Base de dados : MEDLINE
Pesquisa : B01.050.150.200.199.500 [Categoria DeCS]
Referências encontradas : 107 [refinar]
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  1 / 107 MEDLINE  
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[PMID]:28511668
[Au] Autor:Muruganandam G; Raasakka A; Myllykoski M; Kursula I; Kursula P
[Ad] Endereço:Centre for Structural Systems Biology - Helmholtz Centre for Infection Research, German Electron Synchrotron (DESY), Hamburg, Germany.
[Ti] Título:Structural similarities and functional differences clarify evolutionary relationships between tRNA healing enzymes and the myelin enzyme CNPase.
[So] Source:BMC Biochem;18(1):7, 2017 May 16.
[Is] ISSN:1471-2091
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Eukaryotic tRNA splicing is an essential process in the transformation of a primary tRNA transcript into a mature functional tRNA molecule. 5'-phosphate ligation involves two steps: a healing reaction catalyzed by polynucleotide kinase (PNK) in association with cyclic phosphodiesterase (CPDase), and a sealing reaction catalyzed by an RNA ligase. The enzymes that catalyze tRNA healing in yeast and higher eukaryotes are homologous to the members of the 2H phosphoesterase superfamily, in particular to the vertebrate myelin enzyme 2',3'-cyclic nucleotide 3'-phosphodiesterase (CNPase). RESULTS: We employed different biophysical and biochemical methods to elucidate the overall structural and functional features of the tRNA healing enzymes yeast Trl1 PNK/CPDase and lancelet PNK/CPDase and compared them with vertebrate CNPase. The yeast and the lancelet enzymes have cyclic phosphodiesterase and polynucleotide kinase activity, while vertebrate CNPase lacks PNK activity. In addition, we also show that the healing enzymes are structurally similar to the vertebrate CNPase by applying synchrotron radiation circular dichroism spectroscopy and small-angle X-ray scattering. CONCLUSIONS: We provide a structural analysis of the tRNA healing enzyme PNK and CPDase domains together. Our results support evolution of vertebrate CNPase from tRNA healing enzymes with a loss of function at its N-terminal PNK-like domain.
[Mh] Termos MeSH primário: 2´,3´-Nucleotídeo Cíclico Fosfodiesterases/química
Evolução Molecular
[Mh] Termos MeSH secundário: 2',3'-Nucleotídeo Cíclico Fosfodiesterases/metabolismo
2',3'-Nucleotídeo Cíclico Fosfodiesterases/fisiologia
Animais
Dicroísmo Circular
Células Eucarióticas/enzimologia
Anfioxos
Camundongos
Bainha de Mielina/enzimologia
Polinucleotídeo 5'-Hidroxiquinase/química
Polinucleotídeo 5'-Hidroxiquinase/metabolismo
Processamento de RNA
RNA de Transferência/genética
Saccharomyces cerevisiae
Espalhamento a Baixo Ângulo
Difração de Raios X
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
9014-25-9 (RNA, Transfer); EC 2.7.1.78 (Polynucleotide 5'-Hydroxyl-Kinase); EC 3.1.4.- (2',3'-Cyclic-Nucleotide Phosphodiesterases)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170728
[Lr] Data última revisão:
170728
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170518
[St] Status:MEDLINE
[do] DOI:10.1186/s12858-017-0084-2


  2 / 107 MEDLINE  
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[PMID]:28474175
[Au] Autor:Bozzo M; Macrì S; Calzia D; Sgarra R; Manfioletti G; Ramoino P; Lacalli T; Vignali R; Pestarino M; Candiani S
[Ad] Endereço:Dipartimento di Scienze della Terra, dell'Ambiente e della Vita (DISTAV), Università di Genova, viale Benedetto XV 5, 16132, Genoa, Italy.
[Ti] Título:The HMGA gene family in chordates: evolutionary perspectives from amphioxus.
