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. 1993 Aug;175(16):5043–5048. doi: 10.1128/jb.175.16.5043-5048.1993

Characterization of the RNase P RNA of Sulfolobus acidocaldarius.

T E LaGrandeur 1, S C Darr 1, E S Haas 1, N R Pace 1
PMCID: PMC204970  PMID: 7688716

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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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