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Pesquisa : B03.440.400.425.967.930.100 [Categoria DeCS]
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[PMID]:28471538
[Au] Autor:Santos C; Maximiano MR; Ribeiro DG; Oliveira-Neto OB; Murad AM; Franco OL; Mehta A
[Ad] Endereço:Embrapa Recursos Genéticos e Biotecnologia, Brasília, DF, Brazil.
[Ti] Título:Differential accumulation of Xanthomonas campestris pv. campestris proteins during the interaction with the host plant: Contributions of an in vivo system.
[So] Source:Proteomics;17(12), 2017 Jun.
[Is] ISSN:1615-9861
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Xanthomonas campestris pv. campestris (Xcc) is the causal agent of black rot, a highly destructive disease that affects all brassicas. This work aimed to study the interaction Xcc-Brassica oleracea using an in vivo system in an attempt to identify proteins involved in pathogenicity. We used label-free shotgun 2D-nanoUPLC/MS to analyze Xcc proteins in three conditions: in the interaction with susceptible (REK) and resistant (REU) plants and in culture medium (control condition). A model of Xcc-susceptible host interaction is proposed and shows that Xcc increases the abundance of several crucial proteins for infection and cell protection. In this study, we also confirmed the differential expression by qPCR analysis of selected genes. This is the first report showing a large-scale identification of proteins in an in vivo host plant condition. Considering that most studies involving phytopathogens are in vitro (growth in culture medium or in plant extract), this work contributes with relevant information related to the plant-pathogen interaction in planta.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Brassica/metabolismo
Brassica/microbiologia
Fatores de Virulência/metabolismo
Xanthomonas campestris/patogenicidade
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Brassica/crescimento & desenvolvimento
Interações Hospedeiro-Patógeno
Doenças das Plantas/microbiologia
Folhas de Planta/crescimento & desenvolvimento
Folhas de Planta/metabolismo
Folhas de Planta/microbiologia
Proteoma/metabolismo
Fatores de Virulência/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Proteome); 0 (Virulence Factors)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1002/pmic.201700086


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[PMID]:28872321
[Au] Autor:Christenson JK; Robinson SL; Engel TA; Richman JE; Kim AN; Wackett LP
[Ad] Endereço:Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota , Minneapolis, Minnesota 55455, United States.
[Ti] Título:OleB from Bacterial Hydrocarbon Biosynthesis Is a ß-Lactone Decarboxylase That Shares Key Features with Haloalkane Dehalogenases.
[So] Source:Biochemistry;56(40):5278-5287, 2017 Oct 10.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:OleB is an α/ß-hydrolase found in bacteria that biosynthesize long-chain olefinic hydrocarbons, but its function has remained obscure. We report that OleB from the Gram-negative bacterium Xanthomonas campestris performs an unprecedented ß-lactone decarboxylation reaction, to complete cis-olefin biosynthesis. OleB reactions monitored by H nuclear magnetic resonance spectroscopy revealed a selectivity for decarboxylating cis-ß-lactones and no discernible activity with trans-ß-lactones, consistent with the known configuration of pathway intermediates. Protein sequence analyses showed OleB proteins were most related to haloalkane dehalogenases (HLDs) and retained the canonical Asp-His-Asp catalytic triad of HLDs. Unexpectedly, it was determined that an understudied subfamily, denoted as HLD-III, is comprised mostly of OleB proteins encoded within oleABCD gene clusters, suggesting a misannotation. OleB from X. campestris showed very low dehalogenase activity only against haloalkane substrates with long alkyl chains. A haloalkane substrate mimic alkylated wild-type X. campestris OleB but not OleB , implicating this residue as the active site nucleophile as in HLDs. A sequence-divergent OleB, found as part of a natural OleBC fusion and classified as an HLD-III, from the Gram-positive bacterium Micrococcus luteus was demonstrated to have the same activity, stereochemical preference, and dependence on the proposed Asp nucleophile. H O studies with M. luteus OleBC suggested that the canonical alkyl-enzyme intermediate of HLDs is hydrolyzed differently by OleB enzymes, as O is not incorporated into the nucleophilic aspartic acid. This work defines a previously unrecognized reaction in nature, functionally identifies some HLD-III enzymes as ß-lactone decarboxylases, and posits an enzymatic mechanism of ß-lactone decarboxylation.
