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1.
Front Fungal Biol ; 2: 678840, 2021.
Artigo em Inglês | MEDLINE | ID: mdl-37744104

RESUMO

Fungal and bacterial pathogens generate devastating diseases and cause significant tomato crop losses worldwide. Due to chemical pesticides harming the environment and human health, alternative disease control strategies, including microorganismal bio-control agents (BCAs), are increasingly sought-after in agriculture. Bio-control microorganisms such as Trichoderma spp. have been shown to activate induced systemic resistance (ISR) in the host. However, examples of highly active bio-control microorganisms in agricultural settings are still lacking, due primarily to inconsistency in bio-control efficacy, often leading to widespread disease prior to the required ISR induction in the host. As part of its plant colonization strategy, Trichoderma spp. can secrete various compounds and molecules, which can effect host priming/ISR. One of these molecules synthesized and secreted from several species of Trichoderma is the family 11 xylanase enzyme known as ethylene inducing xylanase, EIX. EIX acts as an ISR elicitor in specific plant species and varieties. The response to EIX in tobacco and tomato cultivars is controlled by a single dominant locus, termed LeEIX, which contains two receptors, LeEIX1 and LeEIX2, both belonging to a class of leucine-rich repeat cell-surface glycoproteins. Both receptors are able to bind EIX, however, while LeEIX2 mediates plant defense responses, LeEIX1 acts as a decoy receptor and attenuates EIX induced immune signaling of the LeEIX2 receptor. By mutating LeEIX1 using CRISPR/Cas9, here, we report an enhancement of receptivity to T. harzianum mediated ISR and disease bio-control in tomato.

2.
Plant Cell Environ ; 41(10): 2313-2327, 2018 10.
Artigo em Inglês | MEDLINE | ID: mdl-29790585

RESUMO

Plant recognition and defence against pathogens employs a two-tiered perception system. Surface-localized pattern recognition receptors (PRRs) act to recognize microbial features, whereas intracellular nucleotide-binding leucine-rich repeat receptors (NLRs) directly or indirectly recognize pathogen effectors inside host cells. Employing the tomato PRR LeEIX2/EIX model system, we explored the molecular mechanism of signalling pathways. We identified an NLR that can associate with LeEIX2, termed SlNRC4a (NB-LRR required for hypersensitive response-associated cell death-4). Co-immunoprecipitation demonstrates that SlNRC4a is able to associate with different PRRs. Physiological assays with specific elicitors revealed that SlNRC4a generally alters PRR-mediated responses. SlNRC4a overexpression enhances defence responses, whereas silencing SlNRC4 reduces plant immunity. Moreover, the coiled-coil domain of SlNRC4a is able to associate with LeEIX2 and is sufficient to enhance responses upon EIX perception. On the basis of these findings, we propose that SlNRC4a acts as a noncanonical positive regulator of immunity mediated by diverse PRRs. Thus, SlNRC4a could link both intracellular and extracellular immune perceptions.


Assuntos
Proteínas NLR/fisiologia , Imunidade Vegetal , Proteínas de Plantas/fisiologia , Western Blotting , Proteína 9 Associada à CRISPR , Sistemas CRISPR-Cas , Etilenos/metabolismo , Edição de Genes , Imunoprecipitação , Solanum lycopersicum/imunologia , Solanum lycopersicum/fisiologia , Espectrometria de Massas , Microscopia Confocal , Proteínas NLR/metabolismo , Reguladores de Crescimento de Plantas/metabolismo , Proteínas de Plantas/metabolismo , Plantas Geneticamente Modificadas , Reação em Cadeia da Polimerase , Espécies Reativas de Oxigênio/metabolismo , Receptores de Reconhecimento de Padrão/metabolismo , Receptores de Reconhecimento de Padrão/fisiologia , Transdução de Sinais
3.
Cell Cycle ; 13(21): 3436-41, 2014.
Artigo em Inglês | MEDLINE | ID: mdl-25485587

RESUMO

Animal cell division ends with the cutting of the microtubule and membrane intercellular bridge connecting the 2 daughter cells. This process, known as cytokinetic abscission (abscission), is widely regarded as the last step of cytokinesis, i.e., the last step of the cell cycle. Major breakthroughs have been recently achieved, illuminating mechanistic aspects of abscission; however, the timing of abscission with respect to the mammalian cell cycle remains unclear. In this study, we carefully measured the onset and progression of abscission in dividing cells expressing a G1 reporter. We conclude that abscission commences long after cells enter the G1 phase. Affiliating abscission with G1 is beyond semantics since it essentially postulates that the last step of the cell cycle is regulated in, and probably by, the following cycle.


Assuntos
Citocinese , Células 3T3 , Animais , Proteínas de Ciclo Celular/deficiência , Proteínas de Ciclo Celular/genética , Proteínas de Ciclo Celular/metabolismo , Proteínas de Ligação a DNA/deficiência , Proteínas de Ligação a DNA/genética , Proteínas de Ligação a DNA/metabolismo , Imunofluorescência , Fase G1 , Células HeLa , Humanos , Proteínas Luminescentes/genética , Proteínas Luminescentes/metabolismo , Camundongos , Camundongos Endogâmicos BALB C , Microscopia de Vídeo , Imagem com Lapso de Tempo , Proteína Vermelha Fluorescente
4.
Mol Biol Cell ; 25(23): 3740-8, 2014 Nov 15.
Artigo em Inglês | MEDLINE | ID: mdl-25232011

RESUMO

Recently the ESCRT-III filamentous complex was designated as the driving force for mammalian cell abscission, that is, fission of the intercellular membrane bridge connecting daughter cells at the end of cytokinesis. However, how ESCRT-III is activated to set on abscission has not been resolved. Here we revisit the role of the upstream canonical ESCRT players ESCRT-II and CHMP6 in abscission. Using high-resolution imaging, we show that these proteins form highly ordered structures at the intercellular bridge during abscission progression. Furthermore, we demonstrate that a truncated version of CHMP6, composed of its first 52 amino acids (CHMP6-N), arrives at the intercellular bridge, blocks abscission, and subsequently leads to cell death. This phenotype is abolished in a mutated version of CHMP6-N designed to prevent CHMP6-N binding to its ESCRT-II partner. Of interest, deleting the first 10 amino acids from CHMP6-N does not interfere with its arrival at the intercellular bridge but almost completely abolishes the abscission failure phenotype. Taken together, these data suggest an active role for ESCRT-II and CHMP6 in ESCRT-mediated abscission. Our work advances the mechanistic understanding of ESCRT-mediated membrane fission in cells and introduces an easily applicable tool for upstream inhibition of the ESCRT pathway in live mammalian cells.


Assuntos
Morte Celular/genética , Citocinese/genética , Complexos Endossomais de Distribuição Requeridos para Transporte/metabolismo , Animais , Cães , Complexos Endossomais de Distribuição Requeridos para Transporte/genética , Endossomos/metabolismo , Endossomos/ultraestrutura , Humanos , Células Madin Darby de Rim Canino , Fusão de Membrana/genética , Ligação Proteica
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