Transformation by FosB requires a trans-activation domain missing in FosB2 that can be substituted by heterologous activation domains
| Autor: | R Wisdom, D Rashid, Inder M. Verma, J Yen |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
Chloramphenicol O-Acetyltransferase
Transcriptional Activation Proto-Oncogene Proteins c-jun Molecular Sequence Data Gene Expression Biology Transfection medicine.disease_cause chemistry.chemical_compound Bacterial Proteins Genetics medicine Amino Acid Sequence Gene Cell Line Transformed chemistry.chemical_classification Mutation Alternative splicing Nucleic Acid Hybridization Blotting Northern Precipitin Tests Amino acid Cell biology DNA-Binding Proteins Transformation (genetics) Biochemistry chemistry Transcription preinitiation complex RNA DNA Plasmids Developmental Biology FOSB |
| Zdroj: | Genes & Development. 6:667-675 |
| ISSN: | 1549-5477 0890-9369 |
| DOI: | 10.1101/gad.6.4.667 |
| Popis: | Two functionally distinct proteins derived from the FosB gene by alternative splicing have recently been described. FosB protein transforms fibroblasts efficiently, whereas FosB2 protein, a carboxy-terminally truncated form of FosB, does not, despite the fact that both proteins can participate in high-affinity, sequence-specific DNA binding as part of a heterodimeric complex with c-Jun protein. We show here that the functional difference between these proteins is the result of the presence of a potent proline-rich transcriptional activation domain in the carboxy-terminal amino acids unique to FosB. This conclusion is supported by three lines of evidence: (1) Mutations in the carboxy-terminal region of FosB that impair transcriptional activation also reduce transforming potential, despite the fact that DNA binding as part of a complex with c-Jun is not affected; (2) the carboxy-terminal region unique to FosB functions as an activation domain when fused to the DNA-binding domain of GAL4; and (3) transforming potential can be conferred on FosB2 by fusing any of several different well-characterized trans-activation domains. These results identify an additional functional requirement for transformation by Fos proteins and have implications for the mechanism(s) of mitogenic signaling by the AP-1 transcription complex. |
| Databáze: | OpenAIRE |
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