[Mh] Termos MeSH primário: Carboxiliases/metabolismo
Hidrocarbonetos/metabolismo
Hidrolases/metabolismo
Lactonas/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Biocatálise
Carboxiliases/química
Carboxiliases/genética
Mutagênese Sítio-Dirigida
Especificidade por Substrato
Xanthomonas campestris/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Hydrocarbons); 0 (Lactones); EC 3.- (Hydrolases); EC 3.8.1.5 (haloalkane dehalogenase); EC 4.1.1.- (Carboxy-Lyases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171019
[Lr] Data última revisão:
171019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170906
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00667


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[PMID]:28369120
[Au] Autor:Cai Z; Yuan ZH; Zhang H; Pan Y; Wu Y; Tian XQ; Wang FF; Wang L; Qian W
[Ad] Endereço:State Key Laboratory of Plant Genomics, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China.
[Ti] Título:Fatty acid DSF binds and allosterically activates histidine kinase RpfC of phytopathogenic bacterium Xanthomonas campestris pv. campestris to regulate quorum-sensing and virulence.
[So] Source:PLoS Pathog;13(4):e1006304, 2017 Apr.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:As well as their importance to nutrition, fatty acids (FA) represent a unique group of quorum sensing chemicals that modulate the behavior of bacterial population in virulence. However, the way in which full-length, membrane-bound receptors biochemically detect FA remains unclear. Here, we provide genetic, enzymological and biophysical evidences to demonstrate that in the phytopathogenic bacterium Xanthomonas campestris pv. campestris, a medium-chain FA diffusible signal factor (DSF) binds directly to the N-terminal, 22 amino acid-length sensor region of a receptor histidine kinase (HK), RpfC. The binding event remarkably activates RpfC autokinase activity by causing an allosteric change associated with the dimerization and histidine phosphotransfer (DHp) and catalytic ATP-binding (CA) domains. Six residues were found essential for sensing DSF, especially those located in the region adjoining to the inner membrane of cells. Disrupting direct DSF-RpfC interaction caused deficiency in bacterial virulence and biofilm development. In addition, two amino acids within the juxtamembrane domain of RpfC, Leu172 and Ala178, are involved in the autoinhibition of the RpfC kinase activity. Replacements of them caused constitutive activation of RpfC-mediated signaling regardless of DSF stimulation. Therefore, our results revealed a biochemical mechanism whereby FA activates bacterial HK in an allosteric manner, which will assist in future studies on the specificity of FA-HK recognition during bacterial virulence regulation and cell-cell communication.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Biofilmes/crescimento & desenvolvimento
Ácidos Graxos/metabolismo
Doenças das Plantas/microbiologia
Percepção de Quorum
Xanthomonas campestris/enzimologia
[Mh] Termos MeSH secundário: Regulação Alostérica
Proteínas de Bactérias/genética
Regulação Bacteriana da Expressão Gênica
Genes Reporter
Modelos Moleculares
Mutação
Fenótipo
Fosforilação
Proteínas Quinases/genética
Proteínas Quinases/metabolismo
Transdução de Sinais
Virulência
Xanthomonas campestris/genética
Xanthomonas campestris/patogenicidade
Xanthomonas campestris/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Fatty Acids); 0 (rpfC protein, Xanthomonas); EC 2.7.- (Protein Kinases); EC 2.7.1.- (autophosphorylation-dependent multifunctional protein kinase)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170516
[Lr] Data última revisão:
170516
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170404
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006304


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[PMID]:28267413
[Au] Autor:Wang Z; Wu J; Gao MJ; Zhu L; Zhan XB
[Ad] Endereço:a The Key Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education , School of Biotechnology, Jiangnan University , Wuxi , Jiangsu , China.
[Ti] Título:High production of xanthan gum by a glycerol-tolerant strain Xanthomonas campestris WXLB-006.
[So] Source:Prep Biochem Biotechnol;47(5):468-472, 2017 May 28.
[Is] ISSN:1532-2297
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The superior properties of xanthan gum make it an industrial aginomoto used in many industries, especially in oil recovery. In the present work, xanthan production from glycerol by a mutant strain Xanthomonas campestris WXLB-006 reached as high as 17.8 g/L in flask culture. With the adoption of pH control, varied aeration and agitation, and varied glycerol feeding strategy, xanthan production reached 33.9 g/L in a 7-L fermenter and fermentation time decreased to 60 hr. Instead of difficultly and costly purifying glycerol, this research provides a very good case for glycerol utilization. At the same time, this is the first report on a high glycerol-tolerant strain for microbial polysaccharide production and 33.9 g/L is the highest production of xanthan gum produced from glycerol so far.
