2. Academic Validation
  3. A human short open reading frame (sORF)-encoded polypeptide that stimulates DNA end joining

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

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: hanakahi@uic.edu.
  • 5 Department of Chemistry and Chemical Biology and Harvard University, Cambridge, Massachusetts 02138. Electronic address: saghatelian@chemistry.harvard.edu.
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.

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