INVESTIGADORES
GONZALEZ SCHAIN Nahuel Damian
artículos
Título:
Comparative functional analysis of full-length and N-terminal fragments of phytochrome C, D and E in red light-induced signaling
Autor/es:
ADAM E; KIRCHER S; LIU P; MERAI Z; GONZALEZ SCHAIN N; HORNER M; VICZIAN A; MONTE E; SHARROCK RA; SCHAFER E; NAGY F
Revista:
NEW PHYTOLOGIST
Editorial:
WILEY-BLACKWELL PUBLISHING, INC
Referencias:
Lugar: Londres; Año: 2013 vol. 200 p. 86 - 96
ISSN:
0028-646X
Resumen:
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.