DOCSLIB.ORG

Phytochrome-Mediated Photoperception and Signal Transduction in Higher Plants

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Phytochrome-Mediated Photoperception and Signal Transduction in Higher Plants EMBO reports Phytochrome-mediated photoperception and signal transduction in higher plants Eberhard Schäfer & Chris Bowler1,+ Universitat Freiburg, Institut fur Biologie II/Botanik, Schanzlestrasse 1, D-79104 Freiburg, Germany and 1Molecular Plant Biology Laboratory, Stazione Zoologica ‘Anton Dohrn’, Villa Comunale, I-80121 Naples, Italy Received July 1, 2002; revised September 30, 2002; accepted October 1, 2002 Light provides a major source of information from the environ- Phytochromes are typically encoded by small multigene ment during plant growth and development. Light perception families, e.g. PHYA-PHYE in Arabidopsis (Møller et al., 2002; is mediated through the action of several photoreceptors, Nagy and Schäfer, 2002; Quail, 2002a,b). Each forms a including the phytochromes. Recent results demonstrate that homodimer of ∼240 kDa and light sensitivity is conferred by the light responses involve the regulation of several thousand presence of a tetrapyrrole chromophore covalently bound to the genes. Some of the key events controlling this gene expression N-terminal half of each monomer (Montgomery and Lagarias, are the translocation of the phytochrome photoreceptors into 2002). Dimerization domains are located within the C-terminal the nucleus followed by their binding to transcription factors. half of the proteins, as are other domains involved in the activa- Coupled with these events, the degradation of positively tion of signal transduction (Quail et al., 1995; Quail, 2002a). acting intermediates appears to be an important process Each phytochrome can exist in two photointerconvertible whereby photomorphogenesis is repressed in darkness. This conformations, denoted Pr (a red light-absorbing form) and Pfr review summarizes our current knowledge of these processes. (a far red light-absorbing form) (Figure 1A). Because sunlight is enriched in red light (compared with far red light), phytochrome Introduction is predominantly in the Pfr form in the light, and this can convert back to the Pr form during periods of darkness by a process Plants utilize light as a source of energy and as a source of inform- known as dark reversion. Photoconversion back to Pr can also ation about their environment. Dark-grown (etiolated) seed- be mediated by pulses of far red light. lings display an apical hook, closed and unexpanded cotyledons In dark-grown seedlings, phyA is the most abundant phyto- and elongated hypocotyls. This developmental programme chrome, although it is rapidly degraded upon exposure to light (known as skotomorphogenesis) is necessary for newly germin- (Møller et al., 2002; Nagy and Schäfer, 2002). Expression of the ating seedlings to grow through soil or fallen leaves to reach the PHYA gene is also repressed in the light. The other PHY genes light. Upon light exposure, seedlings undergo de-etiolation: are expressed at much lower levels and their expression is not cotyledons open, expand and begin to photosynthesize, hypocotyl elongation is inhibited and cell differentiation is strongly influenced by light. phyB is more abundant than phyC–E, initiated in vegetative meristems. These events are known as but its mRNA levels are typically only ~1% of those of phyA photomorphogenesis and result largely from light-mediated mRNA in the dark (Quail et al., 1995). In sunlight, however, alterations in gene expression (Ma et al., 2001; Tepperman et al., phyB is the most abundant phytochrome due to phyA degradation. 