The methylotrophic yeast Pichia pastoris synthesizes a functionally active chromophore precursor of the plant photoreceptor phytochrome.

Wu, Shu-Hsing; Lagarias, J. Clark

doi:10.1073/pnas.93.17.8989

Cited by 31 publications

(22 citation statements)

References 33 publications

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“…Recombinant phyA and phyB purified from a variety of sources (different yeast species and E. coli) confirm this view (Kunkel et al 1996). Even recombinant algal phytochrome displays a similar absorption spectrum (Wu & Lagarias 1996). Thus it is likely that all phytochromes possess similar spectral properties.…”

Section: Structure and Function Analysissupporting

confidence: 54%

Light Control of Plant Development

Fankhauser

Chory

1997

Annu. Rev. Cell Dev. Biol.

441

267

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▪ Abstract To grow and develop optimally, all organisms need to perceive and process information from both their biotic and abiotic surroundings. A particularly important environmental cue is light, to which organisms respond in many different ways. Because they are photosynthetic and non-motile, plants need to be especially plastic in response to their light environment. The diverse responses of plants to light require sophisticated sensing of its intensity, direction, duration, and wavelength. The action spectra of light responses provided assays to identify three photoreceptor systems absorbing in the red/far-red, blue/near-ultraviolet, and ultraviolet spectral ranges. Following absorption of light, photoreceptors interact with other signal transduction elements, which eventually leads to many molecular and morphological responses. While a complete signal transduction cascade is not known yet, molecular genetic studies using the model plant Arabidopsis have led to substantial progress in dissecting the signal transduction network. Important gains have been made in determining the function of the photoreceptors, the terminal response pathways, and the intervening signal transduction components.

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Section: Structure and Function Analysissupporting

confidence: 54%

Light Control of Plant Development

Fankhauser

Chory

1997

Annu. Rev. Cell Dev. Biol.

441

267

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“…2 Although it is not known at present, cyanobacteria may be capable of synthesizing P⌽B based on the hypothesis that the cyanobacterial family of eubacteria are the progenitors of the rhodophyte plastids. Together with the presence of P⌽B synthase activity in yeast, Pichia pastoris (21), it is tempting to speculate that P⌽B synthase, the enzyme catalyzing BV reduction to P⌽B, was present in the primitive ancestor for all extant organisms.…”

Section: Figmentioning

confidence: 99%

Phycocyanobilin Is the Natural Precursor of the Phytochrome Chromophore in the Green Alga Mesotaenium caldariorum

McDowell

Lagarias

1997

Journal of Biological Chemistry

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Compared with phytochromes isolated from etiolated higher plant tissues and a number of lower plant species, the absorption spectrum of phytochrome isolated from the unicellular green alga Mesotaenium caldariorum is blue-shifted (Kidd, D. G., and Lagarias, J. C. (1990) J. Biol. Chem. 265, 7029 -7035). The present studies were undertaken to determine whether this blue shift is due to a chromophore other than phytochromobilin or reflects a different protein environment for the phytochromobilin prosthetic group. Using reversed phase high performance liquid chromatography, we show that soluble protein extracts prepared from algal chloroplasts contain the enzyme activities for ferredoxin-dependent conversions of biliverdin IX␣ to (3Z)-phytochromobilin and (3Z)-phytochromobilin to (3Z)-phycocyanobilin. In vitro assembly of recombinant algal apophytochrome was undertaken with (3E)-phytochromobilin and (3E)-phycocyanobilin. The difference spectrum of the (3E)-phycocyanobilin adduct was indistinguishable from that of phytochrome isolated from dark-adapted algal cells, while the (3E)-phytochromobilin adduct displayed red-shifted absorption maxima relative to purified algal phytochrome. These studies indicate that phycocyanobilin is the immediate precursor of the green algal phytochrome chromophore and that phytochromobilin is an intermediate in its biosynthesis in Mesotaenium.

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“…Recombinant proteins were expressed in Escherichia coli M15[pREP] (Qiagen) and purified by affinity chromatography as described (Kim et al, 1997). Expression in the yeast Saccharomyces cerevisiae of Strep-tagged phyA from oat (Avena sativa), purification of the recombinant protein, and chromophore attachment were performed as described (Wu and Lagarias, 1996;Murphy and Lagarias, 1997).…”

Section: Plasmid Construction and Purification Of Recombinant Proteinsmentioning

confidence: 99%

Aux/IAA Proteins Are Phosphorylated by Phytochrome in Vitro

et al. 2000

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Auxin/indole-3-acetic acid (Aux/IAA) genes encode short-lived transcription factors that are induced as a primary response to the plant growth hormone IAA or auxin. Gain-of-function mutations in Arabidopsis genes, SHY2/IAA3, AXR3/IAA17, and AXR2/IAA7 cause pleiotropic phenotypes consistent with enhanced auxin responses, possibly by increasing Aux/IAA protein stability. Semidominant mutations shy2-1D, shy2-2, axr3-1, and axr2-1 induce ectopic light responses in dark-grown seedlings. Because genetic studies suggest that the shy2-1D and shy2-2 mutations bypass phytochrome requirement for certain aspects of photomorphogenesis, we tested whether SHY2/IAA3 and related Aux/IAA proteins interact directly with phytochrome and whether they are substrates for its protein kinase activity. Here we show that recombinant Aux/IAA proteins from Arabidopsis and pea (Pisum sativum) interact in vitro with recombinant phytochrome A from oat (Avena sativa). We further show that recombinant SHY2/IAA3, AXR3/IAA17, IAA1, IAA9, and Ps-IAA4 are phosphorylated by recombinant oat phytochrome A in vitro. Deletion analysis of Ps-IAA4 indicates that phytochrome A phosphorylation occurs on the N-terminal half of the protein. Metabolic labeling and immunoprecipitation studies with affinity-purified antibodies to IAA3 demonstrate increased in vivo steady-state levels of mutant IAA3 in shy2-2 plants and phosphorylation of the SHY2-2 protein in vivo. Phytochrome-dependent phosphorylation of Aux/IAA proteins is proposed to provide one molecular mechanism for integrating auxin and light signaling in plant development.

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The methylotrophic yeast Pichia pastoris synthesizes a functionally active chromophore precursor of the plant photoreceptor phytochrome.

Cited by 31 publications

References 33 publications

Light Control of Plant Development

Light Control of Plant Development

Phycocyanobilin Is the Natural Precursor of the Phytochrome Chromophore in the Green Alga Mesotaenium caldariorum

Aux/IAA Proteins Are Phosphorylated by Phytochrome in Vitro

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