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[PMID]:28915855
[Au] Autor:Chaiyasap P; Ittiwut C; Srichomthong C; Sangsin A; Suphapeetiporn K; Shotelersuk V
[Ad] Endereço:Center of Excellence for Medical Genetics, Department of Pediatrics, Faculty of Medicine, Chulalongkorn University, Bangkok, 10330, Thailand.
[Ti] Título:Massive parallel sequencing as a new diagnostic approach for phenylketonuria and tetrahydrobiopterin-deficiency in Thailand.
[So] Source:BMC Med Genet;18(1):102, 2017 Sep 16.
[Is] ISSN:1471-2350
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Hyperphenylalaninemia (HPA) can be classified into phenylketonuria (PKU) which is caused by mutations in the phenylalanine hydroxylase (PAH) gene, and BH4 deficiency caused by alterations in genes involved in tetrahydrobiopterin (BH4) biosynthesis pathway. Dietary restriction of phenylalanine is considered to be the main treatment of PKU to prevent irreversible intellectual disability. However, the same dietary intervention in BH4 deficiency patients is not as effective, as BH4 is also a cofactor in many neurotransmitter syntheses. METHOD: We utilized next generation sequencing (NGS) technique to investigate four unrelated Thai patients with hyperphenylalaninemia. RESULT: We successfully identified all eight mutant alleles in PKU or BH4-deficiency associated genes including three novel mutations, one in PAH and two in PTS, thus giving a definite diagnosis to these patients. Appropriate management can then be provided. CONCLUSION: This study identified three novel mutations in either the PAH or PTS gene and supported the use of NGS as an alternative molecular genetic approach for definite diagnosis of hyperphenylalaninemia, thus leading to proper management of these patients in Thailand.
[Mh] Termos MeSH primário: Grupo com Ancestrais do Continente Asiático/genética
Sequenciamento de Nucleotídeos em Larga Escala
Fenilalanina Hidroxilase/genética
Fenilcetonúrias/diagnóstico
Fósforo-Oxigênio Liases/genética
[Mh] Termos MeSH secundário: Alelos
Sequência de Aminoácidos
Biopterina/análogos & derivados
Biopterina/biossíntese
Exoma
Feminino
Genótipo
Seres Humanos
Lactente
Masculino
Fenilcetonúrias/genética
Análise de Sequência de DNA
Tailândia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
22150-76-1 (Biopterin); EC 1.14.16.1 (Phenylalanine Hydroxylase); EC 4.6.- (Phosphorus-Oxygen Lyases); EC 4.6.10 (6-pyruvoyltetrahydropterin synthase); EGX657432I (sapropterin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170917
[St] Status:MEDLINE
[do] DOI:10.1186/s12881-017-0464-x


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[PMID]:28792538
[Au] Autor:Wan X; Saito JA; Newhouse JS; Hou S; Alam M
[Ad] Endereço:Department of Microbiology, University of Hawaii, Honolulu, Hawaii, United States of America.
[Ti] Título:The importance of conserved amino acids in heme-based globin-coupled diguanylate cyclases.
[So] Source:PLoS One;12(8):e0182782, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Globin-coupled diguanylate cyclases contain globin, middle, and diguanylate cyclase domains that sense O2 to synthesize c-di-GMP and regulate bacterial motility, biofilm formation, and virulence. However, relatively few studies have extensively examined the roles of individual residues and domains of globin-coupled diguanylate cyclases, which can shed light on their signaling mechanisms and provide drug targets. Here, we report the critical residues of two globin-coupled diguanylate cyclases, EcGReg from Escherichia coli and BpeGReg from Bordetella pertussis, and show that their diguanylate cyclase activity requires an intact globin domain. In the distal heme pocket of the globin domain, residues Phe42, Tyr43, Ala68 (EcGReg)/Ser68 (BpeGReg), and Met69 are required to maintain full diguanylate cyclase activity. The highly conserved amino acids His223/His225 and Lys224/Lys226 in the middle domain of EcGReg/BpeGReg are essential to diguanylate cyclase activity. We also identified sixteen important residues (Leu300, Arg306, Asp333, Phe337, Lys338, Asn341, Asp342, Asp350, Leu353, Asp368, Arg372, Gly374, Gly375, Asp376, Glu377, and Phe378) in the active site and inhibitory site of the diguanylate cyclase domain of EcGReg. Moreover, BpeGReg266 (residues 1-266) and BpeGReg296 (residues 1-296), which only contain the globin and middle domains, can inhibit bacterial motility. Our findings suggest that the distal residues of the globin domain affect diguanylate cyclase activity and that BpeGReg may interact with other c-di-GMP-metabolizing proteins to form mixed signaling teams.