2001; Schroeder et al., 2002). The physiological functions of phyA and phyB are the best characterized (see below), and only recently has some inform- ation been obtained about the roles of phyC–E (Møller et al., The phytochromes 2002). In plants, light-dependent responses are controlled by a series of Classically, phytochrome responses have been defined by photoreceptors that can be classified into three known groups—the their wavelength and fluence or fluence-rate (i.e. intensity) phytochromes, cryptochromes and phototropins (Quail, 2002a). requirements into three groups—very low fluence responses +Corresponding author. Tel: +39 081 583 3241; Fax +39 081 764 1355; E-mail: [email protected] 1042 EMBO reports vol. 3 | no. 11 | pp 1042–1048 | 2002 © 2002 European Molecular Biology Organization review Phytochrome-mediated photoperception to the nucleus in R-HIR conditions whereas phyA nuclear localization is most effective in FR-HIR conditions. Phytochrome localization to the nucleus is a highly significant finding given that many phytochrome responses are dependent upon changes in gene expression. However, it should be noted that phytochrome translocation is rather slow, except for phyA, and that the majority of the intracellular Pfr pool is not trans- located to the nucleus (Nagy and Schäfer, 2002). These and other observations (see below) suggest that phytochromes may activate signalling pathways in both the cytoplasm and the nucleus. Dissection of phytochrome signal transduction pathways Photomorphogenic mutants. Many putative light signal trans- duction intermediates have been identified from mutant screens aimed principally at isolating mutants insensitive to light or mutants displaying constitutive photomorphogenesis in darkness (Møller et al., 2002). The most severe white light-insensitive mutants include photoreceptor mutants, as well as one mutated in a gene encoding a bZIP transcription factor known as HY5 (Oyama et al., 1997). The severity of this mutant demonstrates that HY5 plays a key role in the control of photomorphogenesis (see below). While hy5 mutants are affected in both phyA and phyB signalling, other mutants are affected in one or the other, the majority being specific for phyA (Møller et al., 2002; Nagy Fig. 1. Phytochrome response modes. (A) The phytochrome photocycle. Pr and Schäfer, 2002; Quail, 2002a). and Pfr denote the red and far red light-absorbing conformations of Most phyA signalling mutants are defective in genes encoding phytochrome, respectively, which are reversible depending on light conditions. Pfr can also be converted to Pr in a light-independent process nuclear-localized proteins, e.g. FHY1, FHY3, SPA1, FAR1, LAF1 known as dark reversion (Nagy and Schäfer, 2002). (B) The different and EID1 (see Møller et al., 2002; Nagy and Schäfer, 2002; phytochrome response modes. The influence of red and far red light on each Quail, 2002a,b; Wang and Deng, 2002). However, some have response mode is shown, together with the phytochrome principally involved mutations in genes encoding the cytoplasmic proteins PAT1, in initiating the response. FIN219 and SUB1. Genetic analyses suggest that, apart from SPA1, EID1 and SUB1, all of these proteins act as positive elements in the pathway, i.e. the mutants display reduced sensi- (VLFR), low fluence responses (LFR) and high irradiance tivity to far red light (Nagy and Schäfer, 2002). Interestingly, responses (HIR) (Figure 1B). HIRs are now further subdivided SPA1 and EID1 play distinct roles in phyA signalling, SPA1 being into red (R)- and far red (FR)-HIRs (Nagy and Schäfer, 2002). primarily involved in VLFR and EIDI in FR-HIR signalling (Zhou Studies with phytochrome-deficient mutants grown in defined et al., 2002). Constitutively photomorphogenic mutants are defective in VLFR, LFR and HIR light environments have revealed that genes encoding the COP/DET/FUS family of proteins. Eleven specific phytochromes can be ascribed to individual responses loci have been assigned to this group (det1, cop1, cop8, cop9, (Figure 1B), although significant redundancy exists (Møller et al., cop10, cop11, cop16, fus5, fus8, fus11 and fus12) (Hardtke and 2002; Nagy and Schäfer, 2002). FR-HIR responses are, however, Deng, 2000). The phenotypes of these mutants indicate that specifically mediated by phyA due to the unusual spectral prop- these genes encode negative regulators of light signalling, all of erties of this phytochrome. It has been proposed that a novel which are localized predominantly within the nucleus (see + form of PrA (denoted Pr