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Nucleic Acids Research, 1993, Vol. 21, No. 3 671-679
© 1993

MOLECULAR BIOLOGY

Characterization of ribonuclease P RNAs from thermophilic bacteria

James W. Brown, Elizabeth S. Haas and Norman R. Pace*

Department of Biology and Institute for Molecular and Cellular Biology, IndianaUniversity Bloomington, IN 47401, USA

* To whom correspondence should be addressed

Received September 15, 1992. Revised December 18, 1992. Accepted December 18, 1992.

The catalytic RNA component of bacterial RNase P is responsible for the removal of 5' leader sequences from precursor tRNAs. As part of an on-going phylogenetic comparative characterization of bacterial RNase P, the genes encoding RNase P RNA from the thermophiles Thermotoga maritima, Thermotoga neapolitana, Thermus aquaticus, and a mesophilic relative of the latter, Deinococcus radiodurans, have been cloned and sequenced. RNAs transcribed from these genes in vitro are catalytically active in the absence of other components. Active holoenzymes have been reconstituted from the T.aquaticus and T.maritima RNAs and the protein component of RNase P from Escherichia coli. The RNase P RNAs of T.aquaticus and T.maritima, synthesized in vitro, were characterized biochemically and shown to be inherently resistent to thermal disruption. Several features of these RNAs suggest mechanisms contributing to thermostability. The new sequences provide correlations that refine the secondary structure model of bacterial RNase P RNA.


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