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  1 / 143 MEDLINE  
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[PMID]:28371229
[Au] Autor:Mackey KRM; Post AF; McIlvin MR; Saito MA
[Ad] Endereço:Earth System Science, University of California Irvine, Irvine, CA, 92697, USA.
[Ti] Título:Physiological and proteomic characterization of light adaptations in marine Synechococcus.
[So] Source:Environ Microbiol;19(6):2348-2365, 2017 Jun.
[Is] ISSN:1462-2920
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Marine Synechococcus thrive over a range of light regimes in the ocean. We examined the proteomic, genomic and physiological responses of seven Synechococcus isolates to moderate irradiances (5-80 µE m s ), and show that Synechococcus spans a continuum of light responses ranging from low light optimized (LLO) to high light optimized (HLO). These light responses are linked to phylogeny and pigmentation. Marine sub-cluster 5.1A isolates with higher phycouribilin: phycoerythrobilin ratios fell toward the LLO end of the continuum, while sub-cluster 5.1B, 5.2 and estuarine Synechococcus with less phycouribilin fell toward the HLO end of the continuum. Global proteomes were highly responsive to light, with > 50% of abundant proteins varying more than twofold between the lowest and highest irradiance. All strains downregulated phycobilisome proteins with increasing irradiance. Regulation of proteins involved in photosynthetic electron transport, carbon fixation, oxidative stress protection (superoxide dismutases) and iron and nitrogen metabolism varied among strains, as did the number of high light inducible protein (Hlip) and DNA photolyase genes in their genomes. All but one LLO strain possessed the photoprotective orange carotenoid protein (OCP). The unique combinations of light responses in each strain gives rise to distinct photophysiological phenotypes that may affect Synechococcus distributions in the ocean.
[Mh] Termos MeSH primário: Transporte de Elétrons/genética
Fotossíntese/genética
Ficobilinas/metabolismo
Ficoeritrina/metabolismo
Synechococcus/genética
Synechococcus/fisiologia
Urobilina/análogos & derivados
[Mh] Termos MeSH secundário: Adaptação Ocular
Ciclo do Carbono/genética
Luz
Estresse Oxidativo/genética
Ficobilissomas/metabolismo
Filogenia
Proteômica
Synechococcus/isolamento & purificação
Urobilina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Phycobilins); 0 (Phycobilisomes); 11016-17-4 (Phycoerythrin); 18097-67-1 (phycoerythrobilin); 1856-98-0 (Urobilin); 61932-71-6 (phycourobilin)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171109
[Lr] Data última revisão:
171109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170404
[St] Status:MEDLINE
[do] DOI:10.1111/1462-2920.13744


  2 / 143 MEDLINE  
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[PMID]:27668842
[Au] Autor:Xia X; Partensky F; Garczarek L; Suzuki K; Guo C; Yan Cheung S; Liu H
[Ad] Endereço:Division of Life Science, The Hong Kong University of Science and Technology, Hong Kong.
[Ti] Título:Phylogeography and pigment type diversity of Synechococcus cyanobacteria in surface waters of the northwestern pacific ocean.
[So] Source:Environ Microbiol;19(1):142-158, 2017 Jan.
[Is] ISSN:1462-2920
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The widespread unicellular cyanobacteria Synechococcus are major contributors to global marine primary production. Here, we report their abundance, phylogenetic diversity (as assessed using the RNA polymerase gamma subunit gene rpoC1) and pigment diversity (as indirectly assessed using the laterally transferred cpeBA genes, encoding phycoerythrin-I) in surface waters of the northwestern Pacific Ocean, sampled over nine distinct cruises (2008-2015). Abundance of Synechococcus was low in the subarctic ocean and South China Sea, intermediate in the western subtropical Pacific Ocean, and the highest in the Japan and East China seas. Clades I and II were by far the most abundant Synechococcus lineages, the former dominating in temperate cold waters and the latter in (sub)tropical waters. Clades III and VI were also fairly abundant in warm waters, but with a narrower distribution than clade II. One type of chromatic acclimater (3dA) largely dominated the Synechococcus communities in the subarctic ocean, while another (3dB) and/or cells with a fixed high phycourobilin to phycoerythrobilin ratio (pigment type 3c) predominated at mid and low latitudes. Altogether, our results suggest that the variety of pigment content found in most Synechococcus clades considerably extends the niches that they can colonize and therefore the whole genus habitat.
