Arabidopsis nph1 and npl1: Blue Light Receptors That Mediate Both Phototropism and Chloroplast Relocation

UV-A/blue light acts to regulate a number of physiological processes in higher plants. These include light-driven chloroplast movement and phototropism. The NPH1 gene of Arabidopsis encodes an autophosphorylating protein kinase that functions as a photoreceptor for phototropism in response to low-in...

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Veröffentlicht in:Proceedings of the National Academy of Sciences - PNAS 2001-06, Vol.98 (12), p.6969-6974
Hauptverfasser: Sakai, Tatsuya, Kagawa, Takatoshi, Kasahara, Masahiro, Swartz, Trevor E., Christie, John M., Briggs, Winslow R., Wada, Masamitsu, Okada, Kiyotaka
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container_end_page 6974
container_issue 12
container_start_page 6969
container_title Proceedings of the National Academy of Sciences - PNAS
container_volume 98
creator Sakai, Tatsuya
Kagawa, Takatoshi
Kasahara, Masahiro
Swartz, Trevor E.
Christie, John M.
Briggs, Winslow R.
Wada, Masamitsu
Okada, Kiyotaka
description UV-A/blue light acts to regulate a number of physiological processes in higher plants. These include light-driven chloroplast movement and phototropism. The NPH1 gene of Arabidopsis encodes an autophosphorylating protein kinase that functions as a photoreceptor for phototropism in response to low-intensity blue light. However, nph1 mutants have been reported to exhibit normal phototropic curvature under high-intensity blue light, indicating the presence of an additional phototropic receptor. A likely candidate is the nph1 homologue, npl1, which has recently been shown to mediate the avoidance response of chloroplasts to high-intensity blue light in Arabidopsis. Here we demonstrate that npl1, like nph1, noncovalently binds the chromophore flavin mononucleotide (FMN) within two specialized PAS domains, termed LOV domains. Furthermore, when expressed in insect cells, npl1, like nph1, undergoes light-dependent autophosphorylation, indicating that npl1 also functions as a light receptor kinase. Consistent with this conclusion, we show that a nph1 npl1 double mutant exhibits an impaired phototropic response under both low- and high-intensity blue light. Hence, npl1 functions as a second phototropic receptor under high fluence rate conditions and is, in part, functionally redundant to nph1. We also demonstrate that both chloroplast accumulation in response to low-intensity light and chloroplast avoidance movement in response to high-intensity light are lacking in the nph1 npl1 double mutant. Our findings therefore indicate that nph1 and npl1 show partially overlapping functions in two different responses, phototropism and chloroplast relocation, in a fluence rate-dependent manner.
doi_str_mv 10.1073/pnas.101137598
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subjects Arabidopsis
Arabidopsis - metabolism
Arabidopsis - physiology
Arabidopsis Proteins
Biological Sciences
Chloroplasts
Chloroplasts - physiology
Curvature
Flowers & plants
Fluence
Genes
Hypocotyls
Light
Mutation
nph1 gene
nphl1 gene
Phosphoproteins - metabolism
Photoreceptors
Photosynthetic Reaction Center Complex Proteins - metabolism
Phototropism
Physiological regulation
Plant cells
Plant Proteins - metabolism
Proteins
Receptors
Recombinant Proteins - metabolism
Space life sciences
title Arabidopsis nph1 and npl1: Blue Light Receptors That Mediate Both Phototropism and Chloroplast Relocation
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