NMR structure and comparison of the archaeal histone HFoB from the mesophile Methanobacterium formicicum with HMfB from the hyperthermophile Methanothermus fervidus.
NMR structure and comparison of the archaeal histone HFoB from the mesophile Methanobacterium formicicum with HMfB from the hyperthermophile Methanothermus fervidus.
复制标题
来自嗜温甲酸甲烷杆菌的古菌组蛋白 HFoB 与来自超嗜热菌 Methanothermus fervidus 的 HMfB 的 NMR 结构和比较。
DOI：
10.1021/bi973007a
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发表时间：
1998
期刊：
影响因子：
--
通讯作者：
Summers,MF
中科院分区：
文献类型：
--
作者：
Zhu,W;Sandman,K;Lee,GE;Reeve,JN;Summers,MF
重组古菌组蛋白rHFoB，从mesophileMethanobacteriumformicicicum的溶液状态的结构，已被确定的二维和三维（3D）的质子同源相关的核磁共振（NMR）方法。基于951核Overhauser效应（NOE）衍生的距离限制，rHFoB单体形成组蛋白折叠并组装成对称的（rHFoB）2二聚体，其结构与组装成古细菌核小体一致。rHFoB与来自超嗜热甲烷热菌的rHMfB具有约78%的序列同源性，所获得的结果表明这两种蛋白质具有非常相似的三维结构，骨架原子的均方根偏差为0.65 ± 0.13 μ 2。然而，（rHFoB）2二聚体在较低的温度下展开，并且需要比（rHMfB）2二聚体更高的盐环境来稳定，并且比较结构，我们预测这些差异是由于不利的表面离子相互作用和（rHFoB）2疏水核心中邻近残基G36的更大、更溶剂可及的空腔造成的。
The solution-state structure of the recombinant archaeal histone rHFoB, from the mesophileMethanobacteriumformicicum, has been determined by two- and three-dimensional (3D) proton homonuclear correlated nuclear magnetic resonance (NMR) methods. On the basis of 951 nuclear Overhauser effect (NOE)-derived distance restraints, rHFoB monomers form the histone fold and assemble into symmetric (rHFoB)2dimers that have a structure consistent with assembly into archaeal nucleosomes. rHFoB exhibits ∼78% sequence homology with rHMfB from the hyperthermophileMethanothermus fervidus, and the results obtained demonstrate that these two proteins have very similar 3D structures, with a root-mean-square deviation for backbone atoms of 0.65 ± 0.13 Å2. (rHFoB)2dimers however unfold at lower temperatures and require a higher salt environment for stability than (rHMfB)2dimers, and comparing the structures, we predict that these differences result from unfavorable surface-located ionic interactions and a larger, more solvent-accessible cavity adjacent to residue G36 in the hydrophobic core of (rHFoB)2.