[Mh] Termos MeSH primário: Pigmentos Biológicos/metabolismo
Água do Mar/microbiologia
Synechococcus/classificação
Synechococcus/genética
Synechococcus/metabolismo
[Mh] Termos MeSH secundário: China
Ecossistema
Japão
Oceano Pacífico
Ficobilinas/análise
Ficobilinas/metabolismo
Ficoeritrina/análise
Ficoeritrina/metabolismo
Filogenia
Filogeografia
Pigmentos Biológicos/análise
Synechococcus/isolamento & purificação
Urobilina/análogos & derivados
Urobilina/análise
Urobilina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Phycobilins); 0 (Pigments, Biological); 11016-17-4 (Phycoerythrin); 18097-67-1 (phycoerythrobilin); 1856-98-0 (Urobilin); 61932-71-6 (phycourobilin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170913
[Lr] Data última revisão:
170913
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160927
[St] Status:MEDLINE
[do] DOI:10.1111/1462-2920.13541


  3 / 143 MEDLINE  
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[PMID]:27495242
[Au] Autor:Bemal S; Anil AC
[Ad] Endereço:School of Oceanography, Academy of Scientific and Innovative Research, Council of Scientific and Industrial Research, National Institute of Oceanography (CSIR-NIO), Dona-Paula 403004, Goa, India.
[Ti] Título:Genetic and ecophysiological traits of Synechococcus strains isolated from coastal and open ocean waters of the Arabian Sea.
[So] Source:FEMS Microbiol Ecol;92(11), 2016 Nov.
[Is] ISSN:1574-6941
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The picocyanobacterium Synechococcus is a prominent primary producer in the marine environment. The marine Synechococcus strains are clustered into different clades representing ecologically distinct genotypes. In this study, we compared phylogeny, photophysiology and cell cycles of four novel phycoerythrin-containing Synechococcus strains (clade II of subcluster 5.1) isolated from different depths of the water column (surface and subsurface waters) in coastal and offshore regions of the eastern Arabian Sea. The surface water strains possessed a lesser number of thylakoid layers and had a higher zeaxanthin to chlorophyll a ratio than subsurface strains indicating possible influence of light intensity available at their niche. The DNA distribution pattern of the four strains was bimodal in optimal cellular physiology conditions with cell division restricted to the light period and synchronized with the light-dark cycle. The presence of phycourobilin or phycoerythrobilin and the ratio between these two chromophores in all four strains varied according to available spectral wavelength in situ This study indicates that the timing of cell division is conserved within these genotypically identical Synechococcus strains, despite their having different chromophore ratios. We conclude that the timing of cell division of the Synechococcus strains has a genetic basis rather than being determined by phenotypic characters, such as chromophore content and ratio.
[Mh] Termos MeSH primário: Divisão Celular/genética
Fotossíntese/fisiologia
Synechococcus/crescimento & desenvolvimento
Synechococcus/fisiologia
[Mh] Termos MeSH secundário: Ásia Ocidental
Divisão Celular/fisiologia
Clorofila/análogos & derivados
Clorofila/metabolismo
DNA Bacteriano/genética
Luz
Microscopia Eletrônica de Transmissão
Oceanos e Mares
Fenótipo
Ficobilinas/metabolismo
Ficoeritrina/metabolismo
Filogenia
Synechococcus/genética
Synechococcus/isolamento & purificação
Urobilina/análogos & derivados
Urobilina/metabolismo
Água/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Bacterial); 0 (Phycobilins); 059QF0KO0R (Water); 11016-17-4 (Phycoerythrin); 1406-65-1 (Chlorophyll); 18097-67-1 (phycoerythrobilin); 1856-98-0 (Urobilin); 22309-13-3 (chlorophyll a'); 61932-71-6 (phycourobilin); YF5Q9EJC8Y (chlorophyll a)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170713
[Lr] Data última revisão:
170713
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160807
[St] Status:MEDLINE


  4 / 143 MEDLINE  
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[PMID]:24799690
[Au] Autor:Bixler JN; Cone MT; Hokr BH; Mason JD; Figueroa E; Fry ES; Yakovlev VV; Scully MO
[Ad] Endereço:Texas A&M University, College Station, TX 77843;
[Ti] Título:Ultrasensitive detection of waste products in water using fluorescence emission cavity-enhanced spectroscopy.
