Biosynthesis and Biological Functions of Bilins

Frankenberg, Nicole; Lagarias, J. Clark

doi:10.1016/b978-0-08-092387-1.50013-8

Cited by 74 publications

(88 citation statements)

References 156 publications

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“…In contrast, HMOX1ΔTP exclusively yielded the IXα isomer (Fig. 1B), consistent with high-throughput mammalian, cyanobacterial, and plant heme oxygenases that are coupled with an NADPH-dependent BV reductase (BVR) or with a ferredoxin-dependent bilin reductase (FDBR) such as PCYA or HY2 (31,32). Heme oxygenases with relaxed regiospecificity similar to that of HMOX2 have been documented from insects, organisms that lack light-harvesting biliproteins, oxygen-carrying hemoproteins, and α-specific BV reductases (34).…”

Section: Rna-seq Analysissupporting

confidence: 72%

“…Both genes are found in the nuclear genome and encode proteins with apparent plastid targeting sequences (Fig. S1), which is consistent with plastid synthesis of the known bilin precursors of phytochromes, phycocyanobilin (PCB) and phytochromobilin (PΦB), in streptophytes (31). Chlorophytes also possess a second heme oxygenase gene (HMOX2).…”

Section: Rna-seq Analysissupporting

confidence: 67%

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Retrograde bilin signaling enables Chlamydomonas greening and phototrophic survival

Duanmu

Casero

Dent

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

111

172

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The maintenance of functional chloroplasts in photosynthetic eukaryotes requires real-time coordination of the nuclear and plastid genomes. Tetrapyrroles play a significant role in plastid-tonucleus retrograde signaling in plants to ensure that nuclear gene expression is attuned to the needs of the chloroplast. Well-known sites of synthesis of chlorophyll for photosynthesis, plant chloroplasts also export heme and heme-derived linear tetrapyrroles (bilins), two critical metabolites respectively required for essential cellular activities and for light sensing by phytochromes. Here we establish that Chlamydomonas reinhardtii, one of many chlorophyte species that lack phytochromes, can synthesize bilins in both plastid and cytosol compartments. Genetic analyses show that both pathways contribute to iron acquisition from extracellular heme, whereas the plastid-localized pathway is essential for light-dependent greening and phototrophic growth. Our discovery of a bilin-dependent nuclear gene network implicates a widespread use of bilins as retrograde signals in oxygenic photosynthetic species. Our studies also suggest that bilins trigger critical metabolic pathways to detoxify molecular oxygen produced by photosynthesis, thereby permitting survival and phototrophic growth during the light period.biliverdin | heme oxygenase | iron homeostasis | oxidative stress | RNA-Seq analysisT he daily light-dark cycle requires all oxygenic photosynthetic species to survive the repeated transition from prolonged darkness to phototrophic metabolism at dawn. Most plants are unable to synthesize chlorophyll in darkness and therefore accumulate photosensitizing chlorophyll precursors at night (1). Sunrise induces an oxidative burst as photosynthesis resumes, so the transition to daylight requires careful coordination of many lightdependent processes. Multiple photoreceptors perform such roles in plants, the most notable being the red-sensing, linear tetrapyrrole (bilin)-based phytochromes and the blue-sensing, flavin-based cryptochromes and phototropins (2-5). Bilins are well-established plant retrograde signals, synthesized in plastids but enabling light sensing by cytosolic phytochromes. Phytochrome photoconversion then triggers nuclear translocation to positively regulate photosynthesis-associated nuclear gene (PhANG) expression (6, 7).Genetic studies suggest that plastids also export negative retrograde signals, metabolites that suppress nuclear gene networks targeted by phytochromes (8-10). Among these metabolites are abscisic acid (ABA) (11), tetrapyrroles (12-14), 3′-phosphoadenosine 5′-phosphate (PAP) (15), β-cyclocitral (16), and methylerythritol cyclodiphosphate (MEcPP) (17). Although hypothetical export of a negative tetrapyrrole signal has received considerable support, biochemical evidence for such a retrograde signal remains equivocal in plants (18)(19)(20). Chlorophyte algae diverged from the streptophyte plant lineage over 500 million years ago but share a common chlorophyll a/b-based photosynthetic lightharvesting app...