[So] Source:Dev Genes Evol;227(3):201-211, 2017 Jun.
[Is] ISSN:1432-041X
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:High mobility group A proteins of vertebrates, HMGA1 and 2, are chromatin architectural factors involved in development, cell differentiation, and neoplastic transformation. Here, we characterize an amphioxus HMGA gene ortholog and analyze its expression. As a basal chordate, amphioxus is well placed to provide insights into the evolution of the HMGA gene family, particularly in the transition from invertebrates to vertebrates. Our phylogenetic analysis supports the basal position of amphioxus, echinoderm, and hemichordate HMGA sequences to those of vertebrate HMGA1 and HMGA2. Consistent with this, the genomic landscape around amphioxus HMGA shares features with both. Whole mount in situ hybridization shows that amphioxus HMGA mRNA is detectable from neurula stage onwards in both nervous and non-nervous tissues. This correlates with protein expression monitored immunocytochemically using antibodies against human HMGA2 protein, revealing especially high levels of expression in cells of the lamellar body, the amphioxus homolog of the pineal, suggesting that the gene may have, among its many functions, an evolutionarily conserved role in photoreceptor differentiation.
[Mh] Termos MeSH primário: Proteínas HMGA/genética
Anfioxos/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Clonagem Molecular
Evolução Molecular
Microscopia Eletrônica de Transmissão
Filogenia
Alinhamento de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (HMGA Proteins)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171006
[Lr] Data última revisão:
171006
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170506
[St] Status:MEDLINE
[do] DOI:10.1007/s00427-017-0581-8


  3 / 107 MEDLINE  
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[PMID]:28422959
[Au] Autor:Albuixech-Crespo B; López-Blanch L; Burguera D; Maeso I; Sánchez-Arrones L; Moreno-Bravo JA; Somorjai I; Pascual-Anaya J; Puelles E; Bovolenta P; Garcia-Fernàndez J; Puelles L; Irimia M; Ferran JL
[Ad] Endereço:Department of Genetics, School of Biology, and Institut de Biomedicina (IBUB), University of Barcelona, Barcelona, Spain.
[Ti] Título:Molecular regionalization of the developing amphioxus neural tube challenges major partitions of the vertebrate brain.
[So] Source:PLoS Biol;15(4):e2001573, 2017 Apr.
[Is] ISSN:1545-7885
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:All vertebrate brains develop following a common Bauplan defined by anteroposterior (AP) and dorsoventral (DV) subdivisions, characterized by largely conserved differential expression of gene markers. However, it is still unclear how this Bauplan originated during evolution. We studied the relative expression of 48 genes with key roles in vertebrate neural patterning in a representative amphioxus embryonic stage. Unlike nonchordates, amphioxus develops its central nervous system (CNS) from a neural plate that is homologous to that of vertebrates, allowing direct topological comparisons. The resulting genoarchitectonic model revealed that the amphioxus incipient neural tube is unexpectedly complex, consisting of several AP and DV molecular partitions. Strikingly, comparison with vertebrates indicates that the vertebrate thalamus, pretectum, and midbrain domains jointly correspond to a single amphioxus region, which we termed Di-Mesencephalic primordium (DiMes). This suggests that these domains have a common developmental and evolutionary origin, as supported by functional experiments manipulating secondary organizers in zebrafish and mice.
[Mh] Termos MeSH primário: Encéfalo/embriologia
Embrião não Mamífero/embriologia
Anfioxos/embriologia
Tubo Neural/embriologia
Vertebrados/embriologia
[Mh] Termos MeSH secundário: Animais
Evolução Biológica
Padronização Corporal/genética
Encéfalo/metabolismo
Embrião de Galinha
Embrião não Mamífero/metabolismo
Regulação da Expressão Gênica no Desenvolvimento
Hibridização in Situ Fluorescente
Anfioxos/metabolismo
Masculino
Camundongos Knockout
Modelos Biológicos
Modelos Genéticos
Tubo Neural/metabolismo
Vertebrados/metabolismo
Peixe-Zebra
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170522
[Lr] Data última revisão:
170522
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170420
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pbio.2001573


  4 / 107 MEDLINE  
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[PMID]:28400271
[Au] Autor:Gao Z; Qu B; Ma Z; Jiao D; Ji G; Zhang S
[Ad] Endereço:Laboratory for Evolution & Development, Institute of Evolution & Marine Biodiversity, Ocean University of China, Qingdao 266003, China; Department of Marine Biology, Ocean University of China, Qingdao 266003, China.
