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Serine-To-Alanine Substitutions at the Amino-Terminal Region of Phytochrome a Result in an Increase M Biological Activity

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Serine-To-Alanine Substitutions at the Amino-Terminal Region of Phytochrome a Result in an Increase M Biological Activity Downloaded from genesdev.cshlp.org on September 30, 2021 - Published by Cold Spring Harbor Laboratory Press Serine-to-alanine substitutions at the amino-terminal region of phytochrome A result in an increase m biological activity J6rg Stockhaus, 1-3 Akira Nagatani, 2 Ursula Halfter, 1,2 Steve Kay, 1'4 Masaki Furuya, 2,s and Nam-Hai Chua 1"6 ~The Rockefeller University, Laboratory of Plant Molecular Biology, New York, New York 10021-6399 USA; 2Frontier Research Program, Laboratory of Plant Biological Regulation, RIKEN Institute, Wako, Saitama, 351-01, Japan We have used a tobacco transgenic plant system to assay the structure/function relationship of phytochrome A (phyA), a plant photoreceptor. The amino terminus of phyA from different plant species is very rich in serine residues. To investigate whether these serine residues are required for phytochrome function, the first 10 serine codons encoding amino acid residues 2-4, 10-14, 19, and 20 in the amino-terminal domain of the rice phyA gene (phyA) were changed to alanine codons. The mutant (S/A phyA), as well as the wild-type phyA cDNA, was placed under the control of the 35S promoter, and the chimeric genes were transferred into the tobacco genome by Agrobacterium-mediated transformation. Transgenic tobacco plants expressing either wild-type or S/A phyA showed similar phenotypic alterations, including dwarfism and dark-green leaves. However, hypocotyl elongation experiments revealed that transgenic seedlings expressing S/A phyA showed a higher amplitude of the red light response with respect to the inhibition of hypocotyl elongation. The observed difference is not correlated with expression levels of the transgene. The chromophore is attached to the mutant phyA apoprotein (PHY A), and the mutant photoreceptor is photoreversible, giving a difference spectrum indistinguishable from that of the rice phyA. Our results indicate that the S/A mutant has a higher biological activity as compared with the wild-type rice phyA. [Key Words: Phytochrome; structure/function; tobacco] Received August 7, 1992; revised version accepted October 1, 1992. Autotrophic plants depend on light as the primary en- olated seedlings undergo photomorphogenesis that is ergy source. For this reason, it is essential for the plant to characterized by chlorophyll synthesis, chloroplast de- continuously monitor and adapt to ambient light condi- velopment, leaf expansion, and the cessation of rapid in- tions. The light-sensing function is carried out by several temode elongation. It is known that this process is reg- photosensory pigments that are able to measure light ulated by the complex interaction of several different quantity and quality. In addition, the light-detection photoreceptors (Furuya 1987; Thomas and Johnson mechanism is used to trigger various plant developmen- 1991). One of these photoreceptors is red light-absorbing tal processes ranging from germination to flowering phytochrome, which is the best characterized plant pho- (Kendrick and Kronenberg 1986; Smith and Whitelam toreceptor to date (Furuya 1989; Smith and Whitelam 1990). One of these developmental processes is a phe- 1990). Phytochrome is a chromoprotein consisting of an nomenon termed photomorphogenesis. When germinat- apoprotein {molecular mass of monomer, 118-125 kD) ed in complete darkness, higher plant seedlings exhibit covalently linked to a linear tetrapyrrole (Lagarias and certain characteristic features, including elongated inter- Rapoport 1980). It is synthesized in the dark as the red nodes, reduced leaf size, no chlorophyll synthesis, and light-absorbing form (Pr; h max. = 666 nm), which is arrested development. Upon exposure to light these eti- physiologically inactive. Absorption of red light converts the Pr form to the biologically active far red-absorbing form (Pff; h max. = 730 nm). The light-induced conver- Present addresses: 3Institut fiir Entwicklungs- und Molekularbiologieder Pflanzen, Heinrich-Heine Universit~t Dfisseidorf, 4000 Dfisseldorf 1, sion between the Pr and Pff forms is photoreversible. Germany; 4Department of Biology, University of Virginia, Charlottes- Phytochrome therefore serves as a molecular light ville, Virginia 22901 USA; SAdvancedResearch Laboratory, Hitachi, Ltd. switch, being activated by red light and attenuated by far Laboratory of Plant Biological Regulation, Hatoyama, Saitama, Japan 350-03. red light. 