Oshima Kosuke, Nakashima Takashi, Kakuta Yoshimitsu, Tsumoto Kouhei, Kimura Makoto
Laboratory of Biochemistry, Department of Bioscience and Biotechnology, Graduate School, Faculty of Agriculture, Kyushu University, Fukuoka, Japan.
Biosci Biotechnol Biochem. 2012;76(6):1252-5. doi: 10.1271/bbb.120272. Epub 2012 Jun 7.
The protein component PhoRpp38 of Pyrococcus horikoshii ribonuclease P (RNase P) is known to be a multifunctional RNA-binding protein. Previous biochemical data indicate that it binds to two stem-loops in RNase P RNA (PhopRNA). Thermodynamic analysis revealed that PhoRpp38 and PhopRNA interact with each other with an association constant (Ka) of 1.56×10(7) M(-1). It was further found that PhoRpp38 simultaneously binds two stem-loop structures in PhopRNA with approximately equal affinity. Crystals of PhoRpp38 in complex with the stem-loop were grown and diffracted to a resolution of 7.0 Å on a synchrotron X-ray source.
嗜热栖热菌核糖核酸酶P（RNase P）的蛋白质组分PhoRpp38是一种多功能RNA结合蛋白。先前的生化数据表明，它与RNase P RNA（PhopRNA）中的两个茎环结合。热力学分析显示，PhoRpp38和PhopRNA相互作用的缔合常数（Ka）为1.56×10⁷ M⁻¹。进一步发现，PhoRpp38以近似相等的亲和力同时结合PhopRNA中的两个茎环结构。PhoRpp38与茎环复合物的晶体得以生长，并在同步加速器X射线源上衍射至7.0 Å的分辨率。
