A conserved RNA motif involved in divalent cation utilization by nuclear RNase P
Related Experiment Video
Updated: Nov 3, 2026

Isolation of Cognate RNA-protein Complexes from Cells Using Oligonucleotide-directed Elution
Published on: January 16, 2017
E Pagán-Ramos1, Y Lee, D R Engelke
1Department of Biological Chemistry, The University of Michigan, Ann Arbor 48109-0606, USA.
Abstract:
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.
Related Concept Videos
Conserved Binding Sites
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Conserved Binding Sites
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Conservation of Protein Domains Over Different Proteins
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Cis-regulatory Sequences
Cis-regulatory Sequences
Ribosomal RNA Synthesis
Ribosome biogenesis begins with the synthesis of 5S and 45S pre-rRNAs by distinct RNA polymerases. The primary transcripts are extensively processed and modified before they are bound and folded by ribosomal proteins and assembly factors,...