[Mh] Termos MeSH primário: Glicerol/metabolismo
Microbiologia Industrial/métodos
Polissacarídeos Bacterianos/metabolismo
Xanthomonas campestris/metabolismo
[Mh] Termos MeSH secundário: Fermentação
Concentração de Íons de Hidrogênio
Mutação
Xanthomonas campestris/genética
Xanthomonas campestris/crescimento & desenvolvimento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Polysaccharides, Bacterial); PDC6A3C0OX (Glycerol); TTV12P4NEE (xanthan gum)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171006
[Lr] Data última revisão:
171006
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170308
[St] Status:MEDLINE
[do] DOI:10.1080/10826068.2017.1292288


  5 / 964 MEDLINE  
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[PMID]:28223313
[Au] Autor:Christenson JK; Jensen MR; Goblirsch BR; Mohamed F; Zhang W; Wilmot CM; Wackett LP
[Ad] Endereço:Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, St. Paul, Minnesota, USA.
[Ti] Título:Active Multienzyme Assemblies for Long-Chain Olefinic Hydrocarbon Biosynthesis.
[So] Source:J Bacteriol;199(9), 2017 May 01.
[Is] ISSN:1098-5530
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Bacteria from different phyla produce long-chain olefinic hydrocarbons derived from an OleA-catalyzed Claisen condensation of two fatty acyl coenzyme A (acyl-CoA) substrates, followed by reduction and oxygen elimination reactions catalyzed by the proteins OleB, OleC, and OleD. In this report, OleA, OleB, OleC, and OleD were individually purified as soluble proteins, and all were found to be essential for reconstituting hydrocarbon biosynthesis. Recombinant coexpression of tagged OleABCD proteins from in and purification over His and FLAG columns resulted in OleA separating, while OleBCD purified together, irrespective of which of the four Ole proteins were tagged. Hydrocarbon biosynthetic activity of copurified OleBCD assemblies could be reconstituted by adding separately purified OleA. Immunoblots of nondenaturing gels using anti-OleC reacted with crude protein lysate indicated the presence of a large protein assembly containing OleC in the native host. Negative-stain electron microscopy of recombinant OleBCD revealed distinct large structures with diameters primarily between 24 and 40 nm. Assembling OleB, OleC, and OleD into a complex may be important to maintain stereochemical integrity of intermediates, facilitate the movement of hydrophobic metabolites between enzyme active sites, and protect the cell against the highly reactive ß-lactone intermediate produced by the OleC-catalyzed reaction. Bacteria biosynthesize hydrophobic molecules to maintain a membrane, store carbon, and for antibiotics that help them survive in their niche. The hydrophobic compounds are often synthesized by a multidomain protein or by large multienzyme assemblies. The present study reports on the discovery that long-chain olefinic hydrocarbons made by bacteria from different phyla are produced by multienzyme assemblies in The OleBCD multienzyme assemblies are thought to compartmentalize and sequester olefin biosynthesis from the rest of the cell. This system provides additional insights into how bacteria control specific biosynthetic pathways.
[Mh] Termos MeSH primário: Alcenos/metabolismo
Vias Biossintéticas
Hidrocarbonetos/metabolismo
Complexos Multienzimáticos/metabolismo
Xanthomonas campestris/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Domínio Catalítico
Escherichia coli/genética
Complexos Multienzimáticos/química
Complexos Multienzimáticos/isolamento & purificação
Especificidade por Substrato
Xanthomonas campestris/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Alkenes); 0 (Bacterial Proteins); 0 (Hydrocarbons); 0 (Multienzyme Complexes)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171011
[Lr] Data última revisão:
171011
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170223
[St] Status:MEDLINE


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[PMID]:28155188
[Au] Autor:Sendín LN; Orce IG; Gómez RL; Enrique R; Grellet Bournonville CF; Noguera AS; Vojnov AA; Marano MR; Castagnaro AP; Filippone MP
[Ad] Endereço:Estación Experimental Agroindustrial Obispo Colombres (EEAOC) - Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Instituto de Tecnología Agroindustrial del Noroeste Argentino (ITANOA), Av. William Cross 3150, T4101XAC, Las Talitas, Tucumán, Argentina.
[Ti] Título:Inducible expression of Bs2 R gene from Capsicum chacoense in sweet orange (Citrus sinensis L. Osbeck) confers enhanced resistance to citrus canker disease.
