Structural highlights
Publication Abstract from PubMedNucleosome 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 with full length and a tail-less constructs of Saccharomyces cerevisiae Nap1 (ScNap1) uncovers the role of these tails in self-association, histone-binding, and competing H2A-H2B from DNA. We find that the presence of tails influences the stoichiometry of H2A-H2B-binding and is required to compete 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 a (H3-H4)2 tetramer can simultaneously bind two Nap2 protein homodimers. Characterization of Caenorhabditis elegans Nucleosome Assembly Protein 1 Uncovers the Role of Acidic Tails in Histone Binding.,Sarkar P, Zhang N, Bhattacharyya S, Salvador K, D'Arcy S Biochemistry. 2018 Dec 6. doi: 10.1021/acs.biochem.8b01033. PMID:30521320[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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