Photomorphogenesis in Plants

Kendrick, Richard E.; Kronenberg, G. H. M.

doi:10.1111/j.1751-1097.1990.tb01746.x

Cited by 160 publications

(107 citation statements)

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“…Light triggers a developmental program in plants that leads to photoautotrophic capacity (Kendrick and Kronenberg, 1994). A key step in this process is the biogenesis of chloroplasts from undifferentiated proplastids (Bauer et al, 2001).…”

Section: Introductionmentioning

confidence: 99%

AtToc90, a New GTP-Binding Component of the Arabidopsis Chloroplast Protein Import Machinery

et al. 2004

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AtToc159 is a GTP-binding chloroplast protein import receptor. In vivo, atToc159 is required for massive accumulation of photosynthetic proteins during chloroplast biogenesis. Yet, in mutants lacking atToc159 photosynthetic proteins still accumulate, but at strongly reduced levels whereas non-photosynthetic proteins are imported normally: This suggests a role for the homologues of atToc159 (atToc132, -120 and -90). Here, we show that atToc90 supports accumulation of photosynthetic proteins in plastids, but is not required for import of several constitutive proteins. Part of atToc90 associates with the chloroplast surface in vivo and with the Toc-complex core components (atToc75 and atToc33) in vitro suggesting a function in chloroplast protein import similar to that of atToc159. As both proteins specifically contribute to the accumulation of photosynthetic proteins in chloroplasts they may be components of the same import pathway.

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Section: Introductionmentioning

confidence: 99%

AtToc90, a New GTP-Binding Component of the Arabidopsis Chloroplast Protein Import Machinery

et al. 2004

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“…The developmental changes occurring during photomorphogenesis in plants are mediated by severa1 photoreceptor systems that respond to particular wavelengths and intensities of light; these include phytochromes, the bluelultraviolet (UV)-A photoreceptors, and the UV-B photoreceptor (reviewed in Kendrick and Kronenberg, 1993;Ahmad and Cashmore, 1993). Phytochrome is a red/far-red-light-photoreversible chromoprotein that is synthesized in its physiologically inactive form (Pr) and converted to its active form (Pfr) by red light irradiation (Furuya, 1993).…”

Section: Introductionmentioning

confidence: 99%

Light-regulated modification and nuclear translocation of cytosolic G-box binding factors in parsley.

et al. 1994

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Functional cell-free systems may be excellent tools with which to investigate light-dependent signal transduction mechanisms in plants. By evacuolation of parsley protoplasts and subsequent silicon oil gradient centrifugation of lysed evacuolated protoplasts, we obtained a highly pure and concentrated plasma membrane-containing cytosol. Using GTand G-box DNA elements, we were able to demonstrate a specific localization of a pool of G-box binding activity and factors (GBFs) but not one of GT-box binding activity in this cytosolic fraction. The DNA binding activity of the cytosolic GBFs is modulated in vivo as well as in vitro by light and phosphorylation/dephosphorylation activities. The regulation of cytosolic G-box binding activity by irradiation with continuous white light and phosphorylation correlates with a lightmodulated transport of GBFs to the nucleus. This was shown by a GBF-antibody cotranslocation assay in permeabilized, cell-free evacuolated parsley protoplasts. We propose that a light-regulated subcellular displacement of cytosolic GBFs to the nucleus may be an important step in the signal transduction pathway coupling photoreception to light-dependent gene expression.

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“…Light is used not only as the energy source for photosynthesis, but also as a major environmental signal. To monitor changes in light quality and quantity and to regulate temporal and spatial patterns in photomorphogenesis, plants have evolved at least three different photoreceptor systems: UVB photoreceptors, blue UVA photoreceptors, and phytochromes (1). Of these photoreceptors, the phytochromes are the best characterized.…”

mentioning

confidence: 99%

“…Five genes encoding phytochrome apoproteins have been identified in Arabidopsis (2,3). Mutants of phyA, 1 phyB, and phytochrome D in Arabidopsis have different effects on photomorphogenesis (4 -8). The dominant phytochrome of etiolated seedlings, the light-labile phyA, controls the very low fluence and the high irradiance responses, whereas the dominant phytochrome of green seedlings and mature plants, the light-stable phyB, controls responses governed by red/far-red reversibility or continuous red light (9).…”

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confidence: 99%

In Vivo Characterization of Chimeric Phytochromes in Yeast

Eichenberg

Kunkel

Kretsch

et al. 1999

Journal of Biological Chemistry

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Phytochromes are plant photoreceptors that play a major role in photomorphogenesis. Two members of the phytochrome family have been characterized in some detail. Phytochrome A, which controls very low fluence and high irradiance responses, is rapidly degraded in the light, forms sequestered areas of phytochrome (SAPs), and does not exhibit dark reversion in monocotyledonous seedlings. Phytochrome B mediates red/ far-red reversible responses, is stable in the light, and does not form SAPs. We report on the behavior in yeast of the phytochrome apoproteins of rice PHYA, tobacco PHYB, and chimeric PHYAB and PHYBA and on the behavior of the respective holoprotein adducts after assembly with phycocyanobilin chromophore (PHY*). SAP-like formation in yeast was not observed for PHYB, but was detectable for PHYA, PHYAB, and PHYBA. Rice PHYA* did not undergo dark reversion in yeast. Surprisingly, all other tested phytochrome constructs did exhibit dark reversion, including chimeric phytochromes with a short N-terminal part of tobacco PHYB or parsley PHYA fused to rice PHYA. Furthermore, the proportion of phytochrome undergoing dark reversion and the rate of reversion were increased for both the N terminusswapped constructs and PHYBA*. These results are discussed with respect to structure/function analysis of phytochromes A and B.

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Photomorphogenesis in Plants

Cited by 160 publications

References 0 publications

AtToc90, a New GTP-Binding Component of the Arabidopsis Chloroplast Protein Import Machinery

AtToc90, a New GTP-Binding Component of the Arabidopsis Chloroplast Protein Import Machinery

Light-regulated modification and nuclear translocation of cytosolic G-box binding factors in parsley.

In Vivo Characterization of Chimeric Phytochromes in Yeast

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