[So] Source:Plant Mol Biol;93(6):607-621, 2017 Apr.
[Is] ISSN:1573-5028
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Transgenic expression of the pepper Bs2 gene confers resistance to Xanthomonas campestris pv. vesicatoria (Xcv) pathogenic strains which contain the avrBs2 avirulence gene in susceptible pepper and tomato varieties. The avrBs2 gene is highly conserved among members of the Xanthomonas genus, and the avrBs2 of Xcv shares 96% homology with the avrBs2 of Xanthomonas citri subsp. citri (Xcc), the causal agent of citrus canker disease. A previous study showed that the transient expression of pepper Bs2 in lemon leaves reduced canker formation and induced plant defence mechanisms. In this work, the effect of the stable expression of Bs2 gene on citrus canker resistance was evaluated in transgenic plants of Citrus sinensis cv. Pineapple. Interestingly, Agrobacterium-mediated transformation of epicotyls was unsuccessful when a constitutive promoter (2× CaMV 35S) was used in the plasmid construction, but seven transgenic lines were obtained with a genetic construction harbouring Bs2 under the control of a pathogen-inducible promoter, from glutathione S-transferase gene from potato. A reduction of disease symptoms of up to 70% was observed in transgenic lines expressing Bs2 with respect to non-transformed control plants. This reduction was directly dependent on the Xcc avrBs2 gene since no effect was observed when a mutant strain of Xcc with a disruption in avrBs2 gene was used for inoculations. Additionally, a canker symptom reduction was correlated with levels of the Bs2 expression in transgenic plants, as assessed by real-time qPCR, and accompanied by the production of reactive oxygen species. These results indicate that the pepper Bs2 resistance gene is also functional in a family other than the Solanaceae, and could be considered for canker control.
[Mh] Termos MeSH primário: Capsicum/genética
Citrus sinensis/genética
Citrus sinensis/microbiologia
Doenças das Plantas/microbiologia
Xanthomonas campestris/patogenicidade
[Mh] Termos MeSH secundário: Agrobacterium tumefaciens/genética
Resistência à Doença/genética
Regulação da Expressão Gênica de Plantas
Doenças das Plantas/genética
Brotos de Planta/genética
Plantas Geneticamente Modificadas
Regiões Promotoras Genéticas
Transformação Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1704
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170204
[St] Status:MEDLINE
[do] DOI:10.1007/s11103-017-0586-8


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[PMID]:28045455
[Au] Autor:Bernal P; Allsopp LP; Filloux A; Llamas MA
[Ad] Endereço:MRC Centre for Molecular Bacteriology and Infection, Department of Life Sciences, Imperial College London, London, UK.
[Ti] Título:The Pseudomonas putida T6SS is a plant warden against phytopathogens.
[So] Source:ISME J;11(4):972-987, 2017 Apr.
[Is] ISSN:1751-7370
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Bacterial type VI secretion systems (T6SSs) are molecular weapons designed to deliver toxic effectors into prey cells. These nanomachines have an important role in inter-bacterial competition and provide advantages to T6SS active strains in polymicrobial environments. Here we analyze the genome of the biocontrol agent Pseudomonas putida KT2440 and identify three T6SS gene clusters (K1-, K2- and K3-T6SS). Besides, 10 T6SS effector-immunity pairs were found, including putative nucleases and pore-forming colicins. We show that the K1-T6SS is a potent antibacterial device, which secretes a toxic Rhs-type effector Tke2. Remarkably, P. putida eradicates a broad range of bacteria in a K1-T6SS-dependent manner, including resilient phytopathogens, which demonstrates that the T6SS is instrumental to empower P. putida to fight against competitors. Furthermore, we observed a drastically reduced necrosis on the leaves of Nicotiana benthamiana during co-infection with P. putida and Xanthomonas campestris. Such protection is dependent on the activity of the P. putida T6SS. Many routes have been explored to develop biocontrol agents capable of manipulating the microbial composition of the rhizosphere and phyllosphere. Here we unveil a novel mechanism for plant biocontrol, which needs to be considered for the selection of plant wardens whose mission is to prevent phytopathogen infections.
