The Histone Chaperones Vps75 and Nap1 Form Ring-like, Tetrameric Structures in Solution

Bowman A, et al., 42(9):6038-51, Nucleic Acids Res, 2014

Biochemical and biophysical techniques were used to examine the structure and function of Vps75 and related Nap 1, a yeast histone chaperone that forms homodimeric tetramers as part of its mechanism in regulating nucleosome assembly and disassembly as well as transcription. The Octet RED384 system was used to calculate the <em>K</em><sub>D</sub> for tetramerization formation. Streptavidin biosensors were used. A molecular model for Vps75/NAP1 was determined using pulse electron-electron double resonance (PELDOR), small angle X-ray scattering (SAXS), multi-angle light scattering (MALS) and structure-guided mutagenesis showing the protein forms discrete tetrameric conformation under physiological ionic conditions.

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