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Structure of the Yeast DEAD box protein Mss116p reveals two wedges that crimp RNA

Mark Del Campo1, Alan M Lambowitz

  • 1Institute for Cellular and Molecular Biology, University of Texas at Austin, 78712, USA.

Molecular Cell
|September 15, 2009
PubMed

Insights

The yeast DEAD box protein Mss116p acts as an RNA chaperone. Its crystal structures reveal a unique RNA crimping mechanism involving two wedges for strand separation during essential cellular processes.

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Mss116p is a DEAD box protein crucial for RNA processing in yeast mitochondria.
  • It plays roles in intron splicing, translation, and RNA end processing.
  • Understanding its mechanism is key to deciphering RNA-protein interactions.

Purpose of the Study:

  • To elucidate the structural basis of Mss116p's RNA chaperone activity.
  • To investigate the role of its C-terminal extension in RNA binding and processing.
  • To understand the mechanism of RNA strand separation mediated by Mss116p.

Main Methods:

  • High-resolution X-ray crystallography.
  • Complex formation of Mss116p with RNA oligonucleotides and ATP analogs (AMP-PNP, ADP-BeF(3)(-), ADP-AlF(4)(-)).

Main Results:

  • Determined crystal structures of Mss116p in complex with RNA and ATP analogs.
  • Revealed a closed helicase core conformation with a C-terminal extension.
  • Observed a novel RNA crimping mechanism involving two wedges for strand separation.

Conclusions:

  • Mss116p utilizes a dual-wedge mechanism for RNA strand separation.
  • The C-terminal extension plays a critical role in RNA bending and crimping.
  • These findings refine models of DEAD box protein function and RNA chaperone activity.

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