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Journal of Biochemistry Advance Access originally published online on July 7, 2006
Journal of Biochemistry 2006 140(2):293-298; doi:10.1093/jb/mvj144
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© 2006 The Japanese Biochemical Society.

Regular Paper

Characterization of the Archaeal Ribonuclease P Proteins from Pyrococcus horikoshii OT3

Atsushi Terada, Takashi Honda, Hideo Fukuhara, Kazumasa Hada and Makoto Kimura*

Laboratory of Biochemistry, Department of Bioscience and Biotechnology, Faculty of Agriculture, Graduate School, Kyushu University, Hakozaki 6-10-1, Higashi-ku, Fukuoka 812-8581

* To whom corresponding should be addressed. Tel/Fax: +81-92-642-2853, E-mail: mkimura{at}agr.kyushu-u.ac.jp

Ribonuclease P (RNase P) is a ribonucleoprotein complex involved in the processing of the 5'-leader sequence of precursor tRNA (pre-tRNA). Our earlier study revealed that RNase P RNA (pRNA) and five proteins (PhoPop5, PhoRpp38, PhoRpp21, PhoRpp29, and PhoRpp30) in the hyperthermophilic archaeon Pyrococcus horikoshii OT3 reconstituted RNase P activity that exhibits enzymatic properties like those of the authentic enzyme. In present study, we investigated involvement of the individual proteins in RNase P activity. Two particles (R-3Ps), in which pRNA was mixed with three proteins, PhoPop5, PhoRpp30, and PhoRpp38 or PhoPop5, PhoRpp30, and PhoRpp21 showed a detectable RNase P activity, and five reconstituted particles (R-4Ps) composed of pRNA and four proteins exhibited RNase P activity, albeit at reduced level compared to that of the reconstituted particle (R-5P) composed of pRNA and five proteins. Time-course analysis of the RNase P activities of R-4Ps indicated that the R-4Ps lacking PhoPop5, PhoRpp21, or PhoRpp30 had virtually reduced activity, while omission of PhoRpp29 or PhoRpp38 had a slight effect on the activity. The results indicate that the proteins contribute to RNase P activity in order of PhoPop5 > PhoRpp30 > PhoRpp21 >> PhoRpp29 > PhoRpp38. It was further found that R-4Ps showed a characteristic Mg2+ ion dependency approximately identical to that of R-5P. However, R-4Ps had optimum temperature of around at 55°C which is lower than 70°C for R-5P. Together, it is suggested that the P. horikoshii RNase P proteins are predominantly involved in optimization of the pRNA conformation, though they are individually dispensable for RNase P activity in vitro.


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Home page
 Nucleic Acids ResHome page
N. Jarrous and R. Reiner
Human RNase P: a tRNA-processing enzyme and transcription factor
Nucleic Acids Res., June 28, 2007; 35(11): 3519 - 3524.
[Abstract] [Full Text] [PDF]


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