Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.


Sci. STKE, 8 August 2000
Vol. 2000, Issue 44, p. tw1
[DOI: 10.1126/stke.2000.44.tw1]

EDITORS' CHOICE

Transcription Regulation by Ubiquitination Without Degradation

Ubiquitination is best known for tagging proteins for degradation by the proteasome. SCF complexes are involved in conferring substrate specificity to the E2 ubiquitin-conjugating enzymes. MET genes are involved in the regulation of methionine metabolism in yeast. Kaiser et al. used a genetic approach to determine that cell-cycle arrest in met30 mutants was due to hyperactivity of the Met4 transcription factor. Met30 is part of an SCF complex, and Met30 was required for ubiquitination of Met4; however, the stability of Met4 was unaffected by this posttranslational modification. Chromatin precipitation assays indicate that Met4 is constitutively associated with its target promoters, but that the ubiquitination of Met4 regulates its interaction with the transcription factor Cbf1. Thus, ubiquitination of Met4 is promoted by SCFMet30, which, instead of leading to its degradation, alters the transcriptional activity of Met4 by inhibiting its ability to recruit a second transcriptional regulator, Cbf1.

Kaiser, P., Flick, K., Wittenberg, C., and Reed, S. I. (2000) Regulation of transcription by ubiquitination without proteolysis: Cdc34/SCFMet30-mediated inactivation of the transcription factor Met4. Cell 102: 303-314. [Online Journal]

Citation: Regulation by Ubiquitination Without Degradation. Sci. STKE 2000, tw1 (2000).



To Advertise     Find Products


Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882