A Novel, Transformation-Relevant Activation Domain in Fos Proteins
| Autor: | Rolf Müller, Valérie Jérôme, M. Funk, B. Poensgen, W. Graulich |
|---|---|
| Rok vydání: | 1997 |
| Předmět: |
Transcriptional Activation
Recombinant Fusion Proteins Molecular Sequence Data Saccharomyces cerevisiae Moloney murine sarcoma virus Biology Cell Line Mice Transactivation Transcription (biology) Animals Amino Acid Sequence Molecular Biology Peptide sequence chemistry.chemical_classification Oncogene Proteins v-fos C-terminus Genetic Complementation Test Genes fos 3T3 Cells Cell Biology biology.organism_classification Molecular biology Rats Amino acid Cell biology Cell Transformation Neoplastic chemistry Mutation Transcription preinitiation complex Neoplastic Stem Cells Proto-Oncogene Proteins c-fos Research Article |
| Zdroj: | Molecular and Cellular Biology. 17:537-544 |
| ISSN: | 1098-5549 |
| DOI: | 10.1128/mcb.17.2.537 |
| Popis: | We have previously demonstrated that transformation by Fos is critically dependent on an intact DNA-binding domain (bZip) and a functional N-terminal transactivation motif (N-TM). We now show that a novel motif (C-terminal transactivation motif [C-TM]) near the C terminus also plays an important role in both transformation and the activation of AP1-dependent transcription and that the hydrophobic amino acids in the C-TM are functionally essential. The C-TM is the most crucial element in the C-terminal transactivation domain in Fos, as indicated by its relative strength and context-independent function. The C-TM is clearly different from the previously identified HOB2 domain, located N terminally to the C-TM, and the C-terminally positioned TATA-binding protein-binding domain. We also show that the C-terminal transactivation domain strongly synergizes with the HOB1-like N-TM, even when both domains are present on different proteins within a dimeric complex, and that the C-TM plays a crucial role in this cooperation. These observations can be corroborated in a model in which multiple contacts with the basal machinery are established either to stabilize the transcription complex or to facilitate its sequential assembly. |
| Databáze: | OpenAIRE |
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