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

Mandar T. Naik, Che Chang Chang, Nandita M. Naik, Camy C H Kung, Hsiu Ming Shih, Tai Huang Huang

Research output: Contribution to journalArticle

3 Citations (Scopus)

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 1H, 13C and 15N resonance assignments for the complex between SUMO-1 and 20 residue Daxx C-terminal SIM peptide are reported here.

Original languageEnglish
Pages (from-to)75-77
Number of pages3
JournalBiomolecular NMR Assignments
Volume5
Issue number1
DOIs
Publication statusPublished - Apr 2011
Externally publishedYes

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Keywords

  • Daxx
  • Promyelocytic leukemia
  • SUMO
  • SUMO interaction motif

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry

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