6N2G
Crystal structure of Caenorhabditis elegans NAP1
Summary for 6N2G
Entry DOI | 10.2210/pdb6n2g/pdb |
Descriptor | Nucleosome Assembly Protein (1 entity in total) |
Functional Keywords | nucleosome assembly, histone binding, chaperone |
Biological source | Caenorhabditis elegans |
Total number of polymer chains | 4 |
Total formula weight | 142826.84 |
Authors | Bhattacharyya, S.,DArcy, S. (deposition date: 2018-11-13, release date: 2019-01-30, Last modification date: 2024-03-13) |
Primary citation | Sarkar, P.,Zhang, N.,Bhattacharyya, S.,Salvador, K.,D'Arcy, S. Characterization of Caenorhabditis elegans Nucleosome Assembly Protein 1 Uncovers the Role of Acidic Tails in Histone Binding. Biochemistry, 58:108-113, 2019 Cited by PubMed Abstract: Nucleosome assembly proteins (Naps) influence chromatin dynamics by directly binding to histones. Here we provide a comprehensive structural and biochemical analysis of a Nap protein from Caenorhabditis elegans (CeNap1). CeNap1 naturally lacks the acidic N-terminal tail and has a short C-terminal tail compared to many other Nap proteins. Comparison of CeNap1 with full length and tail-less constructs of Saccharomyces cerevisiae Nap1 uncovers the role of these tails in self-association, histone binding, and Nap competition with DNA for H2A-H2B. We find that the presence of tails influences the stoichiometry of H2A-H2B binding and is required to complete the interactions between H2A-H2B and DNA. The absolute stoichiometry of the Nap protein and H2A-H2B complex is 2:1 or 2:2, with only a very small population of higher-order oligomers occurring at 150 mM NaCl. We also show that H3-H4 binds differently than H2A-H2B and that an (H3-H4) tetramer can simultaneously bind two Nap protein homodimers. PubMed: 30521320DOI: 10.1021/acs.biochem.8b01033 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.003 Å) |
Structure validation
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