Ubiquitinylation of transcription factors c-Jun and c-Fos using reconstituted ubiquitinylating enzymes
| Autor: | David C.H. Yang, Tom Curran, P. Boon Chock, Maria-Luz Hermida-Matsumoto |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
Proteases
Proteasome Endopeptidase Complex Reticulocytes Macromolecular Substances Proto-Oncogene Proteins c-jun Ubiquitin-Protein Ligases Mutant Ubiquitin-Activating Enzymes Biochemistry Substrate Specificity Ligases Adenosine Triphosphate Ubiquitin Multienzyme Complexes Animals Humans Molecular Biology Transcription factor Ubiquitins chemistry.chemical_classification biology c-jun Cell Biology DNA-binding domain Recombinant Proteins Ubiquitin ligase Diphosphates Cysteine Endopeptidases Enzyme chemistry biology.protein Rabbits Proto-Oncogene Proteins c-fos Transcription Factors |
| Zdroj: | The Journal of biological chemistry. 271(9) |
| ISSN: | 0021-9258 |
| Popis: | Recombinant c-Jun and c-Fos were ubiquitinylated by the ubiquitin carrier enzymes E214k, E220k, or E232k in the presence of the ubiquitin-activating enzyme, E1. Addition of ubiquitin protein ligase E3 substantially enhanced the E214k-mediated ubiquitinylation of c-Jun and c-Fos. Truncated c-Jun and c-Fos mutant proteins including wbJun and wbFos were also ubiquitinylated under the same conditions, suggesting the sites of ubiquitinylation are located within the dimerization and DNA binding domains of c-Jun and c-Fos. The E3-dependent ubiquitinylation of c-Jun was inhibited upon the heterodimerization of c-Jun with c-Fos. Further addition of E220k significantly enhanced ubiquitinylation of c-Jun in the heterodimer suggesting a regulatory role of E220k. Polyubiquitinylated c-Jun, wbFos, and wbJun, but not E220k-ubiquitinylated c-Jun, were readily degraded by the ATP-dependent 26 S multicatalytic proteases. These results suggest that the temporal control of c-Jun and c-Fos may be regulated through the ubiquitinylation pathways, and the ubiquitinylation of c-Jun and c-Fos may in turn be regulated in response to the heterodimerization between them and the cooperation between E220k and E3 mediated polyubiquitinylation. |
| Databáze: | OpenAIRE |
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