[Ti] Título:Identification and functional characterization of a novel member of low-density lipoprotein receptor-related protein (LRP)-like family in amphioxus.
[So] Source:Gene;618:42-48, 2017 Jun 30.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Low-density lipoprotein receptor-related protein (LRP) is a group of important endocytic receptors contributing to binding ligands and maintaining internal environment. In this study, we identified a soluble LRP-like molecule in the amphioxus B. japonicum, BjLRP, with an uncharacterized domain structure combination of LY-EGF-CRD-EGF-CRD. It was mainly expressed in the gill, muscle, notochord and testis, and was significantly up-regulated following the challenge with bacteria. Recombinant BjLRP was capable of interacting with both Gram-negative and positive bacteria as well as PAMPs including lipopolysaccharide (LPS), lipoteichoic acid (LTA) and peptidoglycan (PGN). Interestingly, recombinant LY peptide was also able to bind to the Gram-negative and positive bacteria as well as the PAMPs LPS, LTA and PGN. By contrast, none of recombinant EGF1, EGF2, CRD1 and CRD2 had affinity to the bacteria and the PAMPs. In addition, BjLRPΔLY had no affinity to the PAMPs, although BjLRPΔLY showed slight affinity to the bacteria. These suggest that the interaction of BjLRP with the bacteria and PAMPs was primarily attributable to the LY domain. It is clear that BjLRP is a novel pattern recognition protein capable of identifying and interacting with invading bacteria in amphioxus.
[Mh] Termos MeSH primário: Proteínas Relacionadas a Receptor de LDL/genética
Anfioxos/genética
[Mh] Termos MeSH secundário: Animais
Proteínas Relacionadas a Receptor de LDL/metabolismo
Anfioxos/metabolismo
Anfioxos/microbiologia
Lipopolissacarídeos/metabolismo
Ligação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (LDL-Receptor Related Proteins); 0 (Lipopolysaccharides)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170608
[Lr] Data última revisão:
170608
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170413
[St] Status:MEDLINE


  5 / 107 MEDLINE  
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[PMID]:28384204
[Au] Autor:Liao J; Wang K; Yao W; Yi X; Yan H; Chen M; Lan X
[Ad] Endereço:Institute for Laboratory Medicine, Fuzhou General Hospital of Nanjing Command, Fuzhou, Fujian Province, China.
[Ti] Título:Cloning, expression and antioxidant activity of a thioredoxin peroxidase from Branchiostoma belcheri tsingtaunese.
[So] Source:PLoS One;12(4):e0175162, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Peroxiredoxins (Prxs) are ubiquitous antioxidant enzymes that catalyze the thioredoxin- dependent reduction of hydroperoxides. In this study, a novel thioredoxin peroxidase (Bbt-TPx1), a member of the peroxiredoxin superfamily, was found by EST sequence analysis of a cDNA library of Branchiostoma belcheri tsingtaunese ovary. The sequence of a full-length cDNA clone contained an open reading frame encoding a polypeptide of 198 amino acid residues, with a calculated molecular weight of 22,150 Da. The expression patterns of the protein at different developmental stages and adult amphioxus tissues indicate that this enzyme may play important roles in anti-oxidation and innate immunity. The recombinant Bbt-TPx1 protein was expressed with a polyhistidine-tag in Escherichia coli and purified using Ni chromatography followed by SP cation exchange chromatography. The rBbt-TPx1 protein existed as a dimer under non-reducing conditions, and was dissociated into monomers by dithiothreitol (DTT); it might predominantly exist in oligomeric form. The rBbt-TPx1 protein showed a significant thiol-dependent peroxidase activity, removing hydrogen peroxide in the presence of dithiothreitol (DTT), but not glutathione (GSH). Protection of plasmid DNA and the thiol-protein from damage by metal-catalyzed oxidation (MCO) in vitro was also revealed.