A), which has photocycled through Pfr, below). is responsible (Shinomura et al., 2000). Phytochrome-interacting proteins. Attempts to identify phyto- chrome-interacting partners have been most successful using the Phytochrome localization yeast two-hybrid approach. Due to the difficulties of generating a chromophore-reconstituted phytochrome in yeast cells, most In the dark, de novo synthesized phytochrome is in the Pr form yeast two-hybrid experiments have used the C-terminal region. and is localized within the cytoplasm. Upon conversion to Pfr This is far from ideal because the C-termini of phyA and phyB each of the Arabidopsis phytochromes have been found to have been shown to be functionally interchangeable (Quail translocate to the nucleus and to form discrete speckles et al., 1995; Quail, 2002a,b), and because the absence of the (Kircher et al., 2002; Nagy and Schäfer, 2002). The physio- N-terminal chromophore-binding domain presumably creates a logical significance of these observations can be inferred, at least rather artificial bait. Nevertheless, a number of proteins have for phyA and phyB, from the correlations that have been found been identified (Table I). In some cases, these proteins interact between nuclear translocation and response, e.g. phyB localizes with different domains within the phytochrome, but whether EMBO reports vol. 3 | no. 11 | 2002 1043 review E. Schäfer and C. Bowler Table I. Phytochrome-interacting proteins Interacting partner Method Phy A Pfr or Cellular localization Proposed role in phy signalling Reference or B? Pr? ARR4 Y2H B Both N, C Positive regulator of B Sweere et al. (2001) Pull-down Co-IP Aux/IAA Pull-down A Both N Cross-talk with auxin Colón-Carmona et al. (2000) Cry1 Y2H A ? N Photoreceptor co-action Ahmad et al. (1998) Pull-down Cry2 Co-IP B ? N Photoreceptor co-action Màs et al. (2000) FRET ELF3 Y2H B Both N Positive regulator of B in Liu et al. (2001) Pull-down circadian clock NDPK2 Y2H A Pfr>Pr C, N Positive regulator of A and B Choi et al. (1999) Pull-down PIF3 Y2H B(A) Pfr N Positive regulator of B (and A) Ni et al. (1999) Pull-down PIF4 Pull-down B Pfr N Negative regulator of B Huq and Quail (2002) PKS1 Y2H A, B Both C Negative regulator of B Fankhauser et al.
Load more

Recommended publications
  • Effects of Light Regime and Iba Concentration on Adventitious Rooting of an Eastern Cottonwood (Populus Deltoides) Clone
    EFFECTS OF LIGHT REGIME AND IBA CONCENTRATION ON ADVENTITIOUS ROOTING OF AN EASTERN COTTONWOOD (POPULUS DELTOIDES) CLONE Alexander P. Hoffman, Joshua P. Adams, and Andrew Nelson1 Abstract—Eastern cottonwood (Populus deltoides) has received a substantial amount of interest from in- vitro studies within the past decade. The ability to efficiently multiply the stock of established clones such as clone 110412 is a valuable asset for forest endeavors. However, a common problem encountered is initiating adventitious rooting in new micropropagation protocols. Stem segments were collected from bud-broken 1 year old clone 110412 cuttings, sterilized, and stimulated to initiate shoots. Developed shoots (~2 cm in height) were excised and placed into one of three rooting media that included indole-3-butyric acid (IBA) concentrations (0.5 mg/L, 1 mg/L, or 2mg/L) in full strength DKW Medium, full strength Gamborg B5 vitamins, 2 percent sucrose, 0.6 percent agar, 10 mg/L AMP, 0.2 ml/L of Fungigone. In addition to IBA concentration, cuttings were randomly assigned to light rack positions to test the effects of wide spectrum fluorescent light (100 µmol m-2 s-1 photosynthetically active radiation (PAR), 16/8 hour photoperiod) and light emitting diode light (LED; 4:1 red-to-blue diodes, 250 µmol m-2 s-1 PAR, 16/8 hour photoperiod). After a month of exposure, there was limited rooting exhibited across treatments. However, fluorescents (3.58 ± 1.02) produced significantly better performing microcuttings (judged on morphology, visual vigor, and survival) than LEDs (2.7±0.86) (p<0.005). The high light intensity of the LEDs may be prompting weaker performance through unfavorably high transpiration-induced auxin uptake.
