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Crystal structures of T. brucei MRP1/MRP2 guide-RNA binding complex reveal RNA matchmaking mechanism

Maria A Schumacher1, Elham Karamooz, Alena Zíková

  • 1Department of Biochemistry and Molecular Biology, University of Texas, M.D. Anderson Cancer Center, Unit 1000, Houston, 77030, USA. maschuma@mdanderson.org

Cell
|August 23, 2006
PubMed

Insights

Mitochondrial RNA binding proteins MRP1 and MRP2 form a complex essential for RNA editing in kinetoplastids. Structural studies reveal how this complex stabilizes guide RNAs in an unfolded state, facilitating crucial RNA-RNA hybridization for editing.

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Genetics

Background:

  • Mitochondrial RNA binding proteins MRP1 and MRP2 form a complex vital for RNA editing in kinetoplastids.
  • This complex acts as a matchmaker, binding guide RNAs and promoting their hybridization with pre-edited messenger RNAs.

Purpose of the Study:

  • To elucidate the mechanism of RNA matchmaking by the MRP1/MRP2 complex.
  • To determine the structures of the Trypanosoma brucei apoMRP1/MRP2 complex and its complex with guide RNA.

Main Methods:

  • X-ray crystallography was used to determine the structures of the MRP1/MRP2 complex.
  • Structural analysis of the apo-MRP1/MRP2 complex and the MRP1/MRP2-guide RNA complex.

Main Results:

  • The MRP1/MRP2 complex is a heterotetramer, with each subunit sharing a "Whirly" transcription-factor fold.
  • Guide RNA binds electrostatically to a basic surface on the MRP complex.
  • Stem/loop I of the guide RNA remains unfolded, exposing its bases for hybridization.

Conclusions:

  • MRP1/MRP2 functions as an RNA matchmaker by stabilizing guide RNA in an unfolded conformation.
  • This stabilization is critical for enabling RNA-RNA hybridization during the RNA editing process.

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