[Mh] Termos MeSH primário: Antioxidantes/farmacologia
Anfioxos/enzimologia
Peroxirredoxinas/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Sequência de Bases
Cromatografia em Gel
Clonagem Molecular
Eletroforese em Gel de Poliacrilamida
Anfioxos/classificação
Fases de Leitura Aberta
Filogenia
Reação em Cadeia da Polimerase em Tempo Real
Homologia de Sequência de Aminoácidos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); EC 1.11.1.15 (Peroxiredoxins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170907
[Lr] Data última revisão:
170907
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170407
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0175162


  6 / 107 MEDLINE  
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[PMID]:28324048
[Au] Autor:Wang P; Wang M; Ji G; Yang S; Zhang S; Liu Z
[Ad] Endereço:Laboratory for Evolution & Development, Institute of Evolution & Marine Biodiversity, Ocean University of China, Qingdao 266003, China.
[Ti] Título:Demonstration of a Functional Kisspeptin/Kisspeptin Receptor System in Amphioxus With Implications for Origin of Neuroendocrine Regulation.
[So] Source:Endocrinology;158(5):1461-1473, 2017 May 01.
[Is] ISSN:1945-7170
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Amphioxus belongs to the Cephalochordata, which is the most basal subphylum of the chordates. Despite many studies on the endocrine system of amphioxus, key information about its regulation remains ambiguous. Here we clearly demonstrate the presence of a functional kisspeptin/kisspeptin receptor (Kiss-Kissr) system, which is involved in the regulation of reproduction in amphioxus. Evolutionary analyses revealed large expansion of Kiss and Kissr (gpr54) genes in amphioxus, and they might represent the ancestral type of the Kiss/gpr54 genes in chordates. Amphioxus Kiss was obviously expression at the cerebral vesicle and the Hatschek pit, whereas amphioxus gpr54 messenger RNA (mRNA) was abundantly present in nerve cord, ovary, and testes. Amphioxus GPR54-Like1 (GPR54L-1) was shown to be located on the cell membrane. The synthetic amphioxus Kiss-like (KissL) peptides were capable of activating the amphioxus GPR54L-1 with different potencies, hinting the interaction between Kiss and GPR54. Moreover, the expression of amphioxus gpr54 mRNA was significantly decreased during low or high temperature extremes. Importantly, the injection of amphioxus KissL could cause an elevation of zebrafish blood luteinizing hormone level and induce the expression of amphioxus gpb5, a gene encoding the ancestral type of vertebrate pituitary glycoprotein hormones. Also, the expression levels of BjkissL-2 or Bjgpr54L-1 were downregulated after spermiation or spawning. Collectively, the amphioxus Kiss-Kissr system has a correlation with the regulation of reproduction. Our studies provide insights into the functional roles and evolutionary history of the Kiss-Kissr system, as well as the origin of the vertebrate neuroendocrine axis for controlling reproduction.
