Kosaka Shunsuke, Hada Kazumasa, Nakashima Takashi, Kimura Makoto
Laboratory of Structural Biology, Graduate School of Systems Life Sciences, Kyushu University, Fukuoka, Japan.
Biosci Biotechnol Biochem. 2010;74(2):394-6. doi: 10.1271/bbb.90577. Epub 2010 Feb 7.
The activated structure of RNase P RNA (PhopRNA) in Pyrococcus horikoshii OT3 was characterized by circular dichroism (CD) and ultraviolet (UV) absorbance spectra. The results suggested that interaction of four RNase P proteins (PhoPop5, PhoRpp21, PhoRpp29, and PhoRpp30) with PhopRNA results in destabilization of base stacking in PhopRNA, whereas the addition of a fifth protein, PhoRpp38, increases base stacking in PhopRNA.
通过圆二色性（CD）和紫外（UV）吸收光谱对嗜热栖热菌OT3中核糖核酸酶P RNA（PhopRNA）的活化结构进行了表征。结果表明，四种核糖核酸酶P蛋白（PhoPop5、PhoRpp21、PhoRpp29和PhoRpp30）与PhopRNA的相互作用导致PhopRNA中碱基堆积的不稳定，而添加第五种蛋白PhoRpp38则增加了PhopRNA中的碱基堆积。
