synthesis prevents cell cycle progression at the G2 or early M phase, causing the accumulation of large budded cells with a single nucleus, a short spindle and replicated DNA. In ubc9 mutants both CLB5, an S-phase cyclin [4,5], and CLB2, an M-phase cyclin [6,7], are stabilized. In wild-type cells the CLB5 protein is unstable throughout the cell cycle, whereas CLB2 turnover occurs only at a specific cell-cycle stage [8]. Thus distinct degradation signals or regulated interaction with the ubiquitin-protein ligase system may determine the cell-cycle specificity of cyclin proteolysis.
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