9B9R
Cryo-EM structure of the ZBTB5 BTB domain filament
Summary for 9B9R
| Entry DOI | 10.2210/pdb9b9r/pdb |
| EMDB information | 44389 |
| Descriptor | Zinc finger and BTB domain-containing protein 5 (1 entity in total) |
| Functional Keywords | btb domain, transcription factor, zbtb protein, transcription |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 4 |
| Total formula weight | 75145.30 |
| Authors | |
| Primary citation | Park, P.M.C.,Park, J.,Brown, J.,Hunkeler, M.,Roy Burman, S.S.,Donovan, K.A.,Yoon, H.,Nowak, R.P.,Slabicki, M.,Ebert, B.L.,Fischer, E.S. Polymerization of ZBTB transcription factors regulates chromatin occupancy. Mol.Cell, 84:2511-2524.e8, 2024 Cited by PubMed Abstract: BCL6, an oncogenic transcription factor (TF), forms polymers in the presence of a small-molecule molecular glue that stabilizes a complementary interface between homodimers of BCL6's broad-complex, tramtrack, and bric-à-brac (BTB) domain. The BTB domains of other proteins, including a large class of TFs, have similar architectures and symmetries, raising the possibility that additional BTB proteins self-assemble into higher-order structures. Here, we surveyed 189 human BTB proteins with a cellular fluorescent reporter assay and identified 18 ZBTB TFs that show evidence of polymerization. Through biochemical and cryoelectron microscopy (cryo-EM) studies, we demonstrate that these ZBTB TFs polymerize into filaments. We found that BTB-domain-mediated polymerization of ZBTB TFs enhances chromatin occupancy within regions containing homotypic clusters of TF binding sites, leading to repression of target genes. Our results reveal a role of higher-order structures in regulating ZBTB TFs and suggest an underappreciated role for TF polymerization in modulating gene expression. PubMed: 38996460DOI: 10.1016/j.molcel.2024.06.010 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.7 Å) |
Structure validation
Download full validation report
