5JBM
Crystal structgure of Cac1 C-terminus
Summary for 5JBM
| Entry DOI | 10.2210/pdb5jbm/pdb |
| Descriptor | Chromatin assembly factor 1 subunit p90 (2 entities in total) |
| Functional Keywords | nucleosome assembly, histone chaperone, caf-1, chaperone |
| Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Total number of polymer chains | 1 |
| Total formula weight | 16962.01 |
| Authors | Churchill, M.E.A.,Liu, W.,Zhou, Y. (deposition date: 2016-04-13, release date: 2016-10-26, Last modification date: 2023-09-27) |
| Primary citation | Liu, W.H.,Roemer, S.C.,Zhou, Y.,Shen, Z.J.,Dennehey, B.K.,Balsbaugh, J.L.,Liddle, J.C.,Nemkov, T.,Ahn, N.G.,Hansen, K.C.,Tyler, J.K.,Churchill, M.E. The Cac1 subunit of histone chaperone CAF-1 organizes CAF-1-H3/H4 architecture and tetramerizes histones. Elife, 5:-, 2016 Cited by PubMed Abstract: The histone chaperone Chromatin Assembly Factor 1 (CAF-1) deposits tetrameric (H3/H4) histones onto newly-synthesized DNA during DNA replication. To understand the mechanism of the tri-subunit CAF-1 complex in this process, we investigated the protein-protein interactions within the CAF-1-H3/H4 architecture using biophysical and biochemical approaches. Hydrogen/deuterium exchange and chemical cross-linking coupled to mass spectrometry reveal interactions that are essential for CAF-1 function in budding yeast, and importantly indicate that the Cac1 subunit functions as a scaffold within the CAF-1-H3/H4 complex. Cac1 alone not only binds H3/H4 with high affinity, but also promotes histone tetramerization independent of the other subunits. Moreover, we identify a minimal region in the C-terminus of Cac1, including the structured winged helix domain and glutamate/aspartate-rich domain, which is sufficient to induce (H3/H4) tetramerization. These findings reveal a key role of Cac1 in histone tetramerization, providing a new model for CAF-1-H3/H4 architecture and function during eukaryotic replication. PubMed: 27690308DOI: 10.7554/eLife.18023 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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