Vps75 is a histone chaperone that interacts with the fungal-specific histone acetyltransferase Rtt109 and stimulates its acetylation activity on histone H3. Here we report the crystal structure of Vps75 of Candida albicans, one of the most common fungal pathogens. CaVps75 exists as a headphone-like dimer that forms a large negatively charged region on its concave side, showing the potential to bind positively charged regions of histones. The distal ends of the concave side of the CaVps75 dimer are positively charged and each has one more α helix than yeast Vps75. CaVps75 exhibits ionic strength- and concentration-dependent higher oligomerization in solution. In the crystal, two dimers are bound through electrostatic interactions between charged regions on the concave side of their earmuff domains, and this inter-dimer interaction differs from the currently known inter-dimer interactions of Vps75s. Our results will help to understand the role of Vps75 in C. albicans.

Vps75 是一种组蛋白伴侣，与真菌特异性组蛋白乙酰转移酶 Rtt109 相互作用并刺激其对组蛋白 H3 的乙酰化活性。在这里，我们报告了白色念珠菌 Vps75 的晶体结构，白色念珠菌是最常见的真菌病原体之一。Ca Vps75 以耳机状二聚体的形式存在，在其凹面形成一个大的带负电区域，显示出结合组蛋白带正电区域的潜力。Ca Vps75 二聚体的凹侧末端带正电荷，并且每个末端都比酵母 Vps75 多一个 α 螺旋。钙Vps75 在溶液中表现出离子强度和浓度依赖性较高的低聚。在晶体中，两个二聚体通过其耳罩域凹侧的带电区域之间的静电相互作用结合在一起，这种二聚体间的相互作用不同于目前已知的 Vps75s 的二聚体间相互作用。我们的结果将有助于了解 Vps75 在白色念珠菌中的作用。