[Mh] Termos MeSH primário: Evolução Biológica
Kisspeptinas/genética
Anfioxos/genética
Sistemas Neurossecretores/fisiologia
Receptores Acoplados a Proteínas-G/genética
[Mh] Termos MeSH secundário: Animais
Clonagem Molecular
Regulação da Expressão Gênica
Células HEK293
Seres Humanos
Kisspeptinas/isolamento & purificação
Kisspeptinas/fisiologia
Anfioxos/metabolismo
Receptores Acoplados a Proteínas-G/isolamento & purificação
Receptores Acoplados a Proteínas-G/fisiologia
Receptores de Kisspeptina-1
Transfecção
Peixe-Zebra
Proteínas de Peixe-Zebra/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (KISS1R protein, zebrafish); 0 (Kisspeptins); 0 (Receptors, G-Protein-Coupled); 0 (Receptors, Kisspeptin-1); 0 (Zebrafish Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170322
[St] Status:MEDLINE
[do] DOI:10.1210/en.2016-1848


  7 / 107 MEDLINE  
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[PMID]:28103795
[Au] Autor:Carvalho JE; Theodosiou M; Chen J; Chevret P; Alvarez S; De Lera AR; Laudet V; Croce JC; Schubert M
[Ad] Endereço:Sorbonne Universités, UPMC Université Paris 06, CNRS, Laboratoire de Biologie du Développement de Villefranche-sur-Mer, Observatoire Océanologique de Villefranche-sur-Mer, 181 Chemin du Lazaret, 06230, Villefranche-sur-Mer, France.
[Ti] Título:Lineage-specific duplication of amphioxus retinoic acid degrading enzymes (CYP26) resulted in sub-functionalization of patterning and homeostatic roles.
[So] Source:BMC Evol Biol;17(1):24, 2017 Jan 19.
[Is] ISSN:1471-2148
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: During embryogenesis, tight regulation of retinoic acid (RA) availability is fundamental for normal development. In parallel to RA synthesis, a negative feedback loop controlled by RA catabolizing enzymes of the cytochrome P450 subfamily 26 (CYP26) is crucial. In vertebrates, the functions of the three CYP26 enzymes (CYP26A1, CYP26B1, and CYP26C1) have been well characterized. By contrast, outside vertebrates, little is known about CYP26 complements and their biological roles. In an effort to characterize the evolutionary diversification of RA catabolism, we studied the CYP26 genes of the cephalochordate amphioxus (Branchiostoma lanceolatum), a basal chordate with a vertebrate-like genome that has not undergone the massive, large-scale duplications of vertebrates. RESULTS: In the present study, we found that amphioxus also possess three CYP26 genes (CYP26-1, CYP26-2, and CYP26-3) that are clustered in the genome and originated by lineage-specific duplication. The amphioxus CYP26 cluster thus represents a useful model to assess adaptive evolutionary changes of the RA signaling system following gene duplication. The characterization of amphioxus CYP26 expression, function, and regulation by RA signaling demonstrated that, despite the independent origins of CYP26 duplicates in amphioxus and vertebrates, they convergently assume two main roles during development: RA-dependent patterning and protection against fluctuations of RA levels. Our analysis suggested that in amphioxus RA-dependent patterning is sustained by CYP26-2, while RA homeostasis is mediated by CYP26-1 and CYP26-3. Furthermore, comparisons of the regulatory regions of CYP26 genes of different bilaterian animals indicated that a CYP26-driven negative feedback system was present in the last common ancestor of deuterostomes, but not in that of bilaterians. CONCLUSIONS: Altogether, this work reveals the evolutionary origins of the RA-dependent regulation of CYP26 genes and highlights convergent functions for CYP26 enzymes that originated by independent duplication events, hence establishing a novel selective mechanism for the genomic retention of gene duplicates.
[Mh] Termos MeSH primário: Família 26 do Citocromo P450/metabolismo
Anfioxos/genética
Tretinoína/metabolismo
[Mh] Termos MeSH secundário: Animais
Família 26 do Citocromo P450/genética
Desenvolvimento Embrionário
Evolução Molecular
Duplicação Gênica
Genoma
Anfioxos/enzimologia
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
5688UTC01R (Tretinoin); EC 1.14.14.1 (Cytochrome P450 Family 26)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170808
[Lr] Data última revisão:
170808
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170121
[St] Status:MEDLINE
[do] DOI:10.1186/s12862-016-0863-1


  8 / 107 MEDLINE  
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[PMID]:27973733
[Au] Autor:Carmona LM; Schatz DG
[Ad] Endereço:Department of Immunobiology, Yale University School of Medicine, New Haven, CT, USA.