[Mh] Termos MeSH primário: Doenças das Plantas/prevenção & controle
Pseudomonas putida/fisiologia
Tabaco/microbiologia
Xanthomonas campestris/fisiologia
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Agentes de Controle Biológico
Regulação Bacteriana da Expressão Gênica
Doenças das Plantas/microbiologia
Pseudomonas putida/genética
Sistemas de Secreção Tipo VI/genética
Sistemas de Secreção Tipo VI/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Biological Control Agents); 0 (Type VI Secretion Systems)
[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:170104
[St] Status:MEDLINE
[do] DOI:10.1038/ismej.2016.169


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[PMID]:27995281
[Au] Autor:Sabuquillo P; Gea A; Matas IM; Ramos C; Cubero J
[Ad] Endereço:Laboratorio de Bacteriología. Departamento de Protección Vegetal, Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria (INIA), Madrid, Spain.
[Ti] Título:The use of stable and unstable green fluorescent proteins for studies in two bacterial models: Agrobacterium tumefaciens and Xanthomonas campestris pv. campestris.
[So] Source:Arch Microbiol;199(4):581-590, 2017 May.
[Is] ISSN:1432-072X
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Fluorescent proteins have been used to track plant pathogens to understand their host interactions. To be useful, the transgenic pathogens must present similar behaviour than the wild-type isolates. Herein, a GFP marker was used to transform two plant pathogenic bacteria, Agrobacterium and Xanthomonas, to localize and track the bacteria during infection. The transgenic bacteria were evaluated to determine whether they showed the same fitness than the wild-type strains or whether the expression of the GFP protein interfered in the bacterial activity. In Agrobacterium, the plasmid used for transformation was stable in the bacteria and the strain kept the virulence, while Xanthomonas was not able to conserve the plasmid and transformed strains showed virulence variations compared to wild-type strains. Although marking bacteria with GFP to track infection in plants is a common issue, works to validate the transgenic strains and corroborate their fitness are not usual. Results, presented here, confirm the importance of proper fitness tests on the marked strains before performing localization assays, to avoid underestimation of the microbe population or possible artificial effects in its interaction with the plant.
[Mh] Termos MeSH primário: Agrobacterium tumefaciens/genética
Proteínas de Fluorescência Verde/análise
Xanthomonas campestris/genética
[Mh] Termos MeSH secundário: Agrobacterium tumefaciens/patogenicidade
Proteínas de Fluorescência Verde/genética
Modelos Biológicos
Organismos Geneticamente Modificados
Doenças das Plantas/microbiologia
Plantas/microbiologia
Plasmídeos/genética
Transformação Bacteriana
Virulência
Xanthomonas campestris/patogenicidade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
147336-22-9 (Green Fluorescent Proteins)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170802
[Lr] Data última revisão:
170802
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161221
[St] Status:MEDLINE
[do] DOI:10.1007/s00203-016-1327-0


  9 / 964 MEDLINE  
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[PMID]:27928637
[Au] Autor:Han SW; Hwang BK
[Ad] Endereço:Department of Integrative Plant Science, Chung-Ang University, Anseong, 17546, Republic of Korea.
[Ti] Título:Molecular functions of Xanthomonas type III effector AvrBsT and its plant interactors in cell death and defense signaling.
[So] Source:Planta;245(2):237-253, 2017 Feb.
[Is] ISSN:1432-2048
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:MAIN CONCLUSION: Xanthomonas effector AvrBsT interacts with plant defense proteins and triggers cell death and defense response. This review highlights our current understanding of the molecular functions of AvrBsT and its host interactor proteins. The AvrBsT protein is a member of a growing family of effector proteins in both plant and animal pathogens. Xanthomonas type III effector AvrBsT, a member of the YopJ/AvrRxv family, suppresses plant defense responses in susceptible hosts, but triggers cell death signaling leading to hypersensitive response (HR) and defense responses in resistant plants. AvrBsT interacts with host defense-related proteins to trigger the HR cell death and defense responses in plants. Here, we review and discuss recent progress in understanding the molecular functions of AvrBsT and its host interactor proteins in pepper (Capsicum annuum). Pepper arginine decarboxylase1 (CaADC1), pepper aldehyde dehydrogenase1 (CaALDH1), pepper heat shock protein 70a (CaHSP70a), pepper suppressor of the G2 allele of skp1 (CaSGT1), pepper SNF1-related kinase1 (SnRK1), and Arabidopsis acetylated interacting protein1 (ACIP1) have been identified as AvrBsT