    [Show full text]
  • Phytochrome Effects in the Nyctinastic Leaf Movements of Albizzia Julibrissin and Some Other Legumes1 2 William S
    Plant Physiol. (1967) 42, 1413-1418 Phytochrome Effects in the Nyctinastic Leaf Movements of Albizzia julibrissin and Some Other Legumes1 2 William S. Hillman and Willard L. Koukkari Biology Department, Brookhaven National Laboratory, Upton, New York 11973 Received June 5, 1967. Summnary. Participation of phytochrome 'is evident in the nyctinastic responise of leaves of Albizzia julibrissin (silk-tree), Albizzia lophantha, Leucaena glauca, Poinciana gilliesi and Calliandra inequilatera; closure of excised pairs of pinnules upon darkening is rapid following red illumination and slow following far-red. Under good conditions the difiference is obvious within 10 minutes. These observations conifirm a report by Fondeville, Borthwick, and Hendricks on the sensitive plant, Mimosa pudica, but indicate that the efifect bears no necessary relationship to the anomalous sensitivity of Mimosa. In A. julibrissin, phytochrome control is mnarked in experiments conducted early in the daily 12-hour light period and appears absent, or nearly so, toward the end of the light period, perhaps due to interaction with an endogenous circadian rhythm. Effects of leaf maturity and of the position of a pinnule-pair within a leaf are also evident. Tih-ese results are not easily reconciled with hypotheses of phytochrome action through gene activation and nucleic acid synthesis, but are consistent with hypothess ibased onl permeability changes and membrane properties. The mgnitude and reproducibility of the response in A. jutlibrissin suggest its use as a lajboratory exercise; this and related systems should prove valuable for eventuai identification of the mechanism of phytochrome action. Fondeville, Borthwick, and Hendricks (2) re- pinnately twice-compound leaves generally similar in ported on a role of phytochrome in the nyctinastic character to those of Mimosa pudica, (but not obviously response of the sensitive plant, Mimnosa pudica: closure sensitive to the touch.
    [Show full text]
  • Nobel Lecture by Roger Y. Tsien
    CONSTRUCTING AND EXPLOITING THE FLUORESCENT PROTEIN PAINTBOX Nobel Lecture, December 8, 2008 by Roger Y. Tsien Howard Hughes Medical Institute, University of California San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0647, USA. MOTIVATION My first exposure to visibly fluorescent proteins (FPs) was near the end of my time as a faculty member at the University of California, Berkeley. Prof. Alexander Glazer, a friend and colleague there, was the world’s expert on phycobiliproteins, the brilliantly colored and intensely fluorescent proteins that serve as light-harvesting antennae for the photosynthetic apparatus of blue-green algae or cyanobacteria. One day, probably around 1987–88, Glazer told me that his lab had cloned the gene for one of the phycobilipro- teins. Furthermore, he said, the apoprotein produced from this gene became fluorescent when mixed with its chromophore, a small molecule cofactor that could be extracted from dried cyanobacteria under conditions that cleaved its bond to the phycobiliprotein. I remember becoming very excited about the prospect that an arbitrary protein could be fluorescently tagged in situ by genetically fusing it to the phycobiliprotein, then administering the chromophore, which I hoped would be able to cross membranes and get inside cells. Unfortunately, Glazer’s lab then found out that the spontane- ous reaction between the apoprotein and the chromophore produced the “wrong” product, whose fluorescence was red-shifted and five-fold lower than that of the native phycobiliprotein1–3. An enzyme from the cyanobacteria was required to insert the chromophore correctly into the apoprotein. This en- zyme was a heterodimer of two gene products, so at least three cyanobacterial genes would have to be introduced into any other organism, not counting any gene products needed to synthesize the chromophore4.
