A conserved RNA motif involved in divalent cation utilization by nuclear RNase P

Catalytic RNAs are metalloenzymes that require precise coordination of divalent cation cofactors. In RNase P RNA, a conserved structural subdomain that has been implicated in magnesium coordination contains the consensus sequence acAGaRA. Randomization mutagenesis of the analogous sequence in the Sa...

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Bibliographic Details
Published in:RNA (Cambridge) 1996-11, Vol.2 (11), p.1100-1109
Main Authors: Pagán-Ramos, E, Lee, Y, Engelke, D R
Format: Article
Language:English
Subjects:
Base Sequence
Catalysis
Conserved Sequence
Endoribonucleases - genetics
Endoribonucleases - metabolism
Escherichia coli - genetics
Escherichia coli - metabolism
Escherichia coli Proteins
Evolution, Molecular
Genes, Fungal
Kinetics
Magnesium - metabolism
Molecular Sequence Data
Mutagenesis
Nucleic Acid Conformation
Ribonuclease P
RNA Processing, Post-Transcriptional
RNA, Catalytic - genetics
RNA, Catalytic - metabolism
RNA, Fungal - chemistry
RNA, Fungal - genetics
RNA, Fungal - metabolism
Saccharomyces cerevisiae
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - metabolism
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Summary:Catalytic RNAs are metalloenzymes that require precise coordination of divalent cation cofactors. In RNase P RNA, a conserved structural subdomain that has been implicated in magnesium coordination contains the consensus sequence acAGaRA. Randomization mutagenesis of the analogous sequence in the Saccharomyces cerevisiae nuclear RNase P RNA gene, RPR1, gave viable sequence variants that confer magnesium-correctable growth defects and are defective in magnesium cofactor utilization by the RNase P holoenzyme in vitro. Kinetic analysis of the defective holoenzymes suggests that the primary effects were on catalytic rate, rather than substrate recognition. The possible involvement of this RNA subdomain in catalysis is discussed.
ISSN:1355-8382
1469-9001