Modular architecture of eukaryotic RNase P and RNase MRP revealed by electron microscopy
Name
Hipp-2012-Modular architecture.pdf
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10.32 MB
Format
Adobe PDF
Checksum (MD5)
44da12bd634db5b7fa60efd0627144c2
Author(s)
Hipp, Katharina
Galani, Kyriakitsa
Batisse, Claire
Prinz, Simone
Bottcher, Bettina
Date Issued
December 2011
Journal
Nucleic Acids Research
Publisher
Oxford University Press (OUP)
Citation
Hipp, K. et al. “Modular Architecture of Eukaryotic RNase P and RNase MRP Revealed by Electron Microscopy.” Nucleic Acids Research 40.7 (2011): 3275–3288.
Version
Final published version
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 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.
MIT Department
Massachusetts Institute of Technology. Department of Biology
Terms of Use
Creative Commons Attribution Non-Commercial
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DOI of Published Version
https://doi.org/10.1093/nar/gkr1217