[Mh] Termos MeSH primário: Proteínas de Escherichia coli/genética
Proteínas de Escherichia coli/metabolismo
Globinas/metabolismo
Heme/metabolismo
Fósforo-Oxigênio Liases/genética
Fósforo-Oxigênio Liases/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Bordetella pertussis/enzimologia
Bordetella pertussis/genética
Sequência Conservada
Escherichia coli/enzimologia
Escherichia coli/genética
Modelos Moleculares
Mutação
Fenótipo
Domínios Proteicos
Estrutura Secundária de Proteína
Salmonella typhimurium
Homologia de Sequência de Aminoácidos
Natação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Escherichia coli Proteins); 42VZT0U6YR (Heme); 9004-22-2 (Globins); EC 4.6.- (Phosphorus-Oxygen Lyases); EC 4.6.1.- (diguanylate cyclase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171003
[Lr] Data última revisão:
171003
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170810
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0182782


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[PMID]:28652310
[Au] Autor:He C; Zhou Y; Liu F; Liu H; Tan H; Jin S; Wu W; Ge B
[Ad] Endereço:Shanghai Key Lab of Tuberculosis, Shanghai Pulmonary Hospital, Tongji University School of Medicine, Shanghai, China.
[Ti] Título:Bacterial Nucleotidyl Cyclase Inhibits the Host Innate Immune Response by Suppressing TAK1 Activation.
[So] Source:Infect Immun;85(9), 2017 Sep.
[Is] ISSN:1098-5522
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Exoenzyme Y (ExoY) is a type III secretion system effector found in 90% of the isolates. Although it is known that ExoY is a soluble nucleotidyl cyclase that increases the cytoplasmic levels of nucleoside 3',5'-cyclic monophosphates (cNMPs) to mediate endothelial Tau phosphorylation and permeability, its functional role in the innate immune response is still poorly understood. Transforming growth factor ß-activated kinase 1 (TAK1) is critical for mediating Toll-like receptor (TLR) signaling and subsequent activation of NF-κB and AP-1, which are transcriptional activators of innate immunity. Here, we report that ExoY inhibits proinflammatory cytokine production through suppressing the activation of TAK1 as well as downstream NF-κB and mitogen-activated protein (MAP) kinases. Mice infected with ExoY-deficient had higher levels of tumor necrosis factor (TNF) and interleukin-6 (IL-6), more neutrophil recruitment, and a lower bacterial load in lung tissue than mice infected with wild-type Taken together, our findings identify a previously unknown mechanism by which ExoY inhibits the host innate immune response.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Glucosiltransferases/metabolismo
Interações Hospedeiro-Patógeno
Evasão da Resposta Imune
Imunidade Inata
MAP Quinase Quinase Quinases/antagonistas & inibidores
Fósforo-Oxigênio Liases/metabolismo
Pseudomonas aeruginosa/patogenicidade
[Mh] Termos MeSH secundário: Animais
Proteínas de Bactérias/genética
Linhagem Celular
Citocinas/secreção
Modelos Animais de Doenças
Feminino
Deleção de Genes
Glucosiltransferases/genética
Seres Humanos
Camundongos Endogâmicos C57BL
NF-kappa B/metabolismo
Fósforo-Oxigênio Liases/genética
Infecções por Pseudomonas/microbiologia
Infecções por Pseudomonas/patologia
Pseudomonas aeruginosa/enzimologia
Fator de Transcrição AP-1/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Cytokines); 0 (NF-kappa B); 0 (Transcription Factor AP-1); EC 2.4.- (ExoY protein, bacteria); EC 2.4.1.- (Glucosyltransferases); EC 2.7.11.25 (MAP Kinase Kinase Kinases); EC 2.7.11.25 (MAP kinase kinase kinase 7); EC 4.6.- (Phosphorus-Oxygen Lyases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170628
[St] Status:MEDLINE


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[PMID]:28604167
[Au] Autor:Cusick KD; Dale JR; Fitzgerald LA; Little BJ; Biffinger JC
[Ad] Endereço:a Chemistry Department , US Naval Research Laboratory , Washington , DC , USA.
