Abstract
Phylogenetic-comparative and mutational analyses were used to elucidate the structure of the catalytically active RNA component of eubacterial ribonuclease P (RNase P). In addition to the refinement and extension of known structural elements, the analyses revealed a long-range interaction that results in a second pseudoknot in the RNA. This feature strongly constrains the three-dimensional structure of RNase P RNA near the active site. Some RNase P RNAs lack this structure but contain a unique, possibly compensating, structural domain. This suggests that different RNA structures located at different positions in the sequence may have equivalent architectural functions in RNase P RNA.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Bacillus subtilis / enzymology
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Bacillus subtilis / genetics
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Base Composition
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Base Sequence
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Biological Evolution
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Endoribonucleases / genetics*
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Escherichia coli / enzymology
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Escherichia coli / genetics
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Escherichia coli Proteins*
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Models, Molecular
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Molecular Sequence Data
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Mutagenesis
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Nucleic Acid Conformation
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RNA, Bacterial / genetics*
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RNA, Catalytic / genetics*
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Ribonuclease P
Substances
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Escherichia coli Proteins
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RNA, Bacterial
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RNA, Catalytic
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Endoribonucleases
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Ribonuclease P
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ribonuclease P, E coli
Associated data
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GENBANK/M64708
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GENBANK/M64709
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GENBANK/M76239
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GENBANK/M76240
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GENBANK/M76241
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GENBANK/M76242
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GENBANK/M76243
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GENBANK/M76244
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GENBANK/M83742
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GENBANK/S70464