In vitro interactions of histones and alpha-crystallin

被引：7
作者：
Hamilton, Paul D. [1 ]
Andley, Usha P. [1 ]
机构：
[1] Washington Univ, Sch Med, Dept Ophthalmol & Visual Sci, 660 South Euclid Ave,Campus Box 8096, St Louis, MO 63110 USA
来源：
BIOCHEMISTRY AND BIOPHYSICS REPORTS | 2018年 / 15卷
基金：
美国国家卫生研究院;
关键词：
Histone; Complex formation; Cataract; Crystallin;
D O I：
10.1016/j.bbrep.2018.05.005
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The aggregation of crystallins in lenses is associated with cataract formation. We previously reported that mutant crystallins are associated with an increased abundance of histones in knock-in and knockout mouse models. However, very little is known about the specific interactions between lens crystallins and histones. Here, we performed in vitro analyses to determine whether alpha-crystallin interacts with histones directly. Isothermal titration calorimetry revealed a strong histone-alpha-crystallin binding with a K-d of 4x10(-7) M, and the thermodynamic parameters suggested that the interaction was both entropy and enthalpy driven. Size-exclusion chromatography further showed that histone-alpha-crystallin complexes are water soluble but become water insoluble as the concentration of histones is increased. Right-angle light scattering measurements of the watersoluble fractions of histone-alpha-crystallin mixtures showed a decrease in the oligomeric molecular weight of alpha-crystallin, indicating that histones alter the oligomerization of alpha-crystallin. Taken together, these findings reveal for the first time that histones interact with and affect the solubility and aggregation of alpha-crystallin, indicating that the interaction between alpha-crystallin and histones in the lens is functionally important.
引用
收藏
页码：7 / 12
页数：6
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