[Ti] Título:New insights into the evolutionary origins of the recombination-activating gene proteins and V(D)J recombination.
[So] Source:FEBS J;284(11):1590-1605, 2017 Jun.
[Is] ISSN:1742-4658
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The adaptive immune system of jawed vertebrates relies on V(D)J recombination as one of the main processes to generate the diverse array of receptors necessary for the recognition of a wide range of pathogens. The DNA cleavage reaction necessary for the assembly of the antigen receptor genes from an array of potential gene segments is mediated by the recombination-activating gene proteins RAG1 and RAG2. The RAG proteins have been proposed to originate from a transposable element (TE) as they share mechanistic and structural similarities with several families of transposases and are themselves capable of mediating transposition. A number of RAG-like proteins and TEs with sequence similarity to RAG1 and RAG2 have been identified, but only recently has their function begun to be characterized, revealing mechanistic links to the vertebrate RAGs. Of particular significance is the discovery of ProtoRAG, a transposon superfamily found in the genome of the basal chordate amphioxus. ProtoRAG has many of the sequence and mechanistic features predicted for the ancestral RAG transposon and is likely to be an evolutionary relative of RAG1 and RAG2. In addition, early observations suggesting that RAG1 is able to mediate V(D)J recombination in the absence of RAG2 have been confirmed, implying independent evolutionary origins for the two RAG genes. Here, recent progress in identifying and characterizing RAG-like proteins and the TEs that encode them is summarized and a refined model for the evolution of V(D)J recombination and the RAG proteins is presented.
[Mh] Termos MeSH primário: Elementos de DNA Transponíveis/genética
Proteínas de Ligação a DNA/fisiologia
Evolução Molecular
Genes RAG-1
Proteínas de Homeodomínio/fisiologia
Recombinação V(D)J
Vertebrados/imunologia
[Mh] Termos MeSH secundário: Animais
Sequência Conservada
Reparo do DNA por Junção de Extremidades
Proteínas de Ligação a DNA/genética
Transferência Genética Horizontal
Seres Humanos
Anfioxos/genética
Anfioxos/imunologia
Modelos Genéticos
Filogenia
Ouriços-do-Mar/genética
Ouriços-do-Mar/imunologia
Estrelas-do-Mar/genética
Estrelas-do-Mar/imunologia
Transposases/genética
Transposases/fisiologia
VDJ Recombinases/genética
VDJ Recombinases/fisiologia
Vertebrados/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (DNA Transposable Elements); 0 (DNA-Binding Proteins); 0 (Homeodomain Proteins); 0 (V(D)J recombination activating protein 2); 128559-51-3 (RAG-1 protein); EC 2.7.7.- (Transposases); EC 2.7.7.- (VDJ Recombinases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161216
[St] Status:MEDLINE
[do] DOI:10.1111/febs.13990


  9 / 107 MEDLINE  
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[PMID]:27917830
[Au] Autor:Clavel D; Gotthard G; von Stetten D; De Sanctis D; Pasquier H; Lambert GG; Shaner NC; Royant A
[Ad] Endereço:Université Grenoble Alpes, Institut de Biologie Structurale (IBS), F-38044 Grenoble, France.
[Ti] Título:Structural analysis of the bright monomeric yellow-green fluorescent protein mNeonGreen obtained by directed evolution.
[So] Source:Acta Crystallogr D Struct Biol;72(Pt 12):1298-1307, 2016 12 01.
