Crystal structure and functional analysis of an archaeal chromatin protein alba from the hyperthermophilic archaeon Pyrococcus horikoshii OT3
Crystal structure and functional analysis of an archaeal chromatin protein alba from the hyperthermophilic archaeon Pyrococcus horikoshii OT3
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DOI：
10.1271/bbb.70639
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发表时间：
2008-03-01
影响因子：
1.6
通讯作者：
Kimura, Makoto
中科院分区：
文献类型：
--
作者：
Hada, Kazurriasa;Nakashima, Takashi;Kimura, Makoto
Alba蛋白（PhoAlba）的晶体结构从超嗜热古菌，Pyrococcus horikoshii OT 3，确定在2.8埃的分辨率。PhoAlba在结构上属于α/β蛋白，不仅与古细菌同源物相似，而且与RNA结合蛋白相似，包括来自嗜热脂肪芽孢杆菌的起始因子3（IF 3-C）的C末端一半、一种与细胞分裂有关的大肠杆菌蛋白（Yhhp）和一种功能未知的拟南芥蛋白。凝胶迁移实验发现，PhoAlba与堀越毕赤酵母中的核糖核酸酶P（RNase P）RNA（PhopRNA）和前tRNA（Tyr）都有相互作用。然而，添加PhoAlba的重构颗粒组成的PhopRNA和四个或五个蛋白质亚基的前tRNA加工活性或加工活性的最佳温度几乎没有影响。这些结果表明，PhoAlba对堀越伪君子核糖核酸酶P的催化活性贡献很小。
The crystal structure of the Alba protein (PhoAlba) from a hyperthermophilic archaeon, Pyrococcus horikoshii OT3, was determined at a resolution of 2.8 angstrom. PhoAlba structurally belongs to the alpha/beta proteins and is similar not only to archaeal homologues but also to RNA-binding proteins, including the C-terminal half of initiation factor 3 (IF3-C) from Bacillus stearothermophilus, an Esherichia coli protein implicated in cell division (Yhhp), and an Arabidopsis protein of unknown function. We found by gel shift assay that PhoAlba interacts with both ribonuclease P (RNase P) RNA (PhopRNA) and precursor-tRNA(Tyr), (pre-tRNA(Tyr)) in P. horikoshii. However, the addition of PhoAlba to reconstituted particles composed of PhopRNA and four or five protein subunits had little influence on either the pre-tRNA processing activity or the optimum temperature for the processing activity. These results suggest that PhoAlba contributes little to the catalytic activity of P. horikoshii RNase P.