    [Show full text]
  • Phytochrome and Photosystem I Interaction in a High-Energy
    Proc. Nat. Acad. Sci. USA Vol. 69, No. 8, pp. 2150-2154, August 1972 Phytochrome and Photosystem I Interaction in a High-Energy Photoresponse (photosynthesis/photomorphogenesis/anthocyanin/turnip seedlings) MICHAEL SCHNEIDER AND WILLIAM STIMSON Department of Biological Sciences, Columbia University, New York, N.Y. 10027 Communicated by Sterling B. Hendricks, May £6, 1972 ABSTRACT At least two photoreactions can be demon- HER are based upon phytochrome as the sole strated in plant developmental responses: the low-energy photoreceptor. requiring phytochrome system and the high energy reac- Accordingly, HER are believed to arise through the mainte- tion. The action of these photoreactions on the formation nance of a low level of Pfr over a prolonged time. Indeed, the of anthocyanin by turnip seedlings is discussed. The syn- phytochrome and HER photoreactions appear closely linked, thesis of small amounts of anthocyanin can be controlled since photoresponses that exhibit evidence of a HER also solely by phytochrome, as evidenced by the red-far-red exhibit photoreversible effect of brief irradiations. Appreciable phytochrome photoreversibility under appropriate synthesis requires prolonged irradiations, the duration of conditions. The dependence of HER photoresponses on in- irradiation being more important than intensity. The tensity remains more difficult to explain, and is the principal data presented suggest that the energy dependence of subject of this communication. anthocyanin synthesis arises through photosynthesis. A Originally, the involvement of photosynthesis in HER mechanism for the interaction between photosynthesis was and phytochrome is suggested. Under conditions of natural responses suggested by Hendricks, Borthwick, and their illumination of plants, the concentration of the species of associates (5, 13, 14).
    [Show full text]
  • Which Regions of the Electromagnetic Spectrum Do Plants Use to Drive Photosynthesis?
    Which regions of the electromagnetic spectrum do plants use to drive photosynthesis? Green Light: The Forgotten Region of the Spectrum. In the past, plant physiologists used green light as a safe light during experiments that required darkness. It was assumed that plants reflected most of the green light and that it did not induce photosynthesis. Yes, plants do reflect green light but human vision sensitivity peaks in the green region at about 560 nm, which allows us to preferentially see green. Plants do not reflect all of the green light that falls on them but they reflect enough for us to detect it. Read on to find out what the role of green light is in photosynthesis. The electromagnetic spectrum: Light Visible light ranges from low blue to far-red light and is described as the wavelengths between 380 nm and 750 nm, although this varies between individuals. The region between 400 nm and 700 nm is what plants use to drive photosynthesis and is typically referred to as Photosynthetically Active Radiation (PAR). There is an inverse relationship between wavelength and quantum energy, the higher the wavelength the lower quantum energy and vice versa. Plants use wavelengths outside of PAR for the phenomenon known as photomorphogenesis, which is light regulated changes in development, morphology, biochemistry and cell structure and function. The effects of different wavelengths on plant function and form are complex and are proving to be an interesting area of study for many plant scientists. The use of specific and adjustable LEDs allows us to tease apart the roles of specific areas of the spectrum in photosynthesis.
    [Show full text]
  • Separate Functions for Nuclear and Cytoplasmic Cryptochrome 1 During Photomorphogenesis of Arabidopsis Seedlings
    Separate functions for nuclear and cytoplasmic cryptochrome 1 during photomorphogenesis of Arabidopsis seedlings Guosheng Wu and Edgar P. Spalding† Department of Botany, University of Wisconsin, 430 Lincoln Drive, Madison, WI 53706 Edited by Anthony R. Cashmore, University of Pennsylvania, Philadelphia, PA, and approved October 3, 2007 (received for review May 30, 2007) Cryptochrome blue-light receptors mediate many aspects of plant interaction with the COP1 E3 ligase, a regulator of seedling photomorphogenesis, such as suppression of hypocotyl elongation development (13, 14) that is present in the nucleus until light and promotion of cotyledon expansion and root growth. The stimulates its export to the cytoplasm (15). As a COP1 interactor, cryptochrome 1 (cry1) protein of Arabidopsis is present in the cry1 is believed to exert at least some of its effects by influencing nucleus and cytoplasm of cells, but how the functions of one pool the levels of the HY5 transcription factor, which interacts with differ from the other is not known. Nuclear localization and nuclear the promoters of some light-regulated genes (16). Comparative export signals were genetically engineered into GFP-tagged cry1 transcript-profiling studies performed on cry1 mutant and wild- molecules to manipulate cry1 subcellular localization in a cry1-null type seedlings exposed to blue light identified a large number of mutant background. The effectiveness of the engineering was genes exhibiting cry1-dependent expression at the point in time confirmed by confocal microscopy. The ability of nuclear or cyto- when cry1 begins to influence the rate of hypocotyl elongation, plasmic cry1 to rescue a variety of cry1 phenotypes was deter- which is Ϸ45 min after the onset of irradiation (17).
