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Structure and function of the native and recombinant mitochondrial MRP1/MRP2 complex from Trypanosoma brucei
A Zikova, J Kopecna, MA Schumacher, K Stuart, L Trantirek, J Lukes
Jazyk angličtina Země Velká Británie
- MeSH
- chromatografie MeSH
- editace RNA MeSH
- elektronová mikroskopie MeSH
- financování organizované MeSH
- guide RNA, Kinetoplastida metabolismus ultrastruktura MeSH
- lidé MeSH
- mitochondriální proteiny fyziologie metabolismus ultrastruktura MeSH
- prekurzory RNA metabolismus ultrastruktura MeSH
- proteiny spojené s mnohočetnou rezistencí k lékům fyziologie chemie MeSH
- proteiny vázající RNA metabolismus ultrastruktura MeSH
- rekombinantní proteiny farmakologie MeSH
- RNA protozoální genetika MeSH
- Trypanosoma brucei brucei genetika metabolismus MeSH
- zvířata MeSH
- Check Tag
- lidé MeSH
- zvířata MeSH
The mitochondrial RNA-binding proteins (MRP) 1 and 2 play a regulatory role in RNA editing and putative role(s) in RNA processing in Trypanosoma brucei. Here, we report the purification of a high molecular weight protein complex consisting solely of the MRP1 and MRP2 proteins from the mitochondrion of T. brucei. The MRP1/MRP2 complex natively purified from T. brucei and the one reconstituted in Escherichia coli in vivo bind guide (g) RNAs and pre-mRNAs with dissociation constants in the nanomolar range, and efficiently promote annealing of pre-mRNAs with their cognate gRNAs. In addition, the MRP1/MRP2 complex stimulates annealing between two non-cognate RNA molecules suggesting that along with the cognate duplexes, spuriously mismatched RNA hybrids may be formed at some rate in vivo. A mechanism of catalysed annealing of gRNA/pre-mRNA by the MRP1/MRP2 complex is proposed.
Citace poskytuje Crossref.org
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- $a The mitochondrial RNA-binding proteins (MRP) 1 and 2 play a regulatory role in RNA editing and putative role(s) in RNA processing in Trypanosoma brucei. Here, we report the purification of a high molecular weight protein complex consisting solely of the MRP1 and MRP2 proteins from the mitochondrion of T. brucei. The MRP1/MRP2 complex natively purified from T. brucei and the one reconstituted in Escherichia coli in vivo bind guide (g) RNAs and pre-mRNAs with dissociation constants in the nanomolar range, and efficiently promote annealing of pre-mRNAs with their cognate gRNAs. In addition, the MRP1/MRP2 complex stimulates annealing between two non-cognate RNA molecules suggesting that along with the cognate duplexes, spuriously mismatched RNA hybrids may be formed at some rate in vivo. A mechanism of catalysed annealing of gRNA/pre-mRNA by the MRP1/MRP2 complex is proposed.
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