[Ti] Título:Adaptation to copper stress influences biofilm formation in Alteromonas macleodii.
[So] Source:Biofouling;33(6):505-519, 2017 Jul.
[Is] ISSN:1029-2454
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:An Alteromonas macleodii strain was isolated from copper-containing coupons incubated in surface seawater (Key West, FL, USA). In addition to the original isolate, a copper-adapted mutant was created and maintained with 0.78 mM Cu . Biofilm formation was compared between the two strains under copper-amended and low-nutrient conditions. Biofilm formation was significantly increased in the original isolate under copper amendment, while biofilm formation was significantly higher in the mutant under low-nutrient conditions. Biofilm expression profiles of diguanylate cyclase (DGC) genes, as well as genes involved in secretion, differed between the strains. Comparative genomic analysis demonstrated that both strains possessed a large number of gene attachment harboring cyclic di-GMP synthesis and/or degradation domains. One of the DGC genes, induced at very high levels in the mutant, possessed a degradation domain in the original isolate that was lacking in the mutant. The genetic and transcriptional mechanisms contributing to biofilm formation are discussed.
[Mh] Termos MeSH primário: Alteromonas/efeitos dos fármacos
Biofilmes/efeitos dos fármacos
Cobre/farmacologia
Desinfetantes/farmacologia
Farmacorresistência Bacteriana/efeitos dos fármacos
Genes Bacterianos
[Mh] Termos MeSH secundário: Alteromonas/genética
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Biofilmes/crescimento & desenvolvimento
Cobre/análise
GMP Cíclico/análogos & derivados
GMP Cíclico/biossíntese
Desinfetantes/análise
Farmacorresistência Bacteriana/genética
Proteínas de Escherichia coli/genética
Modelos Teóricos
Mutação
Fósforo-Oxigênio Liases/genética
Água do Mar/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Disinfectants); 0 (Escherichia coli Proteins); 61093-23-0 (bis(3',5')-cyclic diguanylic acid); 789U1901C5 (Copper); EC 4.6.- (Phosphorus-Oxygen Lyases); EC 4.6.1.- (diguanylate cyclase); H2D2X058MU (Cyclic GMP)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171003
[Lr] Data última revisão:
171003
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170613
[St] Status:MEDLINE
[do] DOI:10.1080/08927014.2017.1329423


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[PMID]:28601495
[Au] Autor:da Costa Vasconcelos FN; Maciel NK; Favaro DC; de Oliveira LC; Barbosa AS; Salinas RK; de Souza RF; Farah CS; Guzzo CR
[Ad] Endereço:Departamento de Microbiologia, Instituto de Ciências Biomedicas, Universidade de São Paulo, São Paulo, 05508-900, Brazil.
[Ti] Título:Structural and Enzymatic Characterization of a cAMP-Dependent Diguanylate Cyclase from Pathogenic Leptospira Species.
[So] Source:J Mol Biol;429(15):2337-2352, 2017 Jul 21.
[Is] ISSN:1089-8638
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Leptospira interrogans serovar Copenhageni is a human pathogen that causes leptospirosis, a worldwide zoonosis. The L. interrogans genome codes for a wide array of potential diguanylate cyclase (DGC) enzymes with characteristic GGDEF domains capable of synthesizing the cyclic dinucleotide c-di-GMP, known to regulate transitions between different cellular behavioral states in bacteria. Among such enzymes, LIC13137 (Lcd1), which has an N-terminal cGMP-specific phosphodiesterases, adenylyl cyclases, and FhlA (GAF) domain and a C-terminal GGDEF domain, is notable for having close orthologs present only in pathogenic Leptospira species. Although the function and structure of GGDEF and GAF domains have been studied extensively separately, little is known about enzymes with the GAF-GGDEF architecture. In this report, we address the question of how the GAF domain regulates the DGC activity of Lcd1. The full-length Lcd1 and its GAF domain form dimers in solution. The GAF domain binds specifically cAMP (K of 0.24µM) and has an important role in the regulation of the DGC activity of the GGDEF domain. Lcd1 DGC activity is negligible in the absence of cAMP and is significantly enhanced in its presence (specific activity of 0.13s ). The crystal structure of the Lcd1 GAF domain in complex with cAMP provides valuable insights toward explaining its specificity for cAMP and pointing to possible mechanisms by which this cyclic nucleotide regulates the assembly of an active DGC enzyme.
[Mh] Termos MeSH primário: AMP Cíclico/química
AMP Cíclico/metabolismo
Proteínas de Escherichia coli/química
Proteínas de Escherichia coli/metabolismo
Leptospira interrogans/enzimologia
Fósforo-Oxigênio Liases/química
Fósforo-Oxigênio Liases/metabolismo
[Mh] Termos MeSH secundário: Cristalografia por Raios X
Cinética
Modelos Moleculares
Ligação Proteica
Conformação Proteica
Multimerização Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Escherichia coli Proteins); E0399OZS9N (Cyclic AMP); EC 4.6.- (Phosphorus-Oxygen Lyases); EC 4.6.1.- (diguanylate cyclase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170726
[Lr] Data última revisão:
170726
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170612
[St] Status:MEDLINE


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[PMID]:28575400
[Au] Autor:Dalia TN; Yoon SH; Galli E; Barre FX; Waters CM; Dalia AB
[Ad] Endereço:Department of Biology, Indiana University, Bloomington, IN 47401, USA.
[Ti] Título:Enhancing multiplex genome editing by natural transformation (MuGENT) via inactivation of ssDNA exonucleases.
[So] Source:Nucleic Acids Res;45(12):7527-7537, 2017 Jul 07.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Recently, we described a method for multiplex genome editing by natural transformation (MuGENT). Mutant constructs for MuGENT require large arms of homology (>2000 bp) surrounding each genome edit, which necessitates laborious in vitro DNA splicing. In Vibrio cholerae, we uncover that this requirement is due to cytoplasmic ssDNA exonucleases, which inhibit natural transformation. In ssDNA exonuclease mutants, one arm of homology can be reduced to as little as 40 bp while still promoting integration of genome edits at rates of ∼50% without selection in cis. Consequently, editing constructs are generated in a single polymerase chain reaction where one homology arm is oligonucleotide encoded. To further enhance editing efficiencies, we also developed a strain for transient inactivation of the mismatch repair system. As a proof-of-concept, we used these advances to rapidly mutate 10 high-affinity binding sites for the nucleoid occlusion protein SlmA and generated a duodecuple mutant of 12 diguanylate cyclases in V. cholerae. Whole genome sequencing revealed little to no off-target mutations in these strains. Finally, we show that ssDNA exonucleases inhibit natural transformation in Acinetobacter baylyi. Thus, rational removal of ssDNA exonucleases may be broadly applicable for enhancing the efficacy and ease of MuGENT in diverse naturally transformable species.
[Mh] Termos MeSH primário: Proteínas de Bactérias/genética
Exonucleases/genética
Edição de Genes/métodos
Genoma Bacteriano
Transformação Bacteriana
[Mh] Termos MeSH secundário: Acinetobacter/genética
Acinetobacter/metabolismo
Proteínas de Bactérias/antagonistas & inibidores
Proteínas de Bactérias/metabolismo
Reparo de Erro de Pareamento de DNA
DNA Bacteriano/genética
DNA Bacteriano/metabolismo
DNA de Cadeia Simples/genética
DNA de Cadeia Simples/metabolismo
Proteínas de Escherichia coli/genética
Proteínas de Escherichia coli/metabolismo
Exonucleases/antagonistas & inibidores
Exonucleases/deficiência
Recombinação Homóloga
Reação em Cadeia da Polimerase Multiplex/métodos
Mutação
Fósforo-Oxigênio Liases/genética
Fósforo-Oxigênio Liases/metabolismo
Vibrio cholerae/genética
Vibrio cholerae/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (DNA, Bacterial); 0 (DNA, Single-Stranded); 0 (Escherichia coli Proteins); EC 3.1.- (Exonucleases); EC 4.6.- (Phosphorus-Oxygen Lyases); EC 4.6.1.- (diguanylate cyclase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170603
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx496


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[PMID]:28507067
[Au] Autor:Previato-Mello M; Meireles DA; Netto LES; da Silva Neto JF
[Ad] Endereço:Departamento de Biologia Celular e Molecular e Bioagentes Patogênicos, Faculdade de Medicina de Ribeirão Preto, Universidade de São Paulo, Ribeirão Preto, SP, Brazil.
[Ti] Título:Global Transcriptional Response to Organic Hydroperoxide and the Role of OhrR in the Control of Virulence Traits in Chromobacterium violaceum.
[So] Source:Infect Immun;85(8), 2017 Aug.
[Is] ISSN:1098-5522
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A major pathway for the detoxification of organic hydroperoxides, such as cumene hydroperoxide (CHP), involves the MarR family transcriptional regulator OhrR and the peroxidase OhrA. However, the effect of these peroxides on the global transcriptome and the contribution of the OhrA/OhrR system to bacterial virulence remain poorly explored. Here, we analyzed the transcriptome profiles of exposed to CHP and after the deletion of , and we show that OhrR controls the virulence of this human opportunistic pathogen. DNA microarray and Northern blot analyses of CHP-treated cells revealed the upregulation of genes related to the detoxification of peroxides (antioxidant enzymes and thiol-reducing systems), the degradation of the aromatic moiety of CHP (oxygenases), and protection against other secondary stresses (DNA repair, heat shock, iron limitation, and nitrogen starvation responses). Furthermore, we identified two upregulated genes ( and a putative diguanylate cyclase with a GGDEF domain for cyclic di-GMP [c-di-GMP] synthesis) and three downregulated genes (hemolysin, chitinase, and collagenase) in the mutant by transcriptome analysis. Importantly, we show that OhrR directly repressed the expression of the putative diguanylate cyclase. Using a mouse infection model, we demonstrate that the mutant was attenuated for virulence and showed a decreased bacterial burden in the liver. Moreover, an -diguanylate cyclase double mutant displayed the same virulence as the wild-type strain. In conclusion, we have defined the transcriptional response to CHP, identified potential virulence factors such as diguanylate cyclase as members of the OhrR regulon, and shown that uses the transcriptional regulator OhrR to modulate its virulence.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Derivados de Benzeno/metabolismo
Derivados de Benzeno/farmacologia
Chromobacterium/genética
Chromobacterium/patogenicidade
Proteínas Repressoras/metabolismo
Transcrição Genética
[Mh] Termos MeSH secundário: Animais
Carga Bacteriana
Proteínas de Bactérias/genética
Quitinases/genética
Colagenases/genética
Proteínas de Escherichia coli/genética
Perfilação da Expressão Gênica
Regulação Bacteriana da Expressão Gênica