[So] Source:Proc Natl Acad Sci U S A;111(20):7208-11, 2014 May 20.
[Is] ISSN:1091-6490
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Clean water is paramount to human health. In this article, we present a technique for detection of trace amounts of human or animal waste products in water using fluorescence emission cavity-enhanced spectroscopy. The detection of femtomolar concentrations of urobilin, a metabolic byproduct of heme metabolism that is excreted in both human and animal waste in water, was achieved through the use of an integrating cavity. This technique could allow for real-time assessment of water quality without the need for expensive laboratory equipment.
[Mh] Termos MeSH primário: Espectrometria de Fluorescência/métodos
Poluentes Químicos da Água/análise
Purificação da Água/métodos
[Mh] Termos MeSH secundário: Animais
Pigmentos Biliares/química
Bilirrubina/química
Monitoramento Ambiental/instrumentação
Monitoramento Ambiental/métodos
Desenho de Equipamento
Fezes/química
Heme/química
Seres Humanos
Óptica e Fotônica
Espectrometria de Fluorescência/instrumentação
Urina/química
Urobilina/química
Poluição da Água
Qualidade da Água
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Bile Pigments); 0 (Water Pollutants, Chemical); 17G380DO11 (stercobilin); 1856-98-0 (Urobilin); 42VZT0U6YR (Heme); RFM9X3LJ49 (Bilirubin)
[Em] Mês de entrada:1407
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140507
[St] Status:MEDLINE
[do] DOI:10.1073/pnas.1403175111


  5 / 143 MEDLINE  
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[PMID]:24604419
[Au] Autor:Sun YF; Xu JG; Tang K; Miao D; Gärtner W; Scheer H; Zhao KH; Zhou M
[Ad] Endereço:State Key Laboratory of Agricultural Microbiology, Huazhong Agricultural University, Wuhan 430070, P.R. China. zhouming321@126.com.
[Ti] Título:Orange fluorescent proteins constructed from cyanobacteriochromes chromophorylated with phycoerythrobilin.
[So] Source:Photochem Photobiol Sci;13(5):757-63, 2014 May.
[Is] ISSN:1474-9092
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo: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.
[Mh] Termos MeSH primário: Cianobactérias/metabolismo
Proteínas Luminescentes/metabolismo
Ficobilinas/metabolismo
Ficoeritrina/metabolismo
Urobilina/análogos & derivados
[Mh] Termos MeSH secundário: Cianobactérias/química
Proteínas Luminescentes/química
Processos Fotoquímicos
Ficobilinas/química
Ficoeritrina/química
Temperatura Ambiente
Urobilina/química
Urobilina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Luminescent Proteins); 0 (Phycobilins); 11016-17-4 (Phycoerythrin); 18097-67-1 (phycoerythrobilin); 1856-98-0 (Urobilin); 61932-71-6 (phycourobilin)
[Em] Mês de entrada:1504
[Cu] Atualização por classe:140416
[Lr] Data última revisão:
140416
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140308
[St] Status:MEDLINE
[do] DOI:10.1039/c3pp50411e


  6 / 143 MEDLINE  
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[PMID]:23911526
[Au] Autor:Sampson DL; Chng YL; Upton Z; Hurst CP; Parker AW; Parker TJ
[Ad] Endereço:Tissue Repair and Regeneration Program, Brisbane, QLD 4059, Australia. Electronic address: dayle.sampson@qut.edu.au.
[Ti] Título:The highly abundant urinary metabolite urobilin interferes with the bicinchoninic acid assay.
[So] Source:Anal Biochem;442(1):110-7, 2013 Nov 01.