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Section: Rna-seq Analysissupporting

confidence: 72%

Section: Rna-seq Analysissupporting

confidence: 67%

Retrograde bilin signaling enables Chlamydomonas greening and phototrophic survival

Duanmu

Casero

Dent

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

111

172

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“…31 However, PEBchromophorylated GAFs did not form well in E. coli cells following this protocol. 9,21 Changing to PebS was more effective, 22 as it generates PEB from biliverdin as a single enzyme.…”

Section: Autocatalytic Chromophorylation Of Gafs With Pebmentioning

confidence: 88%

Orange fluorescent proteins constructed from cyanobacteriochromes chromophorylated with phycoerythrobilin

Sun

Tang

et al. 2014

Photochem Photobiol Sci

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Cyanobacteriochromes are a structurally and spectrally highly diverse class of phytochrome-related photosensory biliproteins. They contain one or more GAF domains that bind phycocyanobilin (PCB) autocatalytically; some of these proteins are also capable of further modifying PCB to phycoviolobilin or rubins. We tested the chromophorylation with the non-photochromic phycoerythrobilin (PEB) of 16 cyanobacteriochrome GAFs from Nostoc sp. PCC 7120, of Slr1393 from Synechocystis sp. PCC 6803, and of Tlr0911 from Thermosynechococcus elongatus BP-1. Nine GAFs could be autocatalytically chromophorylated in vivo/in E. coli with PEB, resulting in highly fluorescent biliproteins with brightness comparable to that of fluorescent proteins like GFP. In several GAFs, PEB was concomitantly converted to phycourobilin (PUB) during binding. This not only shifted the spectra, but also increased the Stokes shift.The chromophorylated GAFs could be oligomerized further by attaching a GCN4 leucine zipper domain, thereby enhancing the absorbance and fluorescence of the complexes. The presence of both PEB and PUB makes these oligomeric GAF-"bundles" interesting models for energy transfer akin to the antenna complexes found in cyanobacterial phycobilisomes. The thermal and photochemical stability and their strong brightness make these constructs promising orange fluorescent biomarkers.

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“…Phytobilins can be found in photosynthetic organisms ranging from aquatic prokaryotes to multicellular land plants (2). In cyanobacteria, red algae and cryptomonads, FDBRs function not only to synthesize the phytobilin precursors of the light harvesting phycobiliprotein antennae, but the light sensing phytochromes and cyanobacteriochromes as well.…”

Section: Discussionmentioning

confidence: 99%

“…A wide variety of open-chain tetrapyrroles are present in photosynthetic and nonphotosynthetic organisms. The majority of them are found in the phycobiliproteins of pelagic phytoplankton, e.g., phycoerythrin and phycocyanin, where they function as light-harvesting chromophores (2,3). Some of them, like phytochromobilin (PΦB), phycocyanobilin (PCB), and biliverdin IXα (BV), can also act as the chromophores of phytochromes (4).…”

mentioning

confidence: 99%

Distinct phytochrome actions in nonvascular plants revealed by targeted inactivation of phytobilin biosynthesis

Chen

2012

Proc. Natl. Acad. Sci. U.S.A.

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The red/far-red light photoreceptor phytochrome mediates photomorphological responses in plants. For light sensing and signaling, phytochromes need to associate with open-chain tetrapyrrole molecules as the chromophore. Biosynthesis of tetrapyrrole chromophores requires members of ferredoxin-dependent bilin reductases (FDBRs). It was shown that LONG HYPOCOTYL 2 (HY2) is the only FDBR in flowering plants producing the phytochromobilin (PΦB) for phytochromes. However, in the moss Physcomitrella patens, we found a second FDBR that catalyzes the formation of phycourobilin (PUB), a tetrapyrrole pigment usually found as the protein-bound form in cyanobacteria and red algae. Thus, we named the enzyme PUB synthase (PUBS). Severe photomorphogenic phenotypes, including the defect of phytochrome-mediated phototropism, were observed in Physcomitrella patens when both HY2 and PUBS were disrupted by gene targeting. This indicates HY2 and PUBS function redundantly in phytochrome-mediated responses of nonvascular plants. Our studies also show that functional PUBS orthologs are found in selected lycopod and chlorophyte genomes. Using mRNA sequencing for transcriptome profiling, we demonstrate that expression of the majority of red-light-responsive genes are misregulated in the pubs hy2 double mutant. These studies showed that moss phytochromes rapidly repress expression of genes involved in cell wall organization, transcription, hormone responses, and protein phosphorylation but activate genes involved in photosynthesis and stress signaling during deetiolation. We propose that, in nonvascular plants, HY2 and PUBS produce structurally different but functionally similar chromophore precursors for phytochromes. Holophytochromes regulate biological processes through light signaling to efficiently reprogram gene expression for vegetative growth in the light.

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Biosynthesis and Biological Functions of Bilins

Cited by 74 publications

References 156 publications

Retrograde bilin signaling enables Chlamydomonas greening and phototrophic survival

Retrograde bilin signaling enables Chlamydomonas greening and phototrophic survival

Orange fluorescent proteins constructed from cyanobacteriochromes chromophorylated with phycoerythrobilin

Distinct phytochrome actions in nonvascular plants revealed by targeted inactivation of phytobilin biosynthesis

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