The Dynamic Network of RNP RNase P Subunits

Figure 1. Comparison of the RNase P structures, in complex with pre-tRNA from T. maritima (PDB ID: 3Q1R), M. jannaschii (PDB ID: 6K0B, edited to show the monomeric RNase P) and human (PDB ID: 6AHU). The structures were visualized using ChimeraX v1.2 [35].

Figure 2. Comparison of Cryo-EM structures of yeast (left, PDB ID: 6AGB) and human RNase P holoenzymes (right, PDB ID: 6AHR). The human holoenzyme has lost Pop8 found in yeast (light grey) and acquired Rpp14 (yellow) and hRpp40 (red). The black square indicates the corresponding site of human Rpp40 on the yeast holoenzyme. The structures were visualized using ChimeraX v1.2 [35].

Figure 3. Superposition of the RPP25 Cryo-EM structure (grey, PDB ID: 6AHU) with the RPP25-like structural prediction model obtained from the AlphaFold database (light blue, Uniprot ID: Q8N5L8). The comparison was visualized using the Matchmaker tool in ChimeraX v1.2 [35].

Figure 4. Cryo-EM structure of human mt-RNase P bound to mt-tRNATyr as it was deposited in PDB (PDB ID: 7ONU). The structures were visualized using ChimeraX v1.2 [35].

Figure 5. (a) Protein–protein interaction network of RNase P subunits; (b) gene ontology enrichment analysis on the RNase P subunits’ interactants. The protein–protein interactions of each RNase P protein subunit were retrieved from PICKLE (Protein InteraCtion KnowLedgebasE) and illustrated, using Cytoscape v3.8.2 [111,112]. Gene ontology enrichment analysis was performed, using the PANTHER classification system, and P-values were subjected to Bonferroni correction for multiple testing [113].