| Derepression of the NC80 motif is critical for the photoactivation of Arabidopsis CRY2. | |
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MedLine Citation:
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PMID: 17438275 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Cryptochromes are blue light receptors that regulate photomorphogenesis in plants and the circadian clock in animals and plants. Arabidopsis cryptochrome 2 (CRY2) mediates blue light inhibition of hypocotyl elongation and photoperiodic control of floral initiation. CRY2 undergoes blue light-induced phosphorylation, which was hypothesized to be associated with CRY2 photoactivation. To further investigate how light activates CRY2, we analyzed the physiological activities and phosphorylation of various CRY2 fusion proteins in transgenic plants. Our results showed that an 80-residue motif, referred to as NC80, was sufficient to confer the physiological function of CRY2. The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated, suggesting that the blue light-induced CRY2 phosphorylation causes a conformational change to derepress the NC80 motif. Consistent with this hypothesis, the CRY2 C-terminal tail was found to be required for the blue light-induced CRY2 phosphorylation but not for the CRY2 activity. We propose that the PHR domain and the C-terminal tail of the unphosphorylated CRY2 form a "closed" conformation to suppress the NC80 motif in the absence of light. In response to blue light, the C-terminal tail of CRY2 is phosphorylated and electrostatically repelled from the surface of the PHR domain to form an "open" conformation, resulting in derepression of the NC80 motif and signal transduction to trigger photomorphogenic responses. |
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Authors:
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Xuhong Yu; Dror Shalitin; Xuanming Liu; Maskit Maymon; John Klejnot; Hongyun Yang; Javier Lopez; Xiaoying Zhao; Krishnaprasad T Bendehakkalu; Chentao Lin |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't Date: 2007-04-16 |
Journal Detail:
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Title: Proceedings of the National Academy of Sciences of the United States of America Volume: 104 ISSN: 0027-8424 ISO Abbreviation: Proc. Natl. Acad. Sci. U.S.A. Publication Date: 2007 Apr |
Date Detail:
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Created Date: 2007-04-25 Completed Date: 2007-06-06 Revised Date: 2009-11-19 |
Medline Journal Info:
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Nlm Unique ID: 7505876 Medline TA: Proc Natl Acad Sci U S A Country: United States |
Other Details:
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Languages: eng Pagination: 7289-94 Citation Subset: IM |
Affiliation:
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Department of Molecular, Cell, and Developmental Biology, University of California-Los Angeles, Los Angeles, CA 90095, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Motifs Arabidopsis / genetics, metabolism*, radiation effects* Arabidopsis Proteins / chemistry*, metabolism* Cell Nucleus / metabolism, radiation effects Cryptochromes Dimerization Light* Phenotype Phosphorylation / radiation effects Plants, Genetically Modified Protein Conformation / radiation effects Protein Transport / radiation effects Receptors, Cell Surface / metabolism Recombinant Fusion Proteins / metabolism Structure-Activity Relationship |
| Grant Support | |
ID/Acronym/Agency:
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GM 56265/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Arabidopsis Proteins; 0/CRY2 protein, Arabidopsis; 0/Cryptochromes; 0/Receptors, Cell Surface; 0/Recombinant Fusion Proteins |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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