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The Plant Cell, Vol. 14, 1591-1603, July 2002, Copyright © 2002,
American Society of Plant Biologists

Missense Mutation in the PAS2 Domain of Phytochrome A Impairs Subnuclear Localization and a Subset of Responses

Marcelo J. Yanovsky1,a, Juan Pablo Luppi2,3,,a, Daniel Kirchbauer2,b, Ouliana B. Ogorodnikovac, Vitally A. Sineshchekovc, Eva Adamd, Stefan Kircherb, Roberto J. Stanelonie, Eberhard Schäferb, Ferenc Nagyd and Jorge J. Casal4,a

a IFEVA, Facultad de Agronomía, Universidad de Buenos Aires, Av San Martín 4453, 1417-Buenos Aires, Argentina
b Institut für Biologie II, Universität Freiburg, Schänzlestrasse 1, D-79104 Freiburg, Germany
c Biology Department, M.V. Lomonosov Moscow State University, Moscow, Russia
d Institute of Plant Biology, Biological Research Center, P.O. Box 521, H-6701, Szeged, Hungary
e Instituto de Investigaciones Bioquímicas Fundación Campomar, Av Patricias Argentinas 435, 1405-Buenos Aires, Argentina

4 To whom correspondence should be addressed. E-mail casal{at}ifeva.edu.ar; fax 54-11-45-14-87-30

Phytochrome A signaling shows two photobiologically discrete outputs: so-called very-low-fluence responses (VLFR) and high-irradiance responses (HIR). By modifying previous screening protocols, we isolated two Arabidopsis mutants retaining VLFR and lacking HIR. Phytochrome A negatively or positively regulates phytochrome B signaling, depending on light conditions. These mutants retained the negative but lacked the positive regulation. Both mutants carry the novel phyA-302 allele, in which Glu-777 (a residue conserved in angiosperm phytochromes) changed to Lys in the PAS2 motif of the C-terminal domain. The phyA-302 mutants showed a 50% reduction in phytochrome A levels in darkness, but this difference was compensated for by greater stability under continuous far-red light. phyA-302:green fluorescent protein fusion proteins showed normal translocation from the cytosol to the nucleus under continuous far-red light but failed to produce nuclear spots, suggesting that nuclear speckles could be involved in HIR signaling and phytochrome A degradation. We propose that the PAS2 domain of phytochrome A is necessary to initiate signaling in HIR but not in VLFR, likely via interaction with a specific partner.




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