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Global identification of new substrates for the yeast endoribonuclease, RNase mitochondrial RNA processing (MRP).


RNase mitochondrial RNA processing (MRP) is an essential, evolutionarily conserved endoribonuclease composed of 10 different protein subunits and a single RNA. RNase MRP has established roles in multiple pathways including ribosome biogenesis, cell cycle regulation, and mitochondrial DNA replication. Although each of these functions is important to cell growth, additional functions may exist given the essential nature of the complex. To identify novel RNase MRP substrates, we utilized RNA immunoprecipitation and microarray chip analysis to identify RNA that physically associates with RNase MRP. We identified several new potential substrates for RNase MRP including a cell cycle-regulated transcript, CTS1; the yeast homolog of the mammalian p27(Kip1), SIC1; and the U2 RNA component of the spliceosome. In addition, we found RNase MRP to be involved in the regulation of the Ty1 transposon RNA. These results reinforce and broaden the role of RNase MRP in cell cycle regulation and help to identify new roles of this endoribonuclease.

Pubmed ID: 22977255


  • Aulds J
  • Wierzbicki S
  • McNairn A
  • Schmitt ME


The Journal of biological chemistry

Publication Data

October 26, 2012

Associated Grants

  • Agency: NIGMS NIH HHS, Id: GM063798

Mesh Terms

  • Chitinase
  • Cyclin-Dependent Kinase Inhibitor Proteins
  • Endoribonucleases
  • Genes, Fungal
  • Mutation
  • Oligonucleotide Array Sequence Analysis
  • Protein Binding
  • RNA Processing, Post-Transcriptional
  • RNA Stability
  • RNA, Fungal
  • RNA, Messenger
  • Ribosomal Proteins
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Transcription Factors