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자연과학대학
생명과학전공
Journal papers
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The conserved WRPW motif of Hes6 mediates proteasomal degradation
Title
The conserved WRPW motif of Hes6 mediates proteasomal degradation
Authors
Seon A.K.
;
Jea H.S.
;
Kim J.
Ewha Authors
김재상
SCOPUS Author ID
김재상
Issue Date
2005
Journal Title
Biochemical and Biophysical Research Communications
ISSN
0006-291X
Citation
Biochemical and Biophysical Research Communications vol. 332, no. 1, pp. 33 - 36
Indexed
SCI; SCIE; SCOPUS
Document Type
Article
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. © 2005 Elsevier Inc. All rights reserved.
DOI
10.1016/j.bbrc.2005.04.089
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