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J Bacteriol. 1993 August; 175(16): 5043-5048

research-article

Characterization of the RNase P RNA of Sulfolobus acidocaldarius.

T E LaGrandeur, S C Darr, E S Haas and N R Pace

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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J Bacteriol. 1993 August; 175(16): 5043-5048

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