Infecções por Bactérias Gram-Negativas/microbiologia
Proteínas Hemolisinas
Seres Humanos
Peróxido de Hidrogênio
Fígado/microbiologia
Camundongos
Oxigenases/metabolismo
Peroxidases/metabolismo
Fósforo-Oxigênio Liases/genética
Regiões Promotoras Genéticas
Proteínas Repressoras/genética
Estresse Fisiológico
Fatores de Transcrição/genética
Fatores de Transcrição/metabolismo
Virulência
Fatores de Virulência/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Benzene Derivatives); 0 (Escherichia coli Proteins); 0 (Hemolysin Proteins); 0 (Repressor Proteins); 0 (Transcription Factors); 0 (Virulence Factors); 0 (peroxide repressor proteins); BBX060AN9V (Hydrogen Peroxide); EC 1.11.1.- (Peroxidases); EC 1.13.- (Oxygenases); EC 3.2.1.14 (Chitinases); EC 3.4.24.- (Collagenases); EC 4.6.- (Phosphorus-Oxygen Lyases); EC 4.6.1.- (diguanylate cyclase); PG7JD54X4I (cumene hydroperoxide)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170807
[Lr] Data última revisão:
170807
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170517
[St] Status:MEDLINE


  8 / 695 MEDLINE  
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[PMID]:28264994
[Au] Autor:O'Neal L; Ryu MH; Gomelsky M; Alexandre G
[Ad] Endereço:Department of Biochemistry, Cellular and Molecular Biology, University of Tennessee, Knoxville, Tennessee, USA.
[Ti] Título:Optogenetic Manipulation of Cyclic Di-GMP (c-di-GMP) Levels Reveals the Role of c-di-GMP in Regulating Aerotaxis Receptor Activity in Azospirillum brasilense.
[So] Source:J Bacteriol;199(18), 2017 Sep 15.
[Is] ISSN:1098-5530
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Bacterial chemotaxis receptors provide the sensory inputs that inform the direction of navigation in changing environments. Recently, we described the bacterial second messenger cyclic di-GMP (c-di-GMP) as a novel regulator of a subclass of chemotaxis receptors. In , c-di-GMP binds to a chemotaxis receptor, Tlp1, and modulates its signaling function during aerotaxis. Here, we further characterize the role of c-di-GMP in aerotaxis using a novel dichromatic optogenetic system engineered for manipulating intracellular c-di-GMP levels in real time. This system comprises a red/near-infrared-light-regulated diguanylate cyclase and a blue-light-regulated c-di-GMP phosphodiesterase. It allows the generation of transient changes in intracellular c-di-GMP concentrations within seconds of irradiation with appropriate light, which is compatible with the time scale of chemotaxis signaling. We provide experimental evidence that binding of c-di-GMP to the Tlp1 receptor activates its signaling function during aerotaxis, which supports the role of transient changes in c-di-GMP levels as a means of adjusting the response of to oxygen gradients. We also show that intracellular c-di-GMP levels in change with carbon metabolism. Our data support a model whereby c-di-GMP functions to imprint chemotaxis receptors with a record of recent metabolic experience, to adjust their contribution to the signaling output, thus allowing the cells to continually fine-tune chemotaxis sensory perception to their metabolic state. Motile bacteria use chemotaxis to change swimming direction in response to changes in environmental conditions. Chemotaxis receptors sense environmental signals and relay sensory information to the chemotaxis machinery, which ultimately controls the swimming pattern of cells. In bacteria studied to date, differential methylation has been known as a mechanism to control the activity of chemotaxis receptors and modulates their contribution to the overall chemotaxis response. Here, we used an optogenetic system to perturb intracellular concentrations of the bacterial second messenger c-di-GMP to show that in some chemotaxis receptors, c-di-GMP functions in a similar feedback loop to connect the metabolic status of the cells to the sensory activity of chemotaxis receptors.
[Mh] Termos MeSH primário: Azospirillum brasilense/fisiologia
Quimiotaxia
GMP Cíclico/análogos & derivados
Regulação Bacteriana da Expressão Gênica
Locomoção
[Mh] Termos MeSH secundário: Carbono/metabolismo
GMP Cíclico/metabolismo
Proteínas de Escherichia coli/genética
Proteínas de Escherichia coli/metabolismo
Luz
Optogenética/métodos
Oxigênio/metabolismo
Diester Fosfórico Hidrolases/genética
Diester Fosfórico Hidrolases/metabolismo
Fósforo-Oxigênio Liases/genética
Fósforo-Oxigênio Liases/metabolismo
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 61093-23-0 (bis(3',5')-cyclic diguanylic acid); 7440-44-0 (Carbon); EC 3.1.4.- (Phosphoric Diester Hydrolases); EC 4.6.- (Phosphorus-Oxygen Lyases); EC 4.6.1.- (diguanylate cyclase); H2D2X058MU (Cyclic GMP); S88TT14065 (Oxygen)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170907
[Lr] Data última revisão:
170907
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170308
[St] Status:MEDLINE


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[PMID]:28167523
[Au] Autor:Ribbe J; Baker AE; Euler S; O'Toole GA; Maier B
[Ad] Endereço:Department of Physics, University of Cologne, Cologne, Germany.
[Ti] Título:Role of Cyclic Di-GMP and Exopolysaccharide in Type IV Pilus Dynamics.
[So] Source:J Bacteriol;199(8), 2017 Apr 15.
[Is] ISSN:1098-5530
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:For , levels of cyclic di-GMP (c-di-GMP) govern the transition from the planktonic state to biofilm formation. Type IV pili (T4P) are crucial determinants of biofilm structure and dynamics, but it is unknown how levels of c-di-GMP affect pilus dynamics. Here, we scrutinized how c-di-GMP affects molecular motor properties and adhesive behavior of T4P. By means of retraction, T4P generated forces of ∼30 pN. Deletion mutants in the proteins with known roles in biofilm formation, swarming motility, and exopolysaccharide (EPS) production (specifically, the diguanylate cyclases and or the c-di-GMP phosphodiesterase ) showed only modest effects on velocity or force of T4P retraction. At high levels of c-di-GMP, the production of exopolysaccharides, particularly of Pel, is upregulated. We found that Pel production strongly enhances T4P-mediated surface adhesion of , suggesting that T4P-matrix interactions may be involved in biofilm formation by Finally, our data support the previously proposed model of slingshot-like "twitching" motility of Type IV pili (T4P) play various important roles in the transition of bacteria from the planktonic state to the biofilm state, including surface attachment and surface sensing. Here, we investigate adhesion, dynamics, and force generation of T4P after bacteria engage a surface. Our studies showed that two critical components of biofilm formation by , T4P and exopolysaccharides, contribute to enhanced T4P-mediated force generation by attached bacteria. These data indicate a crucial role for the coordinated impact of multiple biofilm-promoting factors during the early stages of attachment to a surface. Our data are also consistent with a previous model explaining why pilus-mediated motility in results in characteristic "twitching" behavior.
