Thermodynamic analysis of a multifunctional RNA-binding protein, PhoRpp38, in the hyperthermophilic archaeon Pyrococcus horikoshii OT3.
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.
Laboratory of Biochemistry, Department of Bioscience and Biotechnology, Graduate School, Faculty of Agriculture, Kyushu University, Fukuoka, Japan.
Kosuke
K
Oshima
Takashi
T
Nakashima
Yoshimitsu
Y
Kakuta
Kouhei
K
Tsumoto
Makoto
M
Kimura
D019843:Archaeal Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D001665:Binding Sites; D002151:Calorimetry; D018360:Crystallography, X-Ray; D024202:Electrophoretic Mobility Shift Assay; D006358:Hot Temperature; D055029:Inverted Repeat Sequences; D007700:Kinetics; D008969:Molecular Sequence Data; D009154:Mutation; D011485:Protein Binding; D043902:Pyrococcus horikoshii / Q000235:genetics / Q000378:metabolism*; D019642:RNA, Archaeal / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D043262:Ribonuclease P / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D013816:Thermodynamics
D019843:Archaeal Proteins; D019642:RNA, Archaeal; D043262:Ribonuclease P