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Prolyl 4-hydroxylation regulates Argonaute 2 stability.

Hank H Qi1, Pat P Ongusaha, Johanna Myllyharju

  • 1Department of Pathology, Harvard Medical School, New Research Building 854, 77 Avenue Louis Pasteur, Boston, Massachusetts 02115, USA.

Nature
|August 12, 2008
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Summary

Hydroxylation of Argonaute 2 (Ago2) by collagen prolyl-4-hydroxylase regulates its stability. This post-translational modification is crucial for effective RNA interference and short interfering RNA activity.

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Area of Science:

  • Molecular Biology
  • Post-translational Modifications
  • RNA Interference

Background:

  • Human Argonaute (Ago) proteins are key components of RNA-induced silencing complexes (RISCs).
  • Ago2's PIWI domain mediates target RNA cleavage, a critical step in RNA interference.
  • RISC assembly and function involve numerous associated proteins, but regulatory mechanisms remain unclear.

Purpose of the Study:

  • To investigate novel regulatory mechanisms of RNA interference.
  • To identify interactions between Ago proteins and other cellular factors.
  • To elucidate the role of post-translational modifications in Ago2 stability and function.

Main Methods:

  • Mass spectrometry to identify protein interactions and post-translational modifications.
  • Co-immunoprecipitation to confirm physical interactions.
  • Short hairpin RNA (shRNA) and CRISPR/Cas9 gene editing to deplete or inactivate specific proteins.
  • Analysis of Ago2 stability and RNA interference activity in modified cells.

Main Results:

  • Physical interactions were identified between Ago2 and subunits of type I collagen prolyl-4-hydroxylase (C-P4H(I)).
  • Endogenous Ago2 was found to be hydroxylated at proline 700 (P700).
  • Depletion of C-P4H(I) subunits or mutation of Ago2 P700 destabilized Ago2 and impaired RISC activity.

Conclusions:

  • Hydroxylation of Ago2 at P700 by C-P4H(I) is a novel post-translational modification.
  • This hydroxylation is essential for maintaining Ago2 stability.
  • Ago2 hydroxylation plays a critical role in regulating RNA interference efficiency.