Structure and function of the native and recombinant mitochondrial MRP1/MRP2 complex from Trypanosoma brucei

. 2008 Jul ; 38 (8-9) : 901-12. [epub] 20080126

Jazyk angličtina Země Anglie, Velká Británie Médium print-electronic

Typ dokumentu časopisecké články, Research Support, N.I.H., Extramural, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/pmid18295767

Grantová podpora
AI14102 NIAID NIH HHS - United States
R01 AI014102-26 NIAID NIH HHS - United States
5R03TW6445 FIC NIH HHS - United States
R01 AI014102 NIAID NIH HHS - United States
R03 TW006445 FIC NIH HHS - United States
R37 AI014102 NIAID NIH HHS - United States

Odkazy

PubMed 18295767
PubMed Central PMC2492832
DOI 10.1016/j.ijpara.2007.12.009
PII: S0020-7519(08)00020-9
Knihovny.cz E-zdroje

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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