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A Short Amino-Terminal Part of Arabidopsis Phytochrome A Induces Constitutive Photomorphogenic Response.
MedLine Citation:
PMID:  22498774     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Phytochrome A (phyA) is the dominant photoreceptor of far-red light sensing in Arabidopsis thaliana. phyA accumulates at high levels in the cytoplasm of etiolated seedlings, and light-induced phyA signaling is mediated by a complex regulatory network. This includes light- and FHY1/FHL protein-dependent translocation of native phyA into the nucleus in vivo. It has also been shown that a short N-terminal fragment of phyA (PHYA406) is sufficient to phenocopy this highly regulated cellular process in vitro. To test the biological activity of this N-terminal fragment of phyA in planta, we produced transgenic phyA-201 plants expressing the PHYA406-YFP (YELLOW FLUORESCENT PROTEIN)-DD, PHYA406-YFP-DD-NLS (nuclear localization signal), and PHYA406-YFP-DD-NES (nuclear export signal) fusion proteins. Here, we report that PHYA406-YFP-DD is imported into the nucleus and this process is partially light-dependent whereas PHYA406-YFP-DD-NLS and PHYA406-YFP-DD-NES display the expected constitutive localization patterns. Our results show that these truncated phyA proteins are light-stable, they trigger a constitutive photomorphogenic-like response when localized in the nuclei, and neither of them induces proper phyA signaling. We demonstrate that in vitro and in vivo PHYA406 Pfr and Pr bind COP1, a general repressor of photomorphogenesis, and co-localize with it in nuclear bodies. Thus, we conclude that, in planta, the truncated PHYA406 proteins inactivate COP1 in the nuclei in a light-independent fashion.
Authors:
András Viczián; Eva Adám; Iris Wolf; János Bindics; Stefan Kircher; Marc Heijde; Roman Ulm; Eberhard Schäfer; Ferenc Nagy
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-4-11
Journal Detail:
Title:  Molecular plant     Volume:  -     ISSN:  1752-9867     ISO Abbreviation:  -     Publication Date:  2012 Apr 
Date Detail:
Created Date:  2012-4-13     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101465514     Medline TA:  Mol Plant     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Affiliation:
Institute of Plant Biology, Biological Research Centre of the Hungarian Academy of Sciences, Temesvári krt. 62., H-6726 Szeged, Hungary.
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