| | |  | | | | Record from Web of Science® | | | | | | |
| Regulation of transcription by ubiquitination without proteolysis: Cdc34/SCFMet30-mediated inactivation of the transcription factor Met4 |
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| Author(s): Kaiser P, Flick K, Wittenberg C, Reed SI |
| Source: CELL Volume: 102 Issue: 3 Pages: 303-314 Published: AUG 4 2000 |
| Times Cited: 151 References: 27 |
| Abstract: Polyubiquitination of proteins by Cdc34/SCF complexes targets them for degradation by the 26S proteasome. The essential F-box protein Met30 is the substrate recognition subunit of the ubiquitin ligase SCFMet30. The critical target of SCFMet30 is the transcription factor Met4, as deletion of MET4 suppresses the lethality of met30 mutants. Surprisingly, Met4 is a relatively stable protein and its abundance is not influenced by Met30. However, transcriptional repression of Met4 target genes correlates with Cdc34 /SCFMet30-dependent ubiquitination of Met4. Functionally, ubiquitinated Met4 associates with target promoters but fails to form functional transcription complexes. Our data reveal a novel proteolysis-independent function for Cdc34/SCF and indicate that ubiquitination of transcription factors can be utilized to directly regulate their activities. |
| Document Type: Article |
| Language: English |
| Reprint Address: Reed, SI (reprint author), Scripps Res Inst, MB7, La Jolla, CA USA |
Addresses:
1. Scripps Res Inst, La Jolla, CA USA |
| Publisher: CELL PRESS, 1050 MASSACHUSETTES AVE, CIRCULATION DEPT, CAMBRIDGE, MA 02138 USA |
| Subject Category: Biochemistry & Molecular Biology; Cell Biology |
| IDS Number: 342BP |
| ISSN: 0092-8674 |
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| | | | | | | | | Record from Web of Science® | | | | | | | | | |