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Characterization of the RNase P RNA of Sulfolobus acidocaldarius.

Department of Biology, Indiana University, Bloomington 47405.

ABSTRACT

RNase P is the ribonucleoprotein enzyme that cleaves precursor sequences from the 5' ends of pre-tRNAs. In Bacteria, the RNA subunit is the catalytic moiety. Eucaryal and archaeal RNase P activities copurify with RNAs, which have not been shown to be catalytic. We report here the analysis of the RNase P RNA from the thermoacidophilic archaeon Sulfolobus acidocaldarius. The holoenzyme was highly purified, and extracted RNA was used to identify the RNase P RNA gene. The nucleotide sequence of the gene was determined, and a secondary structure is proposed. The RNA was not observed to be catalytic by itself, but it nevertheless is similar in sequence and structure to bacterial RNase P RNA. The marked similarity of the RNase P RNA from S. acidocaldarius and that from Haloferax volcanii, the other known archael RNase P RNA, supports the coherence of Archaea as a phylogenetic domain.

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• Russell, A. G., Ebhardt, H., Dennis, P. P. (1999). Substrate Requirements for a Novel Archaeal Endonuclease That Cleaves Within the 5' External Transcribed Spacer of Sulfolobus acidocaldarius Precursor rRNA. Genetics 152: 1373-1385 [Abstract] [Full Text]  
• Pannucci, J. A., Haas, E. S., Hall, T. A., Harris, J. K., Brown, J. W. (1999). RNase P RNAs from some Archaea are catalytically active. Proc. Natl. Acad. Sci. USA 96: 7803-7808 [Abstract] [Full Text]  
• Lygerou, Z, Mitchell, P, Petfalski, E, Seraphin, B, Tollervey, D (1994). The POP1 gene encodes a protein component common to the RNase MRP and RNase P ribonucleoproteins.. Genes Dev. 8: 1423-1433 [Abstract]