7PFA
Trinucleosome of the 4x197 nucleosome array containing H1
Summary for 7PFA
| Entry DOI | 10.2210/pdb7pfa/pdb |
| EMDB information | 13370 |
| Descriptor | Histone H3.2, Histone H4, Histone H2A type 1-B/E, ... (7 entities in total) |
| Functional Keywords | chromatin, nucleosome, linker histone, dna binding protein |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 28 |
| Total formula weight | 872744.64 |
| Authors | Dombrowski, M.,Cramer, P. (deposition date: 2021-08-11, release date: 2022-08-03, Last modification date: 2024-07-17) |
| Primary citation | Dombrowski, M.,Engeholm, M.,Dienemann, C.,Dodonova, S.,Cramer, P. Histone H1 binding to nucleosome arrays depends on linker DNA length and trajectory. Nat.Struct.Mol.Biol., 29:493-501, 2022 Cited by PubMed Abstract: Throughout the genome, nucleosomes often form regular arrays that differ in nucleosome repeat length (NRL), occupancy of linker histone H1 and transcriptional activity. Here, we report cryo-EM structures of human H1-containing tetranucleosome arrays with four physiologically relevant NRLs. The structures show a zig-zag arrangement of nucleosomes, with nucleosomes 1 and 3 forming a stack. H1 binding to stacked nucleosomes depends on the NRL, whereas H1 always binds to the non-stacked nucleosomes 2 and 4. Short NRLs lead to altered trajectories of linker DNA, and these altered trajectories sterically impair H1 binding to the stacked nucleosomes in our structures. As the NRL increases, linker DNA trajectories relax, enabling H1 contacts and binding. Our results provide an explanation for why arrays with short NRLs are depleted of H1 and suited for transcription, whereas arrays with long NRLs show full H1 occupancy and can form transcriptionally silent heterochromatin regions. PubMed: 35581345DOI: 10.1038/s41594-022-00768-w PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (9.7 Å) |
Structure validation
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