[Is] ISSN:2059-7983
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Until recently, genes coding for homologues of the autofluorescent protein GFP had only been identified in marine organisms from the phyla Cnidaria and Arthropoda. New fluorescent-protein genes have now been found in the phylum Chordata, coding for particularly bright oligomeric fluorescent proteins such as the tetrameric yellow fluorescent protein lanYFP from Branchiostoma lanceolatum. A successful monomerization attempt led to the development of the bright yellow-green fluorescent protein mNeonGreen. The structures of lanYFP and mNeonGreen have been determined and compared in order to rationalize the directed evolution process leading from a bright, tetrameric to a still bright, monomeric fluorescent protein. An unusual discolouration of crystals of mNeonGreen was observed after X-ray data collection, which was investigated using a combination of X-ray crystallography and UV-visible absorption and Raman spectroscopies, revealing the effects of specific radiation damage in the chromophore cavity. It is shown that X-rays rapidly lead to the protonation of the phenolate O atom of the chromophore and to the loss of its planarity at the methylene bridge.
[Mh] Termos MeSH primário: Anfioxos/química
Proteínas Luminescentes/química
[Mh] Termos MeSH secundário: Animais
Clonagem Molecular
Cristalografia por Raios X
Evolução Molecular Direcionada/métodos
Proteínas de Fluorescência Verde/química
Proteínas de Fluorescência Verde/genética
Anfioxos/genética
Proteínas Luminescentes/genética
Modelos Moleculares
Mutação
Conformação Proteica
Análise Espectral Raman
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Luminescent Proteins); 147336-22-9 (Green Fluorescent Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171117
[Lr] Data última revisão:
171117
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161206
[St] Status:MEDLINE


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[PMID]:27613144
[Au] Autor:Qu B; Yang S; Ma Z; Gao Z; Zhang S
[Ad] Endereço:Laboratory for Evolution & Development, Institute of Evolution & Marine Biodiversity, Qingdao 266003, China; Department of Marine Biology, Ocean University of China, Qingdao 266003, China.
[Ti] Título:A new LDLa domain-containing C-type lectin with bacterial agglutinating and binding activity in amphioxus.
[So] Source:Gene;594(2):220-228, 2016 Dec 15.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Over 1200 C-type lectin gene models have been identified in amphioxus, but only a few of them have been functionally characterized. In this study, we identified a C-type lectin, BjCTL, with domain structure of LDLa-CTLD-EGF_Lam, the first such data in chordates. It was expressed mainly in the notochord and ovary in a tissue-dependent fashion. Recombinant BjCTL was characterized as a typical Ca -dependent carbohydrate-binding protein capable of agglutinating and binding to both Gram-negative and positive bacteria we tested. In addition, it specifically bound to insoluble lipopolysaccharide, lipoteichoic acid and peptidoglycan, which can be inhibited by galactose. We also showed that the interaction of BjCTL with the bacteria is primarily attributable to CTLD domain. Thus, BjCTL is a novel pattern recognition protein involved in lectin-mediated innate immunity.
[Mh] Termos MeSH primário: Escherichia coli/química
Anfioxos/química
Lectinas Tipo C/química
Staphylococcus aureus/química
[Mh] Termos MeSH secundário: Aglutinação/imunologia
Animais
Bovinos
Escherichia coli/imunologia
Imunidade Inata
Anfioxos/genética
Anfioxos/imunologia
Lectinas Tipo C/genética
Lectinas Tipo C/imunologia
Lipopolissacarídeos/química
Lipopolissacarídeos/imunologia
Peptidoglicano/química
Peptidoglicano/imunologia
Ligação Proteica/imunologia
Domínios Proteicos
Staphylococcus aureus/imunologia
Ácidos Teicoicos/química
Ácidos Teicoicos/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Lectins, C-Type); 0 (Lipopolysaccharides); 0 (Peptidoglycan); 0 (Teichoic Acids); 56411-57-5 (lipoteichoic acid)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170125
[Lr] Data última revisão:
170125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160911
[St] Status:MEDLINE



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