NMR chemical shift assignments of a complex between SUMO-1 and SIM peptide derived from the C-terminus of Daxx

Biomol NMR Assign. 2011 Apr;5(1):75-7. doi: 10.1007/s12104-010-9271-4. Epub 2010 Oct 7.

Abstract

Small Ubiquitin-like MOdifiers (SUMOs) are ubiquitin-like proteins known to covalently modify large number of cellular proteins. The mammalian SUMO family includes four paralogues, SUMO-1 through SUMO-4. Death-associated protein-6, Daxx, is a 740 residue important transcription corepressor known to represses transcriptional potential of several sumolyted transcription factors. Daxx also plays important role in apoptosis. Both terminals of Daxx harbor separate SUMO Interaction Motifs (SIM), which mediate its interaction with SUMO and hence the sumolyted transcription factors. The C-terminal SIM of Daxx preferentially binds SUMO-1. Practically complete (1)H, (13)C and (15)N resonance assignments for the complex between SUMO-1 and 20 residue Daxx C-terminal SIM peptide are reported here.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Nuclear Magnetic Resonance, Biomolecular*
  • Nuclear Proteins / chemistry*
  • Nuclear Proteins / metabolism*
  • Peptides / chemistry*
  • Peptides / metabolism*
  • Protein Binding
  • SUMO-1 Protein / chemistry*
  • SUMO-1 Protein / metabolism*

Substances

  • Nuclear Proteins
  • Peptides
  • SUMO-1 Protein