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Pri sORF peptides induce selective proteasome-mediated protein processing.

J Zanet1, E Benrabah1, T Li2

  • 1Centre de Biologie du Développement, Université de Toulouse III-Paul Sabatier, Bâtiment 4R3, 118 route de Narbonne, F-31062 Toulouse, France. CNRS, UMR5547, Centre de Biologie du Développement, F-31062 Toulouse, France.

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|September 19, 2015
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Summary
This summary is machine-generated.

Small open-reading-frame (smORF) peptides, like Drosophila polished-rice (pri), activate protein processing. These smORFs target repressors for proteasome degradation, revealing novel regulatory roles.

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Area of Science:

  • Molecular Biology
  • Genetics
  • Proteostasis

Background:

  • Small open-reading-frame (smORF) peptides are encoded by various RNAs, but their functions remain largely uncharacterized.
  • Understanding the roles of smORFs is crucial for deciphering complex cellular regulatory networks.

Purpose of the Study:

  • To investigate the function of Drosophila polished-rice (pri) smORF peptides in protein processing.
  • To identify the molecular mechanisms by which smORFs regulate protein activity and stability.

Main Methods:

  • Genome-wide RNA interference (RNAi) screen to identify interacting proteins.
  • Biochemical assays to study protein ubiquitination and proteasomal degradation.
  • Analysis of protein processing and functional conversion of transcription factors.

Main Results:

  • Drosophila pri smORF peptides induce proteasome-mediated processing of the Shavenbaby (Svb) transcription repressor.
  • An E2-E3 ubiquitin-conjugating complex, UbcD6-Ubr3, was identified as essential for pri-dependent Svb targeting to the proteasome.
  • Pri peptides mediate the interaction between Ubr3 and Svb, leading to Svb N-terminal ubiquitination and subsequent degradation, while C-terminal domains ensure partial processing into an active form.

Conclusions:

  • smORF peptides, exemplified by pri, act as regulators of protein processing by controlling the selectivity of ubiquitin ligase binding.
  • This mechanism converts a transcription repressor (Svb) into an activator, highlighting a novel layer of gene regulation.
  • The broader family of smORF peptides likely possesses an extensive repertoire of protein regulatory functions.