Pri sORF peptides induce selective proteasome-mediated protein processing
Copyright policy )Pri sORF peptides induce selective proteasome-mediated protein processing
Small peptide regulates protein activity Coding and noncoding RNAs can produce peptides from small open reading frames (smORFs), with a variety of mostly unknown functions. Using a genome-wide screen, Zanet et al. show that Polished rice (Pri) smORF peptides control fruit fly development by binding to an E3 ubiquitin ligase. This changes the ligase's selectivity and triggers proteasome-dependent maturation of the developmental transcription factor Shavenbaby. Other smORF peptides may act by a similar mechanism to regulate protein activity. Science , this issue p. 1356
- Neurological Research Institute United States
- Baylor College of Medicine United States
- UNIVERSITE FEDERALE DE TOULOUSE MIDI-PYRENEES France
- Paul Sabatier University France
- Howard Hughes Medical Institute United States
570, Proteasome Endopeptidase Complex, [SDV]Life Sciences [q-bio], Ubiquitin-Protein Ligases, Molecular Sequence Data, 610, Pri sORF, Protein processing, Open Reading Frames, Animals, Drosophila Proteins, Amino Acid Sequence, Ubiquitination, Protein Structure, Tertiary, [SDV] Life Sciences [q-bio], DNA-Binding Proteins, Drosophila melanogaster, Gene Expression Regulation, Proteolysis, Ubiquitin-Conjugating Enzymes, peptides, RNA Interference, Peptides, Transcription Factors
570, Proteasome Endopeptidase Complex, [SDV]Life Sciences [q-bio], Ubiquitin-Protein Ligases, Molecular Sequence Data, 610, Pri sORF, Protein processing, Open Reading Frames, Animals, Drosophila Proteins, Amino Acid Sequence, Ubiquitination, Protein Structure, Tertiary, [SDV] Life Sciences [q-bio], DNA-Binding Proteins, Drosophila melanogaster, Gene Expression Regulation, Proteolysis, Ubiquitin-Conjugating Enzymes, peptides, RNA Interference, Peptides, Transcription Factors
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