Intrinsically unstructured N-terminal domain of bZIP transcription factor HY5

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The Arabidopsis HY5 protein is a basic leucine zipper (bZIP) transcription factor that promotes photomorphogenesis. HY5 binds directly to the promoters of light responsible element containing the G-box and thus regulates their transcriptional activity. The level and activity of HY5 are negatively regulated, in a light-dependent manner, by interaction with the COP1 protein, which targets HY5 for proteasome-mediated degradation in the nucleus. Despite its essential roles in plant development, no structural information exists for HY5. In this article, we report the first structural and biophysical characterization of HY5. Using limited proteolysis in combination with mass spectrometry, circular dichroism, and nuclear magnetic resonance spectroscopy, we have deduced that the N-terminal 77 amino acids of HY5 form a premolten globular structure, while amino acids 78-110, which constitute the basic region (BR) of the protein, exist in a molten globule state. Our studies also revealed that the overall structural features of full-length HY5 are dominated largely by the disordered N-terminal domain, despite the existence of a bZIP domain at its C-terminus. We propose that HY5 is a member of the intrinsically unstructured protein (IUP) family, and that HY5 functions as an unstructured protein and benefits from being the same, in vivo.
Publisher
WILEY-LISS
Issue Date
2006-12
Language
English
Article Type
Article
Keywords

MEASLES-VIRUS NUCLEOPROTEIN; NATIVELY UNFOLDED PROTEINS; BASIC LEUCINE-ZIPPER; STRUCTURAL DISORDER; ACTIVATION DOMAIN; BINDING DOMAIN; LIGHT CONTROL; ARABIDOPSIS; GCN4; DNA

Citation

PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, v.65, no.4, pp.856 - 866

ISSN
0887-3585
DOI
10.1002/prot.21089
URI
http://hdl.handle.net/10203/90376
Appears in Collection
BS-Journal Papers(저널논문)CH-Journal Papers(저널논문)
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