    [Show full text]
  • Phytochrome Activates the Plastid-Encoded RNA Polymerase for Chloroplast Biogenesis Via Nucleus-To-Plastid Signaling
    ARTICLE https://doi.org/10.1038/s41467-019-10518-0 OPEN Phytochrome activates the plastid-encoded RNA polymerase for chloroplast biogenesis via nucleus-to-plastid signaling Chan Yul Yoo 1, Elise K. Pasoreck1, He Wang1, Jun Cao2, Gregor M. Blaha3, Detlef Weigel2 & Meng Chen 1 Light initiates chloroplast biogenesis by activating photosynthesis-associated genes encoded by not only the nuclear but also the plastidial genome, but how photoreceptors control 1234567890():,; plastidial gene expression remains enigmatic. Here we show that the photoactivation of phytochromes triggers the expression of photosynthesis-associated plastid-encoded genes (PhAPGs) by stimulating the assembly of the bacterial-type plastidial RNA polymerase (PEP) into a 1000-kDa complex. Using forward genetic approaches, we identified REGULATOR OF CHLOROPLAST BIOGENESIS (RCB) as a dual-targeted nuclear/plastidial phytochrome sig- naling component required for PEP assembly. Surprisingly, RCB controls PhAPG expression primarily from the nucleus by interacting with phytochromes and promoting their localization to photobodies for the degradation of the transcriptional regulators PIF1 and PIF3. RCB- dependent PIF degradation in the nucleus signals the plastids for PEP assembly and PhAPG expression. Thus, our findings reveal the framework of a nucleus-to-plastid anterograde signaling pathway by which phytochrome signaling in the nucleus controls plastidial transcription. 1 Department of Botany and Plant Sciences, Institute for Integrative Genome Biology, University of California,
    [Show full text]
  • Regulation of Phytochrome Gene Expression
    Journal of the Iowa Academy of Science: JIAS Volume 98 Number Article 6 1991 Regulation of Phytochrome Gene Expression J. T. Colbert Colorado State University S. A. Costigan Colorado State University P. Avissar Colorado State University Z. Zhao Colorado State University Let us know how access to this document benefits ouy Copyright © Copyright 1991 by the Iowa Academy of Science, Inc. Follow this and additional works at: https://scholarworks.uni.edu/jias Part of the Anthropology Commons, Life Sciences Commons, Physical Sciences and Mathematics Commons, and the Science and Mathematics Education Commons Recommended Citation Colbert, J. T.; Costigan, S. A.; Avissar, P.; and Zhao, Z. (1991) "Regulation of Phytochrome Gene Expression," Journal of the Iowa Academy of Science: JIAS, 98(2), 63-67. Available at: https://scholarworks.uni.edu/jias/vol98/iss2/6 This Research is brought to you for free and open access by the Iowa Academy of Science at UNI ScholarWorks. It has been accepted for inclusion in Journal of the Iowa Academy of Science: JIAS by an authorized editor of UNI ScholarWorks. For more information, please contact [email protected]. )our. Iowa Acad. Sci. 98(2):63-67, 1991 Regulation of Phytochrome Gene Expression J.T. COLBERT\ S.A. COSTIGAN2, P. AVISSAR3 and Z . ZHA04 Department of Biology, Colorado State University, Ft. Collins, CO 80523 In etiolated oat seedlings exposure to red light results in a decrease in the transcription of the phytochrome genes, the abundance of phytochrome mRNA, and the level of phytochrome protein. Phytochrome itself serves as the photoreceptor for the response of decreased mRNA and transcriprion levels.
