Published online 19 April 2004
Nucleic Acids Research, 2004, Vol. 32, No. 7 2138-2146
© 2004 Oxford University Press
Mutual interactions between subunits of the human RNase MRP ribonucleoprotein complex
Department of Biochemistry, Nijmegen Center for Molecular Life Sciences, University of Nijmegen, Nijmegen, The Netherlands
*To whom correspondence should be addressed at Department of Biochemistry 161, University of Nijmegen, PO Box 9101, NL-6500 HB Nijmegen, The Netherlands. Tel: +31 24 361 6847; Fax: +31 24 354 0525; Email: g.pruijn{at}ncmls.kun.nl
Received January 23, 2004; Revised and Accepted March 23, 2004
The eukaryotic ribonuclease for mitochondrial RNA processing (RNase MRP) is mainly located in the nucleoli and belongs to the small nucleolar ribonucleoprotein (snoRNP) particles. RNase MRP is involved in the processing of pre-rRNA and the generation of RNA primers for mitochondrial DNA replication. A closely related snoRNP, which shares protein subunits with RNase MRP and contains a structurally related RNA subunit, is the pre-tRNA processing factor RNase P. Up to now, 10 protein subunits of these complexes have been described, designated hPop1, hPop4, hPop5, Rpp14, Rpp20, Rpp21, Rpp25, Rpp30, Rpp38 and Rpp40. To get more insight into the assembly of the human RNase MRP complex we studied protein–protein and protein–RNA interactions by means of GST pull-down experiments. A total of 19 direct protein–protein and six direct protein–RNA interactions were observed. The analysis of mutant RNase MRP RNAs showed that distinct regions are involved in the direct interaction with protein subunits. The results provide insight into the way the protein and RNA subunits assemble into a ribonucleoprotein particle. Based upon these data a new model for the architecture of the human RNase MRP complex was generated.
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