Assembly of the Complex between Archaeal RNase P Proteins RPP30 and Pop5

@inproceedings{Crowe2011AssemblyOT,
  title={Assembly of the Complex between Archaeal RNase P Proteins RPP30 and Pop5},
  author={Brandon L. Crowe and Christopher J. Bohlen and Ross C Wilson and Venkat Gopalan and Mark P. Foster},
  booktitle={Archaea},
  year={2011}
}
RNase P is a highly conserved ribonucleoprotein enzyme that represents a model complex for understanding macromolecular RNA-protein interactions. Archaeal RNase P consists of one RNA and up to five proteins (Pop5, RPP30, RPP21, RPP29, and RPP38/L7Ae). Four of these proteins function in pairs (Pop5-RPP30 and RPP21-RPP29). We have used nuclear magnetic resonance (NMR) spectroscopy and isothermal titration calorimetry (ITC) to characterize the interaction between Pop5 and RPP30 from the… CONTINUE READING

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