RNase MRP cleaves pre-tRNASer-Met in the tRNA maturation pathway
| Autor: | Jun Takeda, Masato Taoka, Douglas V. N. P. Oliveira, Kousuke Adachi, Junya Kobayashi, Yuichiro Saito, Toshiaki Isobe, Yuko Nobe, Kouji Hirota |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2014 |
| Předmět: |
Proteomics
Mitochondrial RNA processing RNase P lcsh:Medicine Biology Research and Analysis Methods Biochemistry RNase PH Catalysis stomatognathic system Nucleic Acids Endoribonucleases Schizosaccharomyces Macromolecular Structure Analysis RNA Precursors Amino Acid Sequence RNA structure RNase H lcsh:Science Molecular Biology RNA Transfer Ser Ribonucleoprotein Liquid Chromatography Spectrometric Identification of Proteins Multidisciplinary Biology and life sciences Base Sequence Chromatographic Techniques lcsh:R Proteins RNA Non-coding RNA Molecular biology Enzymes Enzyme Activation RNase MRP Amino Acid Substitution Enzyme Structure Mutation Enzymology biology.protein Nucleic Acid Conformation lcsh:Q Research Article |
| Zdroj: | PLoS ONE, Vol 9, Iss 11, p e112488 (2014) PLoS ONE |
| ISSN: | 1932-6203 |
| Popis: | Ribonuclease mitochondrial RNA processing (RNase MRP) is a multifunctional ribonucleoprotein (RNP) complex that is involved in the maturation of various types of RNA including ribosomal RNA. RNase MRP consists of a potential catalytic RNA and several protein components, all of which are required for cell viability. We show here that the temperature-sensitive mutant of rmp1, the gene for a unique protein component of RNase MRP, accumulates the dimeric tRNA precursor, pre-tRNA(Ser-Met). To examine whether RNase MRP mediates tRNA maturation, we purified the RNase MRP holoenzyme from the fission yeast Schizosaccharomyces pombe and found that the enzyme directly and selectively cleaves pre-tRNA(Ser-Met), suggesting that RNase MRP participates in the maturation of specific tRNA in vivo. In addition, mass spectrometry-based ribonucleoproteomic analysis demonstrated that this RNase MRP consists of one RNA molecule and 11 protein components, including a previously unknown component Rpl701. Notably, limited nucleolysis of RNase MRP generated an active catalytic core consisting of partial mrp1 RNA fragments, which constitute "Domain 1" in the secondary structure of RNase MRP, and 8 proteins. Thus, the present study provides new insight into the structure and function of RNase MRP. |
| Databáze: | OpenAIRE |
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