PUBLICATION
Inventory and analysis of the protein subunits of the ribonucleases P and MRP provides further evidence of homology between the yeast and human enzymes
- Authors
- Rosenblad, M.A., Lopez, M.D., Piccinelli, P., and Samuelsson, T.
- ID
- ZDB-PUB-060927-1
- Date
- 2006
- Source
- Nucleic acids research 34(18): 5145-5156 (Journal)
- Registered Authors
- Keywords
- none
- MeSH Terms
-
- Amino Acid Sequence
- Endoribonucleases/chemistry
- Endoribonucleases/classification*
- Endoribonucleases/genetics
- Fungal Proteins/chemistry
- Fungal Proteins/classification*
- Fungal Proteins/genetics
- Genomics
- Humans
- Molecular Sequence Data
- Phylogeny
- Protein Subunits/chemistry
- Protein Subunits/classification*
- Protein Subunits/genetics
- Ribonuclease P/chemistry
- Ribonuclease P/classification*
- Ribonuclease P/genetics
- Saccharomyces cerevisiae Proteins/chemistry
- Saccharomyces cerevisiae Proteins/classification
- Saccharomyces cerevisiae Proteins/genetics
- Sequence Alignment
- Sequence Analysis, RNA
- Sequence Homology, Amino Acid
- Yeasts/enzymology*
- PubMed
- 16998185 Full text @ Nucleic Acids Res.
Citation
Rosenblad, M.A., Lopez, M.D., Piccinelli, P., and Samuelsson, T. (2006) Inventory and analysis of the protein subunits of the ribonucleases P and MRP provides further evidence of homology between the yeast and human enzymes. Nucleic acids research. 34(18):5145-5156.
Abstract
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.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping