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  1 / 177 MEDLINE  
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[PMID]:28431154
[Au] Autor:Laufer K; Niemeyer A; Nikeleit V; Halama M; Byrne JM; Kappler A
[Ad] Endereço:Geomicrobiology, Center for Applied Geosciences, University of Tuebingen, D-72076 Tuebingen, Germany.
[Ti] Título:Physiological characterization of a halotolerant anoxygenic phototrophic Fe(II)-oxidizing green-sulfur bacterium isolated from a marine sediment.
[So] Source:FEMS Microbiol Ecol;93(5), 2017 May 01.
[Is] ISSN:1574-6941
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Anoxygenic photoautotrophic bacteria which use light energy and electrons from Fe(II) for growth, so-called photoferrotrophs, are suggested to have been amongst the first phototrophic microorganisms on Earth and to have contributed to the deposition of sedimentary iron mineral deposits, i.e. banded iron formations. To date only two isolates of marine photoferrotrophic bacteria exist, both of which are closely related purple non-sulfur bacteria. Here we present a novel green-sulfur photoautotrophic Fe(II) oxidizer isolated from a marine coastal sediment, Chlorobium sp. strain N1, which is closely related to the freshwater green-sulfur bacterium Chlorobium luteolum DSM273 that is incapable of Fe(II) oxidation. Besides Fe(II), our isolated strain grew phototrophically with other inorganic and organic substrates such as sulfide, hydrogen, lactate or yeast extract. Highest Fe(II) oxidation rates were measured at pH 7.0-7.3, the temperature optimum was 25°C. Mössbauer spectroscopy identified ferrihydrite as the main Fe(III) mineral and fluorescence and helium-ion microscopy revealed cell-mineral aggregates without obvious cell encrustation. In summary, our study showed that the new isolate is physiologically adapted to the conditions of its natural habitat but also to conditions as proposed for early Earth and is thus a suitable model organism for further studies addressing phototrophic Fe(II) oxidation on early Earth.
[Mh] Termos MeSH primário: Chlorobium
Compostos Férricos/metabolismo
Sedimentos Geológicos/microbiologia
[Mh] Termos MeSH secundário: Chlorobium/classificação
Chlorobium/isolamento & purificação
Chlorobium/metabolismo
Compostos Ferrosos/metabolismo
Água Doce/microbiologia
Ferro/metabolismo
Luz
Oxirredução
Enxofre/metabolismo
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Ferric Compounds); 0 (Ferrous Compounds); 70FD1KFU70 (Sulfur); 87PZU03K0K (ferric oxyhydroxide); E1UOL152H7 (Iron)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170422
[St] Status:MEDLINE
[do] DOI:10.1093/femsec/fix054


  2 / 177 MEDLINE  
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[PMID]:28104786
[Au] Autor:Green DE; DeAngelis PL
[Ad] Endereço:Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, 940 Stanton L. Young Blvd., BMSB 853,Oklahoma City, OK73126-0901, USA.
[Ti] Título:Identification of a chondroitin synthase from an unexpected source, the green sulfur bacterium Chlorobium phaeobacteroides.
[So] Source:Glycobiology;27(5):469-476, 2017 May 01.
[Is] ISSN:1460-2423
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Glycosaminoglycans (GAGs) are known to be present in all animals as well as some pathogenic microbes. Chondroitin sulfate is the most abundant GAG in mammals where it has various structural and adhesion roles. The Gram-negative bacteria Pasteurella multocida Type F and Escherichia coli K4 produce extracellular capsules composed of unsulfated chondroitin or a fructosylated chondroitin, respectively. Such polysaccharides that are structurally related to host molecules do not generally provoke a strong antibody response thus are thought to be employed as molecular camouflage during infection. We observed a sequence from the photosynthetic green sulfur bacteria, Chlorobium phaeobacteroides DSM 266, which was very similar (~62% identical) to the open reading frames of the known bifunctional chondroitin synthases (PmCS and KfoC); some segments are strikingly conserved amongst the three proteins. Recombinant E. coli-derived Chlorobium enzyme preparations were found to possess bona fide chondroitin synthase activity in vitro. This new catalyst, CpCS, however, has a more promiscuous acceptor usage than the prototypical PmCS, which may be of utility in novel chimeric GAG syntheses. The finding of such a similar chondroitin synthase enzyme in C. phaeobacteroides is unexpected for several reasons including (a) a free-living nonpathogenic organism should not "need" an animal self molecule for protection, (b) the Proteobacteria and the green sulfur bacterial lineages diverged ~2.5-3 billion years ago and (c) the ecological niches of these bacteria are not thought to overlap substantially to facilitate horizontal gene transfer. CpCS provides insight into the structure/function relationship of this class of enzymes.
[Mh] Termos MeSH primário: Chlorobium/enzimologia
Glicosaminoglicanos/metabolismo
N-Acetilgalactosaminiltransferases/genética
N-Acetilgalactosaminiltransferases/isolamento & purificação
[Mh] Termos MeSH secundário: Sequência de Aminoácidos/genética
Sulfatos de Condroitina/química
Escherichia coli/genética
Glicosaminoglicanos/genética
N-Acetilgalactosaminiltransferases/metabolismo
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Glycosaminoglycans); 9007-28-7 (Chondroitin Sulfates); EC 2.4.1.- (N-Acetylgalactosaminyltransferases); EC 2.4.1.175 (chondroitin synthase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170731
[Lr] Data última revisão:
170731
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170121
[St] Status:MEDLINE
[do] DOI:10.1093/glycob/cwx008


  3 / 177 MEDLINE  
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[PMID]:27392085
[Au] Autor:Llorens-Marès T; Liu Z; Allen LZ; Rusch DB; Craig MT; Dupont CL; Bryant DA; Casamayor EO
[Ad] Endereço:Integrative Freshwater Ecology Group, Centro de Estudios Avanzados de Blanes, CEAB-CSIC. Accés Cala Sant Francesc, Girona, Spain.
[Ti] Título:Speciation and ecological success in dimly lit waters: horizontal gene transfer in a green sulfur bacteria bloom unveiled by metagenomic assembly.
[So] Source:ISME J;11(1):201-211, 2017 Jan.
[Is] ISSN:1751-7370
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A natural planktonic bloom of a brown-pigmented photosynthetic green sulfur bacteria (GSB) from the disphotic zone of karstic Lake Banyoles (NE Spain) was studied as a natural enrichment culture from which a nearly complete genome was obtained after metagenomic assembly. We showed in situ a case where horizontal gene transfer (HGT) explained the ecological success of a natural population unveiling ecosystem-specific adaptations. The uncultured brown-pigmented GSB was 99.7% identical in the 16S rRNA gene sequence to its green-pigmented cultured counterpart Chlorobium luteolum DSM 273 . Several differences were detected for ferrous iron acquisition potential, ATP synthesis and gas vesicle formation, although the most striking trait was related to pigment biosynthesis strategy. Chl. luteolum DSM 273 synthesizes bacteriochlorophyll (BChl) c, whereas Chl. luteolum CIII incorporated by HGT a 18-kbp cluster with the genes needed for BChl e and specific carotenoids biosynthesis that provided ecophysiological advantages to successfully colonize the dimly lit waters. We also genomically characterized what we believe to be the first described GSB phage, which based on the metagenomic coverage was likely in an active state of lytic infection. Overall, we observed spread HGT and we unveiled clear evidence for virus-mediated HGT in a natural population of photosynthetic GSB.
[Mh] Termos MeSH primário: Chlorobium/metabolismo
Transferência Genética Horizontal
Lagos/microbiologia
Enxofre/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/metabolismo
Bacterioclorofilas/metabolismo
Chlorobium/classificação
Chlorobium/genética
Chlorobium/isolamento & purificação
Ecossistema
Metagenômica
Fotossíntese
RNA Ribossômico 16S/genética
Espanha
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Bacteriochlorophylls); 0 (RNA, Ribosomal, 16S); 0 (bacteriochlorophyll e); 53986-51-9 (bacteriochlorophyll c); 70FD1KFU70 (Sulfur)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171113
[Lr] Data última revisão:
171113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160709
[St] Status:MEDLINE
[do] DOI:10.1038/ismej.2016.93


  4 / 177 MEDLINE  
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[PMID]:27505298
[Au] Autor:Moreno A; Froehlig JR; Bachas S; Gunio D; Alexander T; Vanya A; Wade H
[Ad] Endereço:Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine , 725 North Wolfe Street, Baltimore, Maryland 21205, United States.
[Ti] Título:Solution Binding and Structural Analyses Reveal Potential Multidrug Resistance Functions for SAV2435 and CTR107 and Other GyrI-like Proteins.
[So] Source:Biochemistry;55(34):4850-63, 2016 Aug 30.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Multidrug resistance (MDR) refers to the acquired ability of cells to tolerate a broad range of toxic compounds. One mechanism cells employ is to increase the level of expression of efflux pumps for the expulsion of xenobiotics. A key feature uniting efflux-related mechanisms is multidrug (MD) recognition, either by efflux pumps themselves or by their transcriptional regulators. However, models describing MD binding by MDR effectors are incomplete, underscoring the importance of studies focused on the recognition elements and key motifs that dictate polyspecific binding. One such motif is the GyrI-like domain, which is found in several MDR proteins and is postulated to have been adapted for small-molecule binding and signaling. Here we report the solution binding properties and crystal structures of two proteins containing GyrI-like domains, SAV2435 and CTR107, bound to various ligands. Furthermore, we provide a comparison with deposited crystal structures of GyrI-like proteins, revealing key features of GyrI-like domains that not only support polyspecific binding but also are conserved among GyrI-like domains. Together, our studies suggest that GyrI-like domains perform evolutionarily conserved functions connected to multidrug binding and highlight the utility of these types of studies for elucidating mechanisms of MDR.
[Mh] Termos MeSH primário: Subfamília B de Transportador de Cassetes de Ligação de ATP/química
Subfamília B de Transportador de Cassetes de Ligação de ATP/metabolismo
Proteínas de Bactérias/química
Proteínas de Bactérias/metabolismo
[Mh] Termos MeSH secundário: Subfamília B de Transportador de Cassetes de Ligação de ATP/genética
Sequência de Aminoácidos
Proteínas de Bactérias/genética
Sítios de Ligação
Chlorobium/genética
Chlorobium/metabolismo
Cristalografia por Raios X
Farmacorresistência Bacteriana Múltipla/genética
Genes Bacterianos
Genes MDR
Ligantes
Modelos Moleculares
Domínios Proteicos
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Homologia de Sequência de Aminoácidos
Soluções
Staphylococcus aureus/genética
Staphylococcus aureus/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ATP Binding Cassette Transporter, Sub-Family B); 0 (Bacterial Proteins); 0 (Ligands); 0 (Recombinant Proteins); 0 (Solutions)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160810
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.6b00651


  5 / 177 MEDLINE  
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[PMID]:27341807
[Au] Autor:Seo D; Kitashima M; Sakurai T; Inoue K
[Ad] Endereço:Division of Material Science, Graduate School of Natural Science and Technology, Kanazawa University, Kakuma, Kanazawa, Ishikawa, 920-1192, Japan. dseo@se.kanazawa-u.ac.jp.
[Ti] Título:Kinetics of NADP /NADPH reduction-oxidation catalyzed by the ferredoxin-NAD(P) reductase from the green sulfur bacterium Chlorobaculum tepidum.
[So] Source:Photosynth Res;130(1-3):479-489, 2016 Dec.
[Is] ISSN:1573-5079
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Ferredoxin-NAD(P) oxidoreductase (FNR, [EC 1.18.1.2], [EC 1.18.1.3]) from the green sulfur bacterium Chlorobaculum tepidum (CtFNR) is a homodimeric flavoprotein with significant structural homology to bacterial NADPH-thioredoxin reductases. CtFNR homologs have been found in many bacteria, but only in green sulfur bacteria among photoautotrophs. In this work, we examined the reactions of CtFNR with NADP , NADPH, and (4S- H)-NADPD by stopped-flow spectrophotometry. Mixing CtFNR with NADPH yielded a rapid decrease of the absorbance in flavin band I centered at 460 nm within 1 ms, and then the absorbance further decreased gradually. The magnitude of the decrease increased with increasing NADPH concentration, but even with ~50-fold molar excess NADPH, the absorbance change was only ~45 % of that expected for fully reduced protein. The absorbance in the charge transfer (CT) band centered around 600 nm increased rapidly within 1 ms, then slowly decreased to about 70 % of the maximum. When CtFNR was mixed with excess NADP , the absorbance in the flavin band I increased to about 70 % of that of CtFNR with an apparent rate of ~4 s , whereas almost no absorption changes were observed in the CT band. Obtained data suggest that the reaction between CtFNR and NADP /NADPH is reversible, in accordance with its physiological function.
[Mh] Termos MeSH primário: Chlorobium/enzimologia
Ferredoxina-NADP Redutase/metabolismo
NADP/metabolismo
[Mh] Termos MeSH secundário: Chlorobium/metabolismo
Cinética
Oxirredução
Estrutura Terciária de Proteína
Espectrofotometria/métodos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
53-59-8 (NADP); EC 1.18.1.2 (Ferredoxin-NADP Reductase)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:171101
[Lr] Data última revisão:
171101
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160626
[St] Status:MEDLINE


  6 / 177 MEDLINE  
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[PMID]:27128465
[Au] Autor:Buchanan BB
[Ad] Endereço:Department of Plant and Microbial Biology, University of California, Berkeley, California 94720; email: view@berkeley.edu.
[Ti] Título:The Path to Thioredoxin and Redox Regulation in Chloroplasts.
[So] Source:Annu Rev Plant Biol;67:1-24, 2016 Apr 29.
[Is] ISSN:1545-2123
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:After a brief discussion of my graduate work at Duke University, I describe a series of investigations on redox proteins at the University of California, Berkeley. Starting with ferredoxin from fermentative bacteria, the Berkeley research fostered experiments that uncovered a pathway for fixing CO2 in bacterial photosynthesis. The carbon work, in turn, opened new vistas, including the discovery that thioredoxin functions universally in regulating the Calvin-Benson cycle in oxygenic photosynthesis. These experiments, which took place over a 50-year period, led to the formulation of a set of biological principles and set the stage for research demonstrating a role for redox in the regulation of previously unrecognized processes extending far beyond photosynthesis.
[Mh] Termos MeSH primário: Carbono/metabolismo
Chlorobium/fisiologia
Cloroplastos/metabolismo
Ferredoxinas/metabolismo
Oxigênio/metabolismo
Fotossíntese
Tiorredoxinas/metabolismo
[Mh] Termos MeSH secundário: Dióxido de Carbono/metabolismo
Chlorobium/metabolismo
Ciclo do Ácido Cítrico
Ferredoxina-NADP Redutase/metabolismo
Oxirredução
Tiorredoxina Dissulfeto Redutase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Ferredoxins); 142M471B3J (Carbon Dioxide); 52500-60-4 (Thioredoxins); 7440-44-0 (Carbon); EC 1.18.1.2 (Ferredoxin-NADP Reductase); EC 1.8.1.9 (Thioredoxin-Disulfide Reductase); S88TT14065 (Oxygen)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170719
[Lr] Data última revisão:
170719
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160430
[St] Status:MEDLINE
[do] DOI:10.1146/annurev-arplant-043015-111949


  7 / 177 MEDLINE  
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[PMID]:26859266
[Au] Autor:Cohan FM
[Ad] Endereço:Department of Biology, Wesleyan University, Middletown, CT 06459, USA. Electronic address: fcohan@wesleyan.edu.
[Ti] Título:Bacterial Speciation: Genetic Sweeps in Bacterial Species.
[So] Source:Curr Biol;26(3):R112-5, 2016 Feb 08.
[Is] ISSN:1879-0445
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:One theory of bacterial speciation states that bacterial and animal species share the property of cohesion, meaning that diversity within a species is constrained. A new study provides direct evidence that genome-wide sweeps can limit diversity within bacterial species.
[Mh] Termos MeSH primário: Bactérias/genética
Especiação Genética
[Mh] Termos MeSH secundário: Chlorobium/genética
Genoma Bacteriano
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1606
[Cu] Atualização por classe:160210
[Lr] Data última revisão:
160210
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160210
[St] Status:MEDLINE


  8 / 177 MEDLINE  
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[PMID]:26565273
[Au] Autor:Duan HG; Dijkstra AG; Nalbach P; Thorwart M
[Ad] Endereço:I. Institut für Theoretische Physik, Universität Hamburg, Jungiusstraße 9, 20355 Hamburg, Germany.
[Ti] Título:Efficient tool to calculate two-dimensional optical spectra for photoactive molecular complexes.
[So] Source:Phys Rev E Stat Nonlin Soft Matter Phys;92(4):042708, 2015 Oct.
[Is] ISSN:1550-2376
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We combine the coherent modified Redfield theory (CMRT) with the equation of motion-phase matching approach (PMA) to calculate two-dimensional photon-echo spectra for photoactive molecular complexes with an intermediate strength of the coupling to their environment. Both techniques are highly efficient, yet they involve approximations at different levels. By explicitly comparing with the numerically exact quasiadiabatic path integral approach, we show for the Fenna-Matthews-Olson complex that the CMRT describes the decay rates in the population dynamics well, but final stationary populations and the oscillation frequencies differ slightly. In addition, we use the combined CMRT+PMA to calculate two-dimensional photon-echo spectra for a simple dimer model. We find excellent agreement with the exact path integral calculations at short waiting times where the dynamics is still coherent. For long waiting times, differences occur due to different final stationary states, specifically for strong system-bath coupling. For weak to intermediate system-bath couplings, which is most important for natural photosynthetic complexes, the combined CMRT+PMA gives reasonable results with acceptable computational efforts.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Complexos de Proteínas Captadores de Luz/química
Modelos Moleculares
Análise Espectral
[Mh] Termos MeSH secundário: Chlorobium
Simulação por Computador
Dimerização
Movimento (Física)
Fótons
Teoria Quântica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (FMO bacteriochlorophyll protein, Bacteria); 0 (Light-Harvesting Protein Complexes)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:151114
[Lr] Data última revisão:
151114
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151114
[St] Status:MEDLINE
[do] DOI:10.1103/PhysRevE.92.042708


  9 / 177 MEDLINE  
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[PMID]:26467441
[Au] Autor:Wreggelsworth KM; Barker D
[Ad] Endereço:School of Biology, University of St Andrews, St Andrews, Fife, KY16 9TH, UK. kristinwreggelsworth@yahoo.com.
[Ti] Título:A comparison of the protein-coding genomes of two green sulphur bacteria, Chlorobium tepidum TLS and Pelodictyon phaeoclathratiforme BU-1.
[So] Source:BMC Res Notes;8:565, 2015 Oct 14.
[Is] ISSN:1756-0500
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Chlorobium tepidum and Pelodictyon phaeoclathratiforme are organisms within the green sulphur bacteria family, Chlorobiaceae, occupying very different habitats. It has recently been proposed that the genera Chlorobium and Pelodictyon are synonymous. RESULTS: To investigate generic boundaries for the two species, protein families were predicted computationally based on sequence similarity across the genome-wide protein sets of Chlorobium tepidum TLS and Pelodictyon phaeoclathratiforme BU-1. The distribution of the resulting protein families across the two species was summarized. The largest number of families exhibited 1:1 putative orthology between the two species (1468 families). Of families unique to one of the species, the largest number was unique to P. phaeoclathratiforme (113 families), of which the largest family contained pentapeptide repeat proteins (16 proteins). Families unique to P. phaeoclathratiforme also included a family of gas vesicle synthesis proteins (four proteins). Although only seven families were identified as containing paralogous proteins in both species (with two or more proteins in each species), this group included families of major biochemical importance. One such family, with three members in each species, contained magnesium chelatase, an enzyme involved in the chlorophyll biosynthetic pathway. CONCLUSION: The unique protein family groups in both C. tepidum and P. phaeoclathratiforme mirror the occupancy of different environments, while key shared family groups provide evidence for a common origin for the species, as previously suggested in the literature. The current study only uses sequence similarity-based protein families for the two species. This, alone, does not permit a firm conclusion to be drawn on the taxonomic question, of whether the two species belong in one genus or two.
[Mh] Termos MeSH primário: Proteínas de Bactérias/genética
Chlorobi/genética
Chlorobium/genética
Genoma Bacteriano
Liases/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas de Bactérias/metabolismo
Chlorobi/classificação
Chlorobi/metabolismo
Chlorobium/classificação
Chlorobium/metabolismo
Biologia Computacional
Ecossistema
Expressão Gênica
Liases/metabolismo
Redes e Vias Metabólicas/genética
Anotação de Sequência Molecular
Dados de Sequência Molecular
Fases de Leitura Aberta
Filogenia
Alinhamento de Sequência
Homologia de Sequência de Aminoácidos
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); EC 4.- (Lyases); EC 4.99.1- (magnesium chelatase)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:151017
[Lr] Data última revisão:
151017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151016
[St] Status:MEDLINE
[do] DOI:10.1186/s13104-015-1535-8


  10 / 177 MEDLINE  
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[PMID]:26310572
[Au] Autor:Rudi K; Ho FY; Gilsbach BK; Pots H; Wittinghofer A; Kortholt A; Klare JP
[Ad] Endereço:Department of Physics, University of Osnabrueck, Barbarastr. 7, 49076 Osnabrueck, Germany.
[Ti] Título:Conformational heterogeneity of the Roc domains in C. tepidum Roc-COR and implications for human LRRK2 Parkinson mutations.
[So] Source:Biosci Rep;35(5), 2015 Aug 26.
[Is] ISSN:1573-4935
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Ras of complex proteins (Roc) is a Ras-like GTP-binding domain that always occurs in tandem with the C-terminal of Roc (COR) domain and is found in bacteria, plants and animals. Recently, it has been shown that Roco proteins belong to the family of G-proteins activated by nucleotide (nt)-dependent dimerization (GADs). We investigated the RocCOR tandem from the bacteria Chlorobium tepidum with site-directed spin labelling and pulse EPR distance measurements to follow conformational changes during the Roco G-protein cycle. Our results confirm that the COR domains are a stable dimerization device serving as a scaffold for the Roc domains that, in contrast, are structurally heterogeneous and dynamic entities. Contrary to other GAD proteins, we observed only minor structural alterations upon binding and hydrolysis of GTP, indicating significant mechanistic variations within this protein class. Mutations in the most prominent member of the Roco family of proteins, leucine-rich repeat (LRR) kinase 2 (LRRK2), are the most frequent cause of late-onset Parkinson's disease (PD). Using a stable recombinant LRRK2 Roc-COR-kinase fragment we obtained detailed kinetic data for the G-protein cycle. Our data confirmed that dimerization is essential for efficient GTP hydrolysis and PD mutations in the Roc domain result in decreased GTPase activity. Previous data have shown that these LRRK2 PD-mutations are located in the interface between Roc and COR. Importantly, analogous mutations in the conserved C. tepidum Roc/COR interface significantly influence the structure and nt-induced conformational changes of the Roc domains.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Chlorobium/química
Doença de Parkinson/genética
Mutação Puntual
Proteínas Serina-Treonina Quinases/química
Proteínas Serina-Treonina Quinases/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Chlorobium/genética
Chlorobium/metabolismo
GTP Fosfo-Hidrolases/metabolismo
Seres Humanos
Serina-Treonina Proteína Quinase-2 com Repetições Ricas em Leucina
Modelos Moleculares
Dados de Sequência Molecular
Doença de Parkinson/metabolismo
Multimerização Proteica
Estrutura Terciária de Proteína
Proteínas Serina-Treonina Quinases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); EC 2.7.11.1 (LRRK2 protein, human); EC 2.7.11.1 (Leucine-Rich Repeat Serine-Threonine Protein Kinase-2); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 3.6.1.- (GTP Phosphohydrolases)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150828
[St] Status:MEDLINE



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