5EJO
Crystal structure of the winged helix domain in Chromatin assembly factor 1 subunit p90
Summary for 5EJO
| Entry DOI | 10.2210/pdb5ejo/pdb |
| Descriptor | Chromatin assembly factor 1 subunit p90 (2 entities in total) |
| Functional Keywords | chromatin assembly factor 1, winged helix domain, nucleosome assembly, nuclear protein |
| Biological source | Saccharomyces cerevisiae S288c (Baker's yeast) |
| Cellular location | Nucleus: Q12495 |
| Total number of polymer chains | 1 |
| Total formula weight | 10549.08 |
| Authors | |
| Primary citation | Zhang, K.,Gao, Y.,Li, J.,Burgess, R.,Han, J.,Liang, H.,Zhang, Z.,Liu, Y. A DNA binding winged helix domain in CAF-1 functions with PCNA to stabilize CAF-1 at replication forks Nucleic Acids Res., 44:5083-5094, 2016 Cited by PubMed Abstract: Chromatin assembly factor 1 (CAF-1) is a histone H3-H4 chaperone that deposits newly synthesized histone (H3-H4)2 tetramers during replication-coupled nucleosome assembly. However, how CAF-1 functions in this process is not yet well understood. Here, we report the crystal structure of C terminus of Cac1 (Cac1C), a subunit of yeast CAF-1, and the function of this domain in stabilizing CAF-1 at replication forks. We show that Cac1C forms a winged helix domain (WHD) and binds DNA in a sequence-independent manner. Mutations in Cac1C that abolish DNA binding result in defects in transcriptional silencing and increased sensitivity to DNA damaging agents, and these defects are exacerbated when combined with Cac1 mutations deficient in PCNA binding. Similar phenotypes are observed for corresponding mutations in mouse CAF-1. These results reveal a mechanism conserved in eukaryotic cells whereby the ability of CAF-1 to bind DNA is important for its association with the DNA replication forks and subsequent nucleosome assembly. PubMed: 26908650DOI: 10.1093/nar/gkw106 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.75 Å) |
Structure validation
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