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RNA 96 (the RNA Society), May 28 - June 2 1996, Madison, WI
RNase P RNA structure in Archaea
J. Brown1, E. Haas1, D. Armbruster2, B. Vucson1, and C. Daniels2
1Department of Microbiology, North Carolina State University,
Raleigh, NC 27695 USA
2Department of Microbiology, The Ohio State University, Columbus, OH
43210 USA
Although the structure of the catalytic RNA component of ribonuclease
P has been well characterized in Bacteria, it has been little studied
in other organisms such as the Archaea. We have determined the
sequences encoding RNase P RNA in eight euryarchaeal species:
Halococcus morrhuae, Natronobacterium gregoryi, Halobacterium
cutirubrum, Halobacterium trapanicum, Methanobacterium
thermoautotrophicum strains deltaH and Marburg, Methanothermus
fervidus, and Thermococcus celer strain AL-1. On the basis
of these and previously available sequences from Sulfolobus
acidocaldarius, Haloferax volcanii and Methanosarcina
barkeri, the secondary structure of RNase P RNA in Archaea has
been analyzed by phylogenetic comparative analysis.
The archaeal RNAs are similar in both primary and secondary structure
to bacterial RNase P RNAs, but unlike their bacterial counterparts
these archaeal RNase P RNAs are not by themselves catalytically
proficient in vitro. Of the 39 nucleotides that are invariant in
bacterial RNase P RNA sequences, 32 (89%) are also present in the
archaeal RNAs. The archaeal consensus secondary structure contains
all but one helix present in the bacterial consensus structure, the
2bp helix P11. P18, present in nearly all bacterial RNase P RNAs and
known to be involved in stabilizing the structure of the RNA, is also
absent in all of the archaeal RNase P RNAs. The structure of the
P15/P16 region, known to be important in substrate recognition and
highly conserved in the bacterial RNAs, is quite variable in the
archaeal RNAs, although in some instances it conforms to the
bacterial consensus. The structural basis for the absolute dependence
of the archaeal RNase P RNAs on (presumably) protein for function is
not obvious from the primary or secondary structures of these
RNAs.
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