assembly of the complex between archaeal rnase p proteins rpp30 and pop5

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ID: 231861
2011
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Abstract
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 hyperthermophilic archaeon Pyrococcus furiosus (Pfu). NMR backbone resonance assignments of free RPP30 (25 kDa) indicate that the protein is well structured in solution, with a secondary structure matching that observed in a closely related crystal structure. Chemical shift perturbations upon the addition of Pop5 (14 kDa) reveal its binding surface on RPP30. ITC experiments confirm a net 1 : 1 stoichiometry for this tight protein-protein interaction and exhibit complex isotherms, indicative of higher-order binding. Indeed, light scattering and size exclusion chromatography data reveal the complex to exist as a 78 kDa heterotetramer with two copies each of Pop5 and RPP30. These results will inform future efforts to elucidate the functional role of the Pop5-RPP30 complex in RNase P assembly and catalysis.
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crowe2011archaeaassembly Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors ;Brandon L. Crowe;Christopher J. Bohlen;Ross C. Wilson;Venkat Gopalan;Mark P. Foster
Journal annals of nuclear energy
Year 2011
DOI
10.1155/2011/891531
URL
http://dx.doi.org/10.1155/2011/891531
Keywords
Microbiology

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