Conserved and variable domains of RNase MRP RNA.

  • Dávila López M
  • Rosenblad M
  • Samuelsson T
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Abstract

Ribonuclease MRP is a eukaryotic ribonucleoprotein complex consisting of one RNA molecule and 7-10 protein subunits. One important function of MRP is to catalyze an endonucleolytic cleavage during processing of rRNA precursors. RNase MRP is evolutionary related to RNase P which is critical for tRNA processing. A large number of MRP RNA sequences that now are available have been used to identify conserved primary and secondary structure features of the molecule. MRP RNA has structural features in common with P RNA such as a conserved catalytic core, but it also has unique features and is characterized by a domain highly variable between species. Information regarding primary and secondary structure features is of interest not only in basic studies of the function of MRP RNA, but also because mutations in the RNA give rise to human genetic diseases such as cartilage-hair hypoplasia.

Author-supplied keywords

  • Animals
  • Endoribonucleases
  • Endoribonucleases: chemistry
  • Endoribonucleases: genetics
  • Endoribonucleases: metabolism
  • Evolution, Molecular
  • Genetic Variation
  • Humans
  • Nucleic Acid Conformation
  • Protein Binding
  • Ribonucleoproteins
  • Ribonucleoproteins: chemistry
  • Ribonucleoproteins: genetics
  • Ribonucleoproteins: metabolism
  • Substrate Specificity

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Authors

  • Marcela Dávila López

  • Magnus Alm Rosenblad

  • Tore Samuelsson

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