The conserved WRPW motif of Hes6 mediates proteasomal degradation

Ah Kang Seon, Hong Seol Jea, Jaesang Kim

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

Abstract

Hes6 belongs to a subfamily of basic helix-loop-helix transcription factors that includes Drosophila Hairy and Enhancer of split genes. Like other members of the family, Hes6 features the WRPW motif which is consisted just of four amino acids at its C-terminus. Here, we show that WRPW motif deletion mutant protein is substantially stabilized in comparison to the full length protein and that the enhanced stability is due to its resistance to proteasomal degradation. The WRPW motif also appears to be sufficient for acceleration of proteolysis as its fusion to two heterologous proteins, the green fluorescent protein (GFP) of Aequoria victoria and Gal4 DNA binding domain of Saccharomyces cerevisiae, significantly destabilized the proteins. These findings demonstrate a novel function of this conserved motif as a degradation signal and raise the possibility of utilizing it for controlling the level of ectopically expressed gene products.

Original languageEnglish
Pages (from-to)33-36
Number of pages4
JournalBiochemical and Biophysical Research Communications
Volume332
Issue number1
DOIs
StatePublished - 24 Jun 2005

Keywords

  • Hes6
  • Proteasome
  • Proteolysis
  • Ubiquitination
  • WRPW

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