Pri sORF peptides induce selective proteasome-mediated protein processing

@article{Zanet2015PriSP,
  title={Pri sORF peptides induce selective proteasome-mediated protein processing},
  author={Jennifer Zanet and E. Benrabah and Ting Li and Anne P{\'e}lissier-Monier and H{\'e}l{\`e}ne Chanut-Delalande and Brice Ronsin and Hugo J. Bellen and Francois Payre and S Fern{\'a}ndez Plaza},
  journal={Science},
  year={2015},
  volume={349},
  pages={1356-1358}
}
A wide variety of RNAs encode small open-reading-frame (smORF/sORF) peptides, but their functions are largely unknown. Here, we show that Drosophila polished-rice (pri) sORF peptides trigger proteasome-mediated protein processing, converting the Shavenbaby (Svb) transcription repressor into a shorter activator. A genome-wide RNA interference screen identifies an E2-E3 ubiquitin-conjugating complex, UbcD6-Ubr3, which targets Svb to the proteasome in a pri-dependent manner. Upon interaction with… CONTINUE READING
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Single-letter abbreviations for the amino acid residues

  • A Ala, C Cys, +17 authors Y Tyr.
  • August 2015 10.1126/science.aac5677
  • 2015

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