    [Show full text]
  • Sumoylation of Phytochrome-B Negatively Regulates Light-Induced Signaling in Arabidopsis Thaliana
    SUMOylation of phytochrome-B negatively regulates light-induced signaling in Arabidopsis thaliana Ari Sadanandoma,1, Éva Ádámb, Beatriz Orosaa, András Vicziánb, Cornelia Klosec, Cunjin Zhanga, Eve-Marie Jossed, László Kozma-Bognárb, and Ferenc Nagyb,d,1 aSchool of Biological and Biomedical Sciences, University of Durham, Durham DH1 3LE, United Kingdom; bPlant Biology Institute, Biological Research Centre, H-6726 Szeged, Hungary; cInstitute of Botany, University of Freiburg, D-79104 Freiburg, Germany; and dInstitute of Molecular Plant Science, School of Biology, University of Edinburgh, Edinburgh EH9 3JR, United Kingdom Edited by George Coupland, Max Planck Institute for Plant Breeding Research, Cologne, Germany, and approved July 16, 2015 (received for review August 8, 2014) The red/far red light absorbing photoreceptor phytochrome-B (phyB) steps of phyB signaling include (i) inactivation or alteration of cycles between the biologically inactive (Pr, λmax, 660 nm) and active the substrate specificity of CONSTITUTIVE PHOTOMOR- (Pfr; λmax, 730 nm) forms and functions as a light quality and quantity PHOGENIC 1 (COP1) that targets proteins to degradation (10), controlled switch to regulate photomorphogenesis in Arabidopsis. (ii) degradation and/or modulation of the transcriptional activity At the molecular level, phyB interacts in a conformation-dependent of negative regulatory PIF TFs (11), and (iii) induction of trans- fashion with a battery of downstream regulatory proteins, including criptional cascades that modulate the expression of 2,500–3,000 PHYTOCHROME INTERACTING FACTOR transcription factors, and genes of the Arabidopsis genome (12). by modulating their activity/abundance, it alters expression pat- The number of phyB Pfr molecules quantitatively determines terns of genes underlying photomorphogenesis.
    [Show full text]
  • Phytochrome Diversity in Green Plants and the Origin of Canonical Plant Phytochromes
    ARTICLE Received 25 Feb 2015 | Accepted 19 Jun 2015 | Published 28 Jul 2015 DOI: 10.1038/ncomms8852 OPEN Phytochrome diversity in green plants and the origin of canonical plant phytochromes Fay-Wei Li1, Michael Melkonian2, Carl J. Rothfels3, Juan Carlos Villarreal4, Dennis W. Stevenson5, Sean W. Graham6, Gane Ka-Shu Wong7,8,9, Kathleen M. Pryer1 & Sarah Mathews10,w Phytochromes are red/far-red photoreceptors that play essential roles in diverse plant morphogenetic and physiological responses to light. Despite their functional significance, phytochrome diversity and evolution across photosynthetic eukaryotes remain poorly understood. Using newly available transcriptomic and genomic data we show that canonical plant phytochromes originated in a common ancestor of streptophytes (charophyte algae and land plants). Phytochromes in charophyte algae are structurally diverse, including canonical and non-canonical forms, whereas in land plants, phytochrome structure is highly conserved. Liverworts, hornworts and Selaginella apparently possess a single phytochrome, whereas independent gene duplications occurred within mosses, lycopods, ferns and seed plants, leading to diverse phytochrome families in these clades. Surprisingly, the phytochrome portions of algal and land plant neochromes, a chimera of phytochrome and phototropin, appear to share a common origin. Our results reveal novel phytochrome clades and establish the basis for understanding phytochrome functional evolution in land plants and their algal relatives. 1 Department of Biology, Duke University, Durham, North Carolina 27708, USA. 2 Botany Department, Cologne Biocenter, University of Cologne, 50674 Cologne, Germany. 3 University Herbarium and Department of Integrative Biology, University of California, Berkeley, California 94720, USA. 4 Royal Botanic Gardens Edinburgh, Edinburgh EH3 5LR, UK. 5 New York Botanical Garden, Bronx, New York 10458, USA.
