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Upf1 ATPase-dependent mRNP disassembly is required for completion of nonsense- mediated mRNA decay

Tobias M Franks1, Guramrit Singh, Jens Lykke-Andersen

  • 1University of Colorado, Boulder, 80309, USA.

Cell
|December 15, 2010
PubMed

Insights

The RNA helicase Upf1

Area of Science:

  • Molecular Biology
  • Gene Expression Regulation
  • RNA Metabolism

Background:

  • Cellular mRNAs are organized into messenger ribonucleoprotein (mRNP) complexes.
  • These complexes regulate gene expression post-transcriptionally.
  • mRNA turnover involves mRNA degradation and protein recycling, but protein release mechanisms are unclear.

Purpose of the Study:

  • To investigate the mechanism of protein release from degrading messenger ribonucleoprotein (mRNP) complexes.
  • To determine the role of the RNA helicase Upf1 in messenger ribonucleoprotein (mRNP) disassembly during nonsense-mediated mRNA decay (NMD).

Main Methods:

  • Studied the ATPase activity of the RNA helicase Upf1.
  • Investigated messenger ribonucleoprotein (mRNP) disassembly during nonsense-mediated mRNA decay (NMD).
  • Analyzed the accumulation of messenger ribonucleoprotein (mRNP) intermediates in the absence of Upf1 ATPase activity.

Main Results:

  • Demonstrated that Upf1 ATPase activity drives messenger ribonucleoprotein (mRNP) disassembly during nonsense-mediated mRNA decay (NMD).
  • Observed accumulation of partially degraded NMD messenger ribonucleoprotein (mRNP) intermediates lacking Upf1 ATPase activity.
  • Showed these intermediates remain associated with NMD factors and localize to processing bodies.

Conclusions:

  • ATP hydrolysis by Upf1 is essential for the disassembly and turnover of messenger ribonucleoprotein (mRNP) complexes during nonsense-mediated mRNA decay (NMD).
  • Uncovered a critical, potentially regulated step in mRNA decay involving protein release.
  • Highlights the need to explore protein release mechanisms in other mRNA decay pathways.

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