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 language | English |
|---|---|
| Pages (from-to) | 33-36 |
| Number of pages | 4 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 332 |
| Issue number | 1 |
| DOIs | |
| State | Published - 24 Jun 2005 |
Bibliographical note
Funding Information:We thank S.Y. Lee for his critical comments on the manuscript. We thank D.J. Anderson for permitting the use of anti-Hes6 antiserum. This research was supported by the Ewha Womans University Research Grant of 2003, by the Korea Science and Engineering Foundation through the Center for Cell Signaling Research at Ewha Womans University, and by a grant (M103KV010010 04K2201 01020; to J. Kim) from Brain Research Center of the 21st Century Frontier Research Program funded by the Ministry of Science and Technology, the Republic of Korea.
Keywords
- Hes6
- Proteasome
- Proteolysis
- Ubiquitination
- WRPW