    [Show full text]
  • Molecular Mechanisms of Phytochrome Signal Transduction in Higher Plants
    Colloids and Surfaces B: Biointerfaces 45 (2005) 154–161 Molecular mechanisms of phytochrome signal transduction in higher plants Li-Ye Chu a,b,1, Hong-Bo Shao a,b,c,∗,1, Mao-Yau Li a a Molecular Biology Laboratory, Bio-informatics College, Chongqing University of Posts & Telecommunications, Chongqing 400065, PR China b Biological Laboratory, Chemical Engineering College, Qingdao University of Science and Technology, Qingdao 266042, China c The State Key Laboratory of Soil Erosion and Dryland Farming on the Loess Plateau, The Centre of Soil and Water Conservation and Eco-environmental Research, The Chinese Academy of Sciences and Northwest Sci-tech University of Agriculture and Forestry, Yangling 712100, PR China Received 9 May 2005; accepted 28 May 2005 Abstract Phytochromes in higher plants play a great role in development, responses to environmental stresses and signal transduction, which are the fundamental principles for higher plants to be adapted to changing environment. Deep and systematic understanding of the phytochrome in higher plants is of crucial importance to molecular biology, purposeful improvement of environment in practice, especially molecular mechanism by which higher plants perceive UV-B stress. The last more than 10 years have seen rapid progress in this field with the aid of a combination of molecular, genetic and cell biological approaches. No doubt, what is the most important, is the application of Arabidopsis experimental system and the generation of various mutants regarding phytochromes (phy A–E). Increasing evidence demonstrates that phytochrome signaling transduction constitutes a highly ordered multidimensional network of events. Some phytochromes and signaling intermediates show light-dependent nuclear-cytoplasmic partitioning, which implies that early signaling events take place in the nucleus and that subcellular localization patterns most probably represent an important signaling control point.
    [Show full text]
  • The Growing and Glowing Toolbox of Fluorescent and Photoactive Proteins
    UC San Diego UC San Diego Previously Published Works Title The Growing and Glowing Toolbox of Fluorescent and Photoactive Proteins. Permalink https://escholarship.org/uc/item/6jx417t1 Journal Trends in biochemical sciences, 42(2) ISSN 0968-0004 Authors Rodriguez, Erik A Campbell, Robert E Lin, John Y et al. Publication Date 2017-02-01 DOI 10.1016/j.tibs.2016.09.010 Peer reviewed eScholarship.org Powered by the California Digital Library University of California HHS Public Access Author manuscript Author ManuscriptAuthor Manuscript Author Trends Biochem Manuscript Author Sci. Author Manuscript Author manuscript; available in PMC 2018 February 01. Published in final edited form as: Trends Biochem Sci. 2017 February ; 42(2): 111–129. doi:10.1016/j.tibs.2016.09.010. The growing and glowing toolbox of fluorescent and photoactive proteins Erik A. Rodriguez1, Robert E. Campbell2, John Y. Lin3, Michael Z. Lin4, Atsushi Miyawaki5, Amy E. Palmer6, Xiaokun Shu7, Jin Zhang1, and Roger Y. Tsien1,8 1Department of Pharmacology, University of California, San Diego, La Jolla, California, 92093, USA. 2Department of Chemistry, University of Alberta, Edmonton, Alberta, T6G 2G2, Canada. 3School of Medicine, University of Tasmania, Hobart, Tasmania, 7000, Australia. 4Department of Bioengineering, Stanford University, Stanford, CA, 94305, USA and Department of Pediatrics, Stanford University, Stanford, CA, 94305, USA. 5Laboratory for Cell Function Dynamics, Brain Science Institute, RIKEN, 2-1 Hirosawa, Wako, Saitama, 351-0198, Japan. 6Department of Chemistry and Biochemistry, BioFrontiers Institute, University of Colorado Boulder, CO, 80303, USA. 7Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA, 94158, USA and Cardiovascular Research Institute, University of California, San Francisco, San Francisco, CA, 94158, USA.
    [Show full text]