6Corresponding author. Several cDNA and genomic clones encoding phy- 2364 GENES& DEVELOPMENT 6:2364-2372 9 1992by Cold Spring Harbor Laboratory ISSN 0890-9369/92 $3.00 Downloaded from genesdev.cshlp.org on September 30, 2021 - Published by Cold Spring Harbor Laboratory Press PhyA mutant with increased biological activity tochrome have been isolated and characterized (for re- of phyA from different species contain a preponderance view, see Quail 1991). Sequence analysis revealed that of serine residues. Figure 1A compares the first 20 amino the cDNA clones encode distinct apoproteins (PHY A, acids of phyA from different monocotyledonous and di- PHY B, PHY C, etc.). Among these different types of cotyledonous species. The serine-rich character is con- phytochrome, phytochrome A (phyA), also referred to as served among phyA molecules from evolutionarily di- type I phytochrome (Furuya 1989), is the best character- vergent species such as the monocot rice and the dicot ized so far. Some data have accumulated concerning its tobacco (Fig. 1A). Of the first 20 amino-terminal amino domain structure and the conformational changes that acids of rice phyA, 10 are serine residues {amino acids the molecule undergoes during photoconversion (Vier- 2--4, 10-14, 19, and 20). This observation prompted us to stra and Quail 1986; Yamamoto 1990; Parker et al. 1991). investigate whether these serine residues are essential However, very little is known about the sequence of mo- for the function of rice phyA in vivo. To address this lecular events by which phyA triggers the diverse phys- question, we have chosen to assay the activity of mu- iological responses. The availability of full-length cDNA tated phyA in transgenic tobacco plants. The first 10 clones encoding phyA from different plant species made serine codons of a rice phyA cDNA (Kay et al. 1989a) it possible to express this particular photoreceptor in were changed to alanine codons (Fig. 1B), and the mu- transgenic plants. It was found that expression of mono- tated cDNA was fused downstream of the 35S promoter cot phyA in transgenic tobacco or tomato plants induces of cauliflower mosaic virus. This construct was trans- phenotypic changes that include semidwarfism and ferred into the Nicotiana tabacum var. Xanthi genome dark-green leaves (Boylan and Quail 1989; Keller et al. by Agrobacterium-mediated transformation. Transgenic 1989; Nagatani et al. 1991), as well as altered patterns of tobacco plants expressing rice wild-type (RW) phyA un- endogenous cab gene expression (Kay et al. 1989b). In der the transcriptional regulation of the 35S promoter particular, it was shown that the introduced rice gene were used as controls throughout these studies. phyA can regulate the hypocotyl length of transgenic Eight independent transgenic plants expressing the tobacco seedlings, resulting in shorter hypocotyls, as mutated rice phyA cDNA (S/A) showed phenotypic compared with untransformed control seedlings, under changes, such as shortened intemodes and dark-green dim white light (Nagatani et al. 1991). Similar results leaves. Similar phenotypes have been described previ- were obtained with the expression of oat phyA in trans- ously for plants expressing wild-type phyA genes (Boylan genie Arabidopsis (Boylan and Quail 1991). Therefore, and Quail 1989; Keller et al. 1989; Nagatani et al. 1991). these transgenic systems can be used to analyze the This characteristic phenotype indicated that the rice S/A structure/function relationship of phyA in vivo. phyA mutant was still functional (Fig. 1C). Because the We are interested in studying the functions of different plants shown in Figure 1C were grown under light con- domains of phyA using rice phyA as a model system. We ditions that were saturating for most phytochrome re- have first focused on the amino-terminal domain, be- sponses, it was not possible to perform comparative cause previous studies (Vierstra and Quail 1986; Ya- studies of transgenic plants expressing either the rice mamoto 1990; Parker et al. 1991) demonstrated that this wild-type phyA (RW phyA) or the S/A phyA mutant. To domain (amino-terminal 10 kD of phytochrome) under- analyze the biological activity of the expressed rice phyA goes significant conformational changes upon photocon- molecules, we have chosen the hypocotyl elongation as- version from the Pr to the Pfr form (Cordonnier et al. say described by Nagatani et al. (1991) as a sensitive ex- 1985; Jones et al. 1985; Lagarias and Mercurio 1985; perimental system. Chai et al. 1987; Vierstra et al. 1987}. In the Pfr form, the T 1 seeds of independent transgenic plants were im- amino-terminal domain interacts with the chromophore bibed under white light for 24 hr and subsequently irra- environment and alters the spectral properties of this diated with 15 x 10 -~ W/m 2 red light for 6 days. Under molecule (Vierstra and Quail 1983}. An inspection of these growth conditions, phytochrome is limiting for the amino-terminal amino acid sequences of phyA from dif- inhibition of hypocotyl elongation, which is known to be ferent species revealed that these sequences are enriched a characteristic phytochrome
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