[Mh] Termos MeSH primário: GMP Cíclico/análogos & derivados
Fímbrias Bacterianas/classificação
Fímbrias Bacterianas/metabolismo
Polissacarídeos Bacterianos/metabolismo
Pseudomonas aeruginosa/metabolismo
[Mh] Termos MeSH secundário: Sistemas de Secreção Bacterianos
GMP Cíclico/genética
GMP Cíclico/metabolismo
Proteínas de Escherichia coli/classificação
Proteínas de Escherichia coli/genética
Proteínas de Escherichia coli/metabolismo
Fímbrias Bacterianas/genética
Deleção de Genes
Regulação Bacteriana da Expressão Gênica/fisiologia
Regulação Enzimológica da Expressão Gênica
Movimento
Oxigênio/metabolismo
Diester Fosfórico Hidrolases/genética
Diester Fosfórico Hidrolases/metabolismo
Fósforo-Oxigênio Liases/classificação
Fósforo-Oxigênio Liases/genética
Fósforo-Oxigênio Liases/metabolismo
Polissacarídeos Bacterianos/genética
Pseudomonas aeruginosa/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Secretion Systems); 0 (Escherichia coli Proteins); 0 (Polysaccharides, Bacterial); 128531-82-8 (exopolysaccharide, Pseudomonas); 61093-23-0 (bis(3',5')-cyclic diguanylic acid); EC 3.1.4.- (Phosphoric Diester Hydrolases); EC 4.6.- (Phosphorus-Oxygen Lyases); EC 4.6.1.- (diguanylate cyclase); H2D2X058MU (Cyclic GMP); S88TT14065 (Oxygen)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170928
[Lr] Data última revisão:
170928
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170208
[St] Status:MEDLINE


  10 / 695 MEDLINE  
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[PMID]:28148244
[Au] Autor:Ahmad I; Cimdins A; Beske T; Römling U
[Ad] Endereço:Department of Microbiology, Tumor and Cell Biology, Karolinska Institutet, Stockholm, Sweden.
[Ti] Título:Detailed analysis of c-di-GMP mediated regulation of csgD expression in Salmonella typhimurium.
[So] Source:BMC Microbiol;17(1):27, 2017 Feb 02.
[Is] ISSN:1471-2180
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The secondary messenger cyclic di-GMP promotes biofilm formation by up regulating the expression of csgD, encoding the major regulator of rdar biofilm formation in Salmonella typhimurium. The GGDEF/EAL domain proteins regulate the c-di-GMP turnover. There are twenty- two GGDEF/EAL domain proteins in the genome of S. typhimurium. In this study, we dissect the role of individual GGDEF/EAL proteins for csgD expression and rdar biofilm development. RESULTS: Among twelve GGDEF domains, two proteins upregulate and among fifteen EAL domains, four proteins down regulate csgD expression. We identified two additional GGDEF proteins required to promote optimal csgD expression. With the exception of the EAL domain of STM1703, solely, diguanylate cyclase and phosphodiesterase activities are required to regulate csgD mediated rdar biofilm formation. Identification of corresponding phosphodiesterases and diguanylate cyclases interacting in the csgD regulatory network indicates various levels of regulation by c-di-GMP. The phosphodiesterase STM1703 represses transcription of csgD via a distinct promoter upstream region. CONCLUSION: The enzymatic activity and the protein scaffold of GGDEF/EAL domain proteins regulate csgD expression. Thereby, c-di-GMP adjusts csgD expression at multiple levels presumably using a multitude of input signals.
[Mh] Termos MeSH primário: Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
GMP Cíclico/análogos & derivados
Domínios Proteicos
Salmonella typhimurium/metabolismo
Salmonella typhimurium/fisiologia
[Mh] Termos MeSH secundário: Proteínas de Bactérias/isolamento & purificação
Biofilmes/crescimento & desenvolvimento
GMP Cíclico/metabolismo
Proteínas de Escherichia coli/metabolismo
Deleção de Genes
Regulação Bacteriana da Expressão Gênica/genética
Mutação
Fenótipo
Diester Fosfórico Hidrolases/metabolismo
Fósforo-Oxigênio Liases/metabolismo
Domínios Proteicos/genética
Salmonella typhimurium/enzimologia
Salmonella typhimurium/genética
Transdução de Sinais
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Escherichia coli Proteins); 61093-23-0 (bis(3',5')-cyclic diguanylic acid); EC 3.1.4.- (Phosphoric Diester Hydrolases); EC 4.6.- (Phosphorus-Oxygen Lyases); EC 4.6.1.- (diguanylate cyclase); H2D2X058MU (Cyclic GMP)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170925
[Lr] Data última revisão:
170925
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170203
[St] Status:MEDLINE
[do] DOI:10.1186/s12866-017-0934-5



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