Transformation by FosB requires a trans-activation domain missing in FosB2 that can be substituted by heterologous activation domains.

Abstract excerpt

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...

Topics

• Amino Acid Sequence
• Bacterial Proteins
• Blotting, Northern
• Cell Line, Transformed
• Chloramphenicol O-Acetyltransferase
• DNA-Binding Proteins
• Gene Expression
• Molecular Sequence Data
• Mutation
• Nucleic Acid Hybridization