[Is] ISSN:1096-0309
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Estimation of total protein concentration is an essential step in any protein- or peptide-centric analysis pipeline. This study demonstrates that urobilin, a breakdown product of heme and a major constituent of urine, interferes considerably with the bicinchoninic acid (BCA) assay. This interference is probably due to the propensity of urobilin to reduce cupric ions (Cu(2+)) to cuprous ions (Cu(1+)), thus mimicking the reduction of copper by proteins, which the assay was designed to do. In addition, it is demonstrated that the Bradford assay is more resistant to the influence of urobilin and other small molecules. As such, urobilin has a strong confounding effect on the estimate of total protein concentrations obtained by BCA assay and thus this assay should not be used for urinary protein quantification. It is recommended that the Bradford assay be used instead.
[Mh] Termos MeSH primário: Proteínas/análise
Quinolinas/química
Urobilina/metabolismo
Urobilina/urina
[Mh] Termos MeSH secundário: Cobre/química
Cobre/metabolismo
Seres Humanos
Proteínas/química
Quinolinas/metabolismo
Valores de Referência
Sensibilidade e Especificidade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Proteins); 0 (Quinolines); 1856-98-0 (Urobilin); 789U1901C5 (Copper); CX56TX9Y1I (bicinchoninic acid)
[Em] Mês de entrada:1411
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130806
[St] Status:MEDLINE


  7 / 143 MEDLINE  
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[PMID]:23246570
[Au] Autor:Mölzer C; Pfleger B; Putz E; Roßmann A; Schwarz U; Wallner M; Bulmer AC; Wagner KH
[Ad] Endereço:Department of Nutritional Sciences, Emerging Field Oxidative Stress and DNA Stability, Faculty of Life Sciences, University of Vienna, Althanstraße 14, 1090 Vienna, Austria. christine.moelzer@univie.ac.at
[Ti] Título:In vitro DNA-damaging effects of intestinal and related tetrapyrroles in human cancer cells.
[So] Source:Exp Cell Res;319(4):536-45, 2013 Feb 15.
[Is] ISSN:1090-2422
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Epidemiological studies report a negative association between circulating bilirubin concentrations and the risk for cancer and cardiovascular disease. Structurally related tetrapyrroles also possess in vitro anti-genotoxic activity and may prevent mutation prior to malignancy. Furthermore, few data suggest that tetrapyrroles exert anti-carcinogenic effects via induction of cell cycle arrest and apoptosis. To further investigate whether tetrapyrroles provoke DNA-damage in human cancer cells, they were tested in the single cell gel electrophoresis assay (SCGE). Eight tetrapyrroles (unconjugated bilirubin, bilirubin ditaurate, biliverdin, biliverdin-/bilirubin dimethyl ester, urobilin, stercobilin and protoporphyrin) were added to cultured Caco2 and HepG2 cells and their effects on comet formation (% tail DNA) were assessed. Flow cytometric assessment (apoptosis/necrosis, cell cycle, intracellular radical species generation) assisted in revealing underlying mechanisms of intracellular action. Cells were incubated with tetrapyrroles at concentrations of 0.5, 5 and 17µM for 24h. Addition of 300µM tertiary-butyl hydroperoxide to cells served as a positive control. Tetrapyrrole incubation mostly resulted in increased DNA-damage (comet formation) in Caco2 and HepG2 cells. Tetrapyrroles that are concentrated within the intestine, including protoporphyrin, urobilin and stercobilin, led to significant comet formation in both cell lines, implicating the compounds in inducing DNA-damage and apoptosis in cancer cells found within organs of the digestive system.
