6Z0S
Allostery through DNA drives phenotype switching
Summary for 6Z0S
| Entry DOI | 10.2210/pdb6z0s/pdb |
| EMDB information | 11022 12260 |
| Descriptor | comG promoter DNA - strand A, comG promoter DNA - strand B (2 entities in total) |
| Functional Keywords | transcription-factor, dna-binding, a-tract, allostery, dna binding protein |
| Biological source | Bacillus subtilis More |
| Total number of polymer chains | 2 |
| Total formula weight | 57358.86 |
| Authors | Rosenblum, G.,Elad, N.,Rozenberg, H.,Wiggers, F.,Jungwirth, J.,Hofmann, H. (deposition date: 2020-05-11, release date: 2021-04-07, Last modification date: 2024-05-22) |
| Primary citation | Rosenblum, G.,Elad, N.,Rozenberg, H.,Wiggers, F.,Jungwirth, J.,Hofmann, H. Allostery through DNA drives phenotype switching. Nat Commun, 12:2967-2967, 2021 Cited by PubMed Abstract: Allostery is a pervasive principle to regulate protein function. Growing evidence suggests that also DNA is capable of transmitting allosteric signals. Yet, whether and how DNA-mediated allostery plays a regulatory role in gene expression remained unclear. Here, we show that DNA indeed transmits allosteric signals over long distances to boost the binding cooperativity of transcription factors. Phenotype switching in Bacillus subtilis requires an all-or-none promoter binding of multiple ComK proteins. We use single-molecule FRET to demonstrate that ComK-binding at one promoter site increases affinity at a distant site. Cryo-EM structures of the complex between ComK and its promoter demonstrate that this coupling is due to mechanical forces that alter DNA curvature. Modifications of the spacer between sites tune cooperativity and show how to control allostery, which allows a fine-tuning of the dynamic properties of genetic circuits. PubMed: 34016970DOI: 10.1038/s41467-021-23148-2 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (5.7 Å) |
Structure validation
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