Thermodynamic stability of archaeal histones
Thermodynamic stability of archaeal histones
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DOI：
10.1021/bi973006i
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发表时间：
1998-07-28
期刊：
影响因子：
2.9
通讯作者：
Reeve, JN
中科院分区：
文献类型：
--
作者：
Li, WT;Grayling, RA;Reeve, JN
利用圆二色光谱（CD）和差示扫描量热法（DSC）测定了四种重组(r)古细菌组蛋白（来自中温菌甲酸甲烷杆菌的rHFoB，来自嗜热菌ferthanothermus fervidus和热球菌菌株GB-3a的rHMfA、rHMfB和rHPyAl）展开的温度、盐和pH依赖性。这些蛋白质的热展开是90%可逆的，具有浓度依赖的表观T-m值和不对称展开转变，这与组蛋白二聚体展开成两个随机线圈单体的两态展开模型很好地吻合。rHPyAl二聚体在无盐的情况下是稳定的，而rHMfA、rHMfB和rHFoB二聚体在20℃和pH 2下在含有
The temperature, salt, and pH dependencies of unfolding of four recombinant (r) archaeal histones (rHFoB from the mesophile Methanobacterium formicicum, and rHMfA, rHMfB, and rHPyAl from the hyperthermophiles Methanothermus fervidus and Pyrococcus strain GB-3a) have been determined by circular dichroism spectroscopy (CD) and differential scanning calorimetry (DSC). The thermal unfolding of these proteins is >90% reversible, with concentration-dependent apparent T-m values and asymmetric unfolding transitions that are fit well by a two-state unfolding model in which a histone dimer unfolds to two random coil monomers. rHPyAl dimers are stable in the absence of salt, whereas rHMfA, rHMfB, and rHFoB dimers unfold at 20 degrees C and pH 2 in solutions containing