[Mh] Termos MeSH primário: Dano ao DNA/efeitos dos fármacos
Intestinos/metabolismo
Neoplasias/patologia
Tetrapirróis/metabolismo
Tetrapirróis/farmacologia
[Mh] Termos MeSH secundário: Antioxidantes/farmacologia
Pigmentos Biliares/farmacologia
Bilirrubina/análogos & derivados
Bilirrubina/farmacologia
Células CACO-2
Ensaio Cometa
Relação Dose-Resposta a Droga
Avaliação Pré-Clínica de Medicamentos
Citometria de Fluxo
Células Hep G2
Seres Humanos
Neoplasias/genética
Concentração Osmolar
Protoporfirinas/farmacologia
Urobilina/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antioxidants); 0 (Bile Pigments); 0 (Protoporphyrins); 0 (Tetrapyrroles); 17G380DO11 (stercobilin); 1856-98-0 (Urobilin); RFM9X3LJ49 (Bilirubin)
[Em] Mês de entrada:1303
[Cu] Atualização por classe:151119
[Lr] Data última revisão:
151119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:121219
[St] Status:MEDLINE


  8 / 143 MEDLINE  
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[PMID]:22588203
[Au] Autor:Everroad RC; Wood AM
[Ad] Endereço:Institute for Ecology and Evolutionary Biology, formerly Center for Ecology and Evolutionary Biology, 5289 University of Oregon, Eugene, OR 97403, USA. rcraig@riken.jp
[Ti] Título:Phycoerythrin evolution and diversification of spectral phenotype in marine Synechococcus and related picocyanobacteria.
[So] Source:Mol Phylogenet Evol;64(3):381-92, 2012 Sep.
[Is] ISSN:1095-9513
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In marine Synechococcus there is evidence for the adaptive evolution of spectrally distinct forms of the major light harvesting pigment phycoerythrin (PE). Recent research has suggested that these spectral forms of PE have a different evolutionary history than the core genome. However, a lack of explicit statistical testing of alternative hypotheses or for selection on these genes has made it difficult to evaluate the evolutionary relationships between spectral forms of PE or the role horizontal gene transfer (HGT) may have had in the adaptive phenotypic evolution of the pigment system in marine Synechococcus. In this work, PE phylogenies of picocyanobacteria with known spectral phenotypes, including newly co-isolated strains of marine Synechococcus from the Gulf of Mexico, were constructed to explore the diversification of spectral phenotype and PE evolution in this group more completely. For the first time, statistical evaluation of competing evolutionary hypotheses and tests for positive selection on the PE locus in picocyanobacteria were performed. Genes for PEs associated with specific PE spectral phenotypes formed strongly supported monophyletic clades within the PE tree with positive directional selection driving evolution towards higher phycourobilin (PUB) content. The presence of the PUB-lacking phenotype in PE-containing marine picocyanobacteria from cyanobacterial lineages identified as Cyanobium is best explained by HGT into this group from marine Synechococcus. Taken together, these data provide strong examples of adaptive evolution of a single phenotypic trait in bacteria via mutation, positive directional selection and horizontal gene transfer.
[Mh] Termos MeSH primário: Evolução Biológica
Transferência Genética Horizontal
Ficoeritrina/genética
Synechococcus/genética
[Mh] Termos MeSH secundário: DNA Bacteriano/genética
Golfo do México
Fenótipo
Ficobilinas/análise
Ficoeritrina/análise
Filogenia
RNA Ribossômico 16S/genética
Seleção Genética
Análise de Sequência de DNA
Synechococcus/classificação
Urobilina/análogos & derivados
Urobilina/análise
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (DNA, Bacterial); 0 (Phycobilins); 0 (RNA, Ribosomal, 16S); 11016-17-4 (Phycoerythrin); 1856-98-0 (Urobilin); 61932-71-6 (phycourobilin)
[Em] Mês de entrada:1210
[Cu] Atualização por classe:120703
[Lr] Data última revisão:
120703
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120517
[St] Status:MEDLINE
[do] DOI:10.1016/j.ympev.2012.04.013


  9 / 143 MEDLINE  
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[PMID]:22566621
[Au] Autor:Chen YR; Su YS; Tu SL
[Ad] Endereço:Institute of Plant and Microbial Biology, Academia Sinica, Taipei 11529, Taiwan.
[Ti] Título:Distinct phytochrome actions in nonvascular plants revealed by targeted inactivation of phytobilin biosynthesis.
[So] Source:Proc Natl Acad Sci U S A;109(21):8310-5, 2012 May 22.
[Is] ISSN:1091-6490
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo: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.
