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-Structure paper
| Title | Modular architecture of eukaryotic RNase P and RNase MRP revealed by electron microscopy. |
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| Journal, issue, pages | Nucleic Acids Res, Vol. 40, Issue 7, Page 3275-3288, Year 2012 |
| Publish date | Dec 13, 2011 |
 Authors | Katharina Hipp / Kyriaki Galani / Claire Batisse / Simone Prinz / Bettina Böttcher /  |
| PubMed Abstract | Ribonuclease P (RNase P) and RNase MRP are closely related ribonucleoprotein enzymes, which process RNA substrates including tRNA precursors for RNase P and 5.8 S rRNA precursors, as well as some ...Ribonuclease P (RNase P) and RNase MRP are closely related ribonucleoprotein enzymes, which process RNA substrates including tRNA precursors for RNase P and 5.8 S rRNA precursors, as well as some mRNAs, for RNase MRP. The structures of RNase P and RNase MRP have not yet been solved, so it is unclear how the proteins contribute to the structure of the complexes and how substrate specificity is determined. Using electron microscopy and image processing we show that eukaryotic RNase P and RNase MRP have a modular architecture, where proteins stabilize the RNA fold and contribute to cavities, channels and chambers between the modules. Such features are located at strategic positions for substrate recognition by shape and coordination of the cleaved-off sequence. These are also the sites of greatest difference between RNase P and RNase MRP, highlighting the importance of the adaptation of this region to the different substrates. |
 External links | Nucleic Acids Res / PubMed:22167472 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 15.0 - 17.0 Å |
| Structure data |  EMDB-1928:  EMDB-1929: |
| Source |
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Saccharomyces cerevisiae (brewer's yeast)