Heterodimerization of the human RNase P/MRP subunits Rpp20 and Rpp25 is a prerequisite for interaction with the P3 arm of RNase MRP RNA
Katherine LD Hands-Taylor, Luigi Martino, Renee Tata, Jeffrey J Babon, Tam T Bui, Alex F Drake, Rebecca L Beavil, Ger JM Pruijn, Paul R Brown, Maria R Conte
NUCLEIC ACIDS RESEARCH | OXFORD UNIV PRESS | Published : 2010
Rpp20 and Rpp25 are two key subunits of the human endoribonucleases RNase P and MRP. Formation of an Rpp20-Rpp25 complex is critical for enzyme function and sub-cellular localization. We present the first detailed in vitro analysis of their conformational properties, and a biochemical and biophysical characterization of their mutual interaction and RNA recognition. This study specifically examines the role of the Rpp20/Rpp25 association in the formation of the ribonucleoprotein complex. The interaction of the individual subunits with the P3 arm of the RNase MRP RNA is revealed to be negligible whereas the 1:1 Rpp20:Rpp25 complex binds to the same target with an affinity of the order of nM. T..View full abstract
Awarded by Medical Research Council
Awarded by MRC
The Wellcome Trust for the Biomolecular Centre for Molecular Spectroscopy (to M.R.C., A.F.D.); EPSRC-case PhD studentship (to K.L.D.H-T.). Funding for open access charge: The Wellcome Trust.