[Mh] Termos MeSH primário: Bryopsida/enzimologia
Oxirredutases/metabolismo
Ficobilinas/biossíntese
Ficoeritrina/biossíntese
Proteínas de Plantas/metabolismo
Plastídeos/fisiologia
Urobilina/análogos & derivados
[Mh] Termos MeSH secundário: Bryopsida/genética
Bryopsida/crescimento & desenvolvimento
Regulação Enzimológica da Expressão Gênica/efeitos da radiação
Regulação da Expressão Gênica de Plantas/efeitos da radiação
Técnicas de Inativação de Genes
Luz
Dados de Sequência Molecular
Oxirredutases/genética
Fotoperíodo
Fitocromo/genética
Fitocromo/metabolismo
Proteínas de Plantas/genética
Tetrapirróis/biossíntese
Transcriptoma/fisiologia
Urobilina/biossíntese
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Phycobilins); 0 (Plant Proteins); 0 (Tetrapyrroles); 11016-17-4 (Phycoerythrin); 11121-56-5 (Phytochrome); 1856-98-0 (Urobilin); 61932-71-6 (phycourobilin); EC 1.- (Oxidoreductases)
[Em] Mês de entrada:1208
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120509
[St] Status:MEDLINE
[do] DOI:10.1073/pnas.1201744109


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[PMID]:22465853
[Au] Autor:Tang K; Zeng XL; Yang Y; Wang ZB; Wu XJ; Zhou M; Noy D; Scheer H; Zhao KH
[Ad] Endereço:State Key Laboratory of Agricultural Microbiology, Huazhong Agricultural University, Wuhan, PR China.
[Ti] Título:A minimal phycobilisome: fusion and chromophorylation of the truncated core-membrane linker and phycocyanin.
[So] Source:Biochim Biophys Acta;1817(7):1030-6, 2012 Jul.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Phycobilisomes, the light-harvesting antennas in cyanobacteria and red algae, consist of an allophycocyanin core that is attached to the membrane via a core-membrane linker, and rods comprised of phycocyanin and often also phycoerythrin or phycoerythrocyanin. Phycobiliproteins show excellent energy transfer among the chromophores that renders them biomarkers with large Stokes-shifts absorbing over most of the visible spectrum and into the near infrared. Their application is limited, however, due to covalent binding of the chromophores and by solubility problems. We report construction of a water-soluble minimal chromophore-binding unit of the red-absorbing and fluorescing core-membrane linker. This was fused to minimal chromophore-binding units of phycocyanin. After double chromophorylation with phycocyanobilin, in E. coli, the fused phycobiliproteins absorbed light in the range of 610-660nm, and fluoresced at ~670nm, similar to phycobilisomes devoid of phycoerythr(ocyan)in. The fused phycobiliprotein could also be doubly chromophorylated with phycoerythrobilin, resulting in a chromoprotein absorbing around 540-575nm, and fluorescing at ~585nm. The broad absorptions and the large Stokes shifts render these chromoproteins candidates for imaging; they may also be helpful in studying phycobilisome assembly.
[Mh] Termos MeSH primário: Membrana Celular/metabolismo
Ficobilissomas/metabolismo
Ficocianina/metabolismo
Proteínas Recombinantes de Fusão/metabolismo
[Mh] Termos MeSH secundário: Absorção
Apoproteínas/metabolismo
Escherichia coli/metabolismo
Liases/metabolismo
Ficobilinas/metabolismo
Ficoeritrina/metabolismo
Solubilidade
Espectrometria de Fluorescência
Urobilina/análogos & derivados
Urobilina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Apoproteins); 0 (Phycobilins); 0 (Phycobilisomes); 0 (Recombinant Fusion Proteins); 0 (phycoviolobilin); 11016-15-2 (Phycocyanin); 11016-17-4 (Phycoerythrin); 18097-67-1 (phycoerythrobilin); 1856-98-0 (Urobilin); 61932-71-6 (phycourobilin); EC 4.- (Lyases)
[Em] Mês de entrada:1304
[Cu] Atualização por classe:161126
[Lr] Data última revisão:
161126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120403
[St] Status:MEDLINE
[do] DOI:10.1016/j.bbabio.2012.03.018



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