Inventory and analysis of the protein subunits of the ribonucleases P and MRP provides further evidence of homology between the yeast and human enzymes.

• The RNases P and MRP are involved in tRNA and rRNA processing, respectively. Both enzymes in eukaryotes are composed of an RNA molecule and 9-12 protein subunits. Most of the protein subunits are shared between RNases P and MRP. We have here performed a computational analysis of the protein subunits in a broad range of eukaryotic organisms using profile-based searches and phylogenetic methods. A number of novel homologues were identified, giving rise to a more complete inventory of RNase P/MRP proteins. We present evidence of a relationship between fungal Pop8 and the protein subunit families Rpp14/Pop5 as well as between fungal Pop6 and metazoan Rpp25. These relationships further emphasize a structural and functional similarity between the yeast and human P/MRP complexes. We have also identified novel P and MRP RNAs and analysis of all available sequences revealed a K-turn motif in a large number of these RNAs. We suggest that this motif is a binding site for the Pop3/Rpp38 proteins and we discuss other structural features of the RNA subunit and possible relationships to the protein subunit repertoire.

Nyckelord

Amino Acid Sequence

Endoribonucleases

chemistry

classification

genetics

Fungal Proteins

chemistry

classification

genetics

Genomics

Humans

Molecular Sequence Data

Phylogeny

Protein Subunits

chemistry

classification

genetics

Ribonuclease P

chemistry

classification

genetics

Saccharomyces cerevisiae Proteins

chemistry

classification

genetics

Sequence Alignment

Sequence Analysis

RNA

Sequence Homology

Amino Acid

Yeasts

enzymology

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