Mechanism of c-Myb–C/EBPβ Cooperation from Separated Sites on a Promoter
| Autor: | Shunsuke Ishii, Ko Sato, Hisayuki Morii, Shioka Takata, Atsushi Fujikawa, Motoko Sasaki, Takashi Kumasaka, Kazumi Kimura, Kazuhiro Ogata, Masaaki Shiina, Emi Ichikawa-Iwata, Tahir H. Tahirov, Masaki Yamamoto, Taiko Inoue-Bungo |
|---|---|
| Jazyk: | angličtina |
| Předmět: |
Transcriptional Activation
animal structures Molecular Sequence Data Crystal structure Biology General Biochemistry Genetics and Molecular Biology Proto-Oncogene Proteins c-myc chemistry.chemical_compound Structure-Activity Relationship Transcription (biology) Acetyltransferases Humans MYB Luciferase Amino Acid Sequence Promoter Regions Genetic Gene Binding Sites Crystallography Biochemistry Genetics and Molecular Biology(all) Point mutation CCAAT-Enhancer-Binding Protein-beta fungi Proteins Promoter Molecular biology Oncogene Proteins v-myb Protein Structure Tertiary chemistry Mutagenesis Nucleic Acid Conformation DNA |
| Zdroj: | Cell. (1):57-70 |
| ISSN: | 0092-8674 |
| DOI: | 10.1016/S0092-8674(01)00636-5 |
| Popis: | c-Myb, but not avian myeloblastosis virus (AMV) v-Myb, cooperates with C/EBP beta to regulate transcription of myeloid-specific genes. To assess the structural basis for that difference, we determined the crystal structures of complexes comprised of the c-Myb or AMV v-Myb DNA-binding domain (DBD), the C/EBP beta DBD, and a promoter DNA fragment. Within the c-Myb complex, a DNA-bound C/EBP beta interacts with R2 of c-Myb bound to a different DNA fragment; point mutations in v-Myb R2 eliminate such interaction within the v-Myb complex. GST pull-down assays, luciferase trans-activation assays, and atomic force microscopy confirmed that the interaction of c-Myb and C/EBP beta observed in crystal mimics their long range interaction on the promoter, which is accompanied by intervening DNA looping. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|