interactors in pepper and Arabidopsis. Gene expression profiling, virus-induced gene silencing, and transient transgenic overexpression approaches have advanced the functional characterization of AvrBsT-interacting proteins in plants. AvrBsT is localized in the cytoplasm and forms protein-protein complexes with host interactors. All identified AvrBsT interactors regulate HR cell death and defense responses in plants. Notably, CaSGT1 physically binds to both AvrBsT and pepper receptor-like cytoplasmic kinase1 (CaPIK1) in the cytoplasm. During infection with Xanthomonas campestris pv. vesicatoria strain Ds1 (avrBsT), AvrBsT is phosphorylated by CaPIK1 and forms the active AvrBsT-CaSGT1-CaPIK1 complex, which ultimately triggers HR cell death and defense responses. Collectively, the AvrBsT interactor proteins are involved in plant cell death and immunity signaling.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Capsicum/microbiologia
Interações Hospedeiro-Patógeno
Células Vegetais/microbiologia
Xanthomonas campestris/patogenicidade
[Mh] Termos MeSH secundário: Aldeído Desidrogenase/genética
Aldeído Desidrogenase/metabolismo
Proteínas de Bactérias/genética
Capsicum/metabolismo
Carboxiliases/genética
Carboxiliases/metabolismo
Morte Celular
Proteínas de Choque Térmico HSP70/metabolismo
Células Vegetais/metabolismo
Proteínas de Plantas/genética
Proteínas de Plantas/metabolismo
Transdução de Sinais
Xanthomonas campestris/metabolismo
Xanthomonas campestris/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (HSP70 Heat-Shock Proteins); 0 (Plant Proteins); EC 1.2.1.3 (Aldehyde Dehydrogenase); EC 4.1.1.- (Carboxy-Lyases); EC 4.1.1.19 (arginine decarboxylase)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:171005
[Lr] Data última revisão:
171005
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161209
[St] Status:MEDLINE
[do] DOI:10.1007/s00425-016-2628-x


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[PMID]:27895129
[Au] Autor:Hausner J; Hartmann N; Jordan M; Büttner D
[Ad] Endereço:Institute of Biology, Genetics Department, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany.
[Ti] Título:The Predicted Lytic Transglycosylase HpaH from Xanthomonas campestris pv. vesicatoria Associates with the Type III Secretion System and Promotes Effector Protein Translocation.
[So] Source:Infect Immun;85(2), 2017 Feb.
[Is] ISSN:1098-5522
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The pathogenicity of the Gram-negative plant-pathogenic bacterium Xanthomonas campestris pv. vesicatoria depends on a type III secretion (T3S) system, which spans both bacterial membranes and translocates effector proteins into plant cells. The assembly of the T3S system presumably involves the predicted lytic transglycosylase (LT) HpaH, which is encoded adjacent to the T3S gene cluster. Bacterial LTs degrade peptidoglycan and often promote the formation of membrane-spanning macromolecular protein complexes. In the present study, we show that HpaH localizes to the bacterial periplasm and binds to peptidoglycan as well as to components of the T3S system, including the predicted periplasmic inner rod proteins HrpB1 and HrpB2 as well as the pilus protein HrpE. In vivo translocation assays revealed that HpaH promotes the translocation of various effector proteins and of early substrates of the T3S system, suggesting a general contribution of HpaH to type III-dependent protein export. Mutant studies and the analysis of reporter fusions showed that the N-terminal region of HpaH contributes to protein function and is proteolytically cleaved. The N-terminally truncated HpaH cleavage product is secreted into the extracellular milieu by a yet-unknown transport pathway, which is independent of the T3S system.
[Mh] Termos MeSH primário: Peptidoglicano Glicosiltransferase/metabolismo
Sistemas de Secreção Tipo III
Xanthomonas campestris/fisiologia
Xanthomonas vesicatoria/fisiologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Sequência de Bases
Códon de Iniciação
Expressão Gênica
Regulação Bacteriana da Expressão Gênica
Modelos Moleculares
Conformação Molecular
Peptidoglicano/química
Peptidoglicano/metabolismo
Peptidoglicano Glicosiltransferase/química
Peptidoglicano Glicosiltransferase/genética
Plantas/microbiologia
Ligação Proteica
Biossíntese de Proteínas
Domínios e Motivos de Interação entre Proteínas
Transporte Proteico
Proteólise
Proteínas Recombinantes de Fusão/metabolismo
Deleção de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Codon, Initiator); 0 (Peptidoglycan); 0 (Recombinant Fusion Proteins); 0 (Type III Secretion Systems); EC 2.4.1.129 (Peptidoglycan Glycosyltransferase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170726
[Lr] Data última revisão:
170726
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161130
[St] Status:MEDLINE



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