Comparative functional analysis of full-length and N-terminal fragments of phytochrome C, D and E in red light-induced signaling

© 2013 The Authors. New Phytologist © 2013 New Phytologist Trust.

Bibliographische Detailangaben
Veröffentlicht in:The New phytologist. - 1979. - 200(2013), 1 vom: 18. Okt., Seite 86-96
1. Verfasser: Ádám, Éva (VerfasserIn)
Weitere Verfasser: Kircher, Stefan, Liu, Peng, Mérai, Zsuzsanna, González-Schain, Nahuel, Hörner, Maximilian, Viczián, András, Monte, Elena, Sharrock, Robert A, Schäfer, Eberhard, Nagy, Ferenc
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2013
Zugriff auf das übergeordnete Werk:The New phytologist
Schlagworte:Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. nuclear body formation nuclear translocation photomorphogenesis photoreceptor phytochrome E Arabidopsis Proteins mehr... Phytochrome 11121-56-5
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245 1 0 |a Comparative functional analysis of full-length and N-terminal fragments of phytochrome C, D and E in red light-induced signaling 
264 1 |c 2013 
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520 |a © 2013 The Authors. New Phytologist © 2013 New Phytologist Trust. 
520 |a Phytochromes (phy) C, D and E are involved in the regulation of red/far-red light-induced photomorphogenesis of Arabidopsis thaliana, but only limited data are available on the mode of action and biological function of these lesser studied phytochrome species. We fused N-terminal fragments or full-length PHYC, D and E to YELLOW FLUORESCENT PROTEIN (YFP), and analyzed the function, stability and intracellular distribution of these fusion proteins in planta. The activity of the constitutively nuclear-localized homodimers of N-terminal fragments was comparable with that of full-length PHYC, D, E-YFP, and resulted in the regulation of various red light-induced photomorphogenic responses in the studied genetic backgrounds. PHYE-YFP was active in the absence of phyB and phyD, and PHYE-YFP controlled responses, as well as accumulation, of the fusion protein in the nuclei, was saturated at low fluence rates of red light and did not require functional FAR-RED ELONGATED HYPOCOTYL1 (FHY-1) and FHY-1-like proteins. Our data suggest that PHYC-YFP, PHYD-YFP and PHYE-YFP fusion proteins, as well as their truncated N-terminal derivatives, are biologically active in the modulation of red light-regulated photomorphogenesis. We propose that PHYE-YFP can function as a homodimer and that low-fluence red light-induced translocation of phyE and phyA into the nuclei is mediated by different molecular mechanisms 
650 4 |a Comparative Study 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 4 |a Research Support, U.S. Gov't, Non-P.H.S. 
650 4 |a nuclear body formation 
650 4 |a nuclear translocation 
650 4 |a photomorphogenesis 
650 4 |a photoreceptor 
650 4 |a phytochrome E 
650 7 |a Arabidopsis Proteins  |2 NLM 
650 7 |a Phytochrome  |2 NLM 
650 7 |a 11121-56-5  |2 NLM 
700 1 |a Kircher, Stefan  |e verfasserin  |4 aut 
700 1 |a Liu, Peng  |e verfasserin  |4 aut 
700 1 |a Mérai, Zsuzsanna  |e verfasserin  |4 aut 
700 1 |a González-Schain, Nahuel  |e verfasserin  |4 aut 
700 1 |a Hörner, Maximilian  |e verfasserin  |4 aut 
700 1 |a Viczián, András  |e verfasserin  |4 aut 
700 1 |a Monte, Elena  |e verfasserin  |4 aut 
700 1 |a Sharrock, Robert A  |e verfasserin  |4 aut 
700 1 |a Schäfer, Eberhard  |e verfasserin  |4 aut 
700 1 |a Nagy, Ferenc  |e verfasserin  |4 aut 
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773 1 8 |g volume:200  |g year:2013  |g number:1  |g day:18  |g month:10  |g pages:86-96 
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