A human short open reading frame (sORF)-encoded polypeptide that stimulates DNA end joining

  • J Biol Chem. 2014 Apr 18;289(16):10950-10957. doi: 10.1074/jbc.C113.533968.
Sarah A Slavoff  1 ,  Jinho Heo  2 ,  Bogdan A Budnik  3 ,  Leslyn A Hanakahi  4 ,  Alan Saghatelian  5
Affiliations
  • 1. Department of Chemistry and Chemical Biology and Harvard University, Cambridge, Massachusetts 02138.
  • 2. Department of Medicinal Chemistry and Pharmacognosy, University of Illinois College of Pharmacy, Rockford, Illinois 60612.
  • 3. Faculty of Arts and Sciences (FAS) Center for Systems Biology, Harvard University, Cambridge, Massachusetts 02138 and.
  • 4. Department of Medicinal Chemistry and Pharmacognosy, University of Illinois College of Pharmacy, Rockford, Illinois 60612. Electronic address: [email protected].
  • 5. Department of Chemistry and Chemical Biology and Harvard University, Cambridge, Massachusetts 02138. Electronic address: [email protected].
PMID: 24610814 DOI: 10.1074/jbc.C113.533968
Abstract

The recent discovery of numerous human short open reading frame (sORF)-encoded polypeptides (SEPs) has raised important questions about the functional roles of these molecules in cells. Here, we show that a 69-amino acid SEP, MRI-2, physically interacts with the Ku heterodimer to stimulate DNA double-strand break ligation via nonhomologous end joining. The characterization of MRI-2 suggests that this SEP may participate in DNA repair and underscores the potential of SEPs to serve important biological functions in mammalian cells.

Keywords
DNA Repair; Peptide Interactions; Peptides; Protein-Protein Interactions; Proteomics; Short ORF.