9 research outputs found

    对氨基苯甲酸在拟南芥根生长发育中对生长素运输的调控

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    为探究对氨基苯甲酸(PABA)影响拟南芥(Arabidopsis thaliana)根部生长发育的作用机制,以野生型和DR5∷GUS转基因拟南芥为实验材料,研究了PABA外源处理对根系形态结构和生长素运输的影响.结果表明:200μmol/L PABA可以明显抑制拟南芥幼苗主根生长并促进侧根和根毛的发育.PABA可增强生长素类似物2,4-D对幼苗主根生长的抑制作用和对根毛伸长的促进作用;相反,PABA可在一定程度上减弱生长素运输抑制剂NPA对幼苗主根和根毛生长发育的抑制作用.此外,PABA可诱导拟南芥根尖生长素的积累以及生长素极性运输相关基因PIN1、PIN3和AUX1的表达.综上所述,PABA可调节根部生长素运输和分布,在拟南芥根生长发育过程中起重要作用.国家自然科学基金(30571259

    对氨基苯甲酸在拟南芥根生长发育中对生长素运输的调控

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    为探究对氨基苯甲酸(PABA)影响拟南芥根部生长发育的作用机制,通过以野生型拟南芥和DR5::GUS转基因拟南芥为实验材料,研究了PABA外源处理对根系形态结构和生长素的运输和分布的影响。结果表明:200 μmol/L PABA可以明显抑制拟南芥幼苗主根生长,并促进侧根和根毛的发育。PABA可增强生长素类似物2,4-D对幼苗主根生长抑制的影响,促进根毛伸长;相反,PABA可在一定程度上恢复生长素运输抑制剂NPA对幼苗主根和根毛生长发育的抑制作用。此外,PABA可以诱导拟南芥根尖生长素的积累,并影响生长素极性运输相关基因PIN1、PIN3和AUX1的表达。综上所述,PABA可调节根部生长素运输和分布,在拟南芥根生长发育过程中起重要作用。国家自然科学基金(30571259

    Quantitative nature of Arabidopsis responses during compatible and incompatible interactions with the bacterial pathogen Pseudomonas syringae

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    We performed large-scale mRNA expression profiling using an Affymetrix GeneChip to study Arabidopsis responses to the bacterial pathogen Pseudomonas syringae. The interactions were compatible (virulent bacteria) or incompatible (avirulent bacteria), including a nonhost interaction and interactions mediated by two different avirulence gene-resistance (R) gene combinations. Approximately 2000 of the similar to8000 genes monitored showed reproducible significant expression level changes in at least one of the interactions. Analysis of biological variation suggested that the system behavior of the plant response in an incompatible interaction was robust but that of a compatible interaction was not. A large part of the difference between incompatible and compatible interactions can be explained quantitatively. Despite high similarity between responses mediated by the R genes RPS2 and RPM1 in wild-type plants, RPS2-mediated responses were strongly suppressed by the ndr1 mutation and the NahG transgene, whereas RPM1-mediated responses were not. This finding is consistent with the resistance phenotypes of these plants. We propose a simple quantitative model with a saturating response curve that approximates the overall behavior of this plant-pathogen system

    基因编辑的法律与伦理问题

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    跨域同仁聚焦公共话题,本辑围绕基因编辑的法律与伦理议题,各位学者基于不同的立场与视角做出不同的评议。为尊重言论,兹实录对话,仅做最低限度的技术处理

    含灰气体激波沿平壁传播时诱导的边界层流动

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    研究含灰气体激波沿平直壁面传播过程中在壁面附近形成的层流边界层流动.依照双边连续介质双向耦合模型处理含灰气体激波的波后流动及其诱导的边界层问题,控制方程采用有限差分方法数值求解,给出了激波下游两相流场特性并考虑了含灰气体激波的松弛结构对边界层流动的影响

    Direct delivery of bacterial avirulence proteins into resistant Arabidopsis protoplasts leads to hypersensitive cell death

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    Many bacterial avirulence (Avr) proteins, including the Pseudomonas syringae proteins, AvrRpt2 and AvrB, appear to be recognized inside the host plant cell by resistance mechanisms mediated by the cognate resistance (R ) genes. It is thought that Avr proteins are either delivered directly into the host cell via the bacterial type III secretion system (TTSS) or taken up by the plant cell following secretion into the apoplast through the TTSS. Recently, it was shown that the Xanthomonas campestris AvrBs2 protein can be delivered directly into the host plant cell by the TTSS. However, it is not known whether other type III effectors of phytopathogens behave similarly. Here, using a novel protein transfection method, we demonstrate that AvrRpt2 and AvrB must enter the plant cell to be recognized by R gene-mediated mechanisms. First, we established a hypersensitive cell death assay for protoplasts using the membrane-impermeable, nuclear-staining dye, YO-PRO-1, and transgenic Arabidopsis plants that carry an inducible avrRpt2 gene. Second, we transfected E. coli -produced AvrRpt2 or AvrB proteins into Arabidopsis protoplasts using a protein transfection kit based on the carrier peptide Pep-1, and demonstrated that hypersensitive cell death occurs in a gene-for-gene-specific manner. In contrast, these Avr proteins failed to elicit hypersensitive cell death when they were applied to protoplasts without the carrier peptide. We conclude that our preparations of E. coli -produced AvrRpt2 and AvrB are active, that AvrRpt2 and AvrB must be delivered into the plant cell to be recognized, and that a method based on a carrier peptide can be used to introduce proteins into plant cells

    Mutational analysis of the Arabidopsis nucleotide binding site-leucine-rich repeat resistance gene RPS2

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    Disease resistance proteins containing a nucleotide binding site (NBS) and a leucine-rich repeat (LRR) region compose the largest class of disease resistance proteins. These so-called NBS-LRR proteins confer resistance against a wide variety of phytopathogens. To help elucidate the mechanism by which NBS-LRR proteins recognize and transmit pathogen-derived signals, we analyzed mutant versions of the Arabidopsis NBS-LRR protein RPS2. The RPS2 gene confers resistance against Pseudomonas syringae strains carrying the avirulence gene avrRpt2. The activity of RPS2 derivatives in response to AvrRpt2 was measured by using a functional transient expression assay or by expressing the mutant proteins in transgenic plants. Directed mutagenesis revealed that the NBS and an N-terminal leucine zipper (LZ) motif were critical for RPS2 function. Mutations near the N terminus, including an LZ mutation, resulted in proteins that exhibited a dominant negative effect on wild-type RPS2. Scanning the RPS2 molecule with a small in-frame internal deletion demonstrated that RPS2 does not have a large dispensable region. Overexpression of RPS2 in the transient assay in the absence of avrRpt2! also led to an apparent resistant response, presumably a consequence of a low basal activity of RPS2. The NBS and LZ were essential for this overdose effect, whereas the entire LRR was dispensable. RPSP interaction with a 75-kD protein (p75) required an N-terminal portion of RPSP that is smaller than the region required for the overdose effect. These findings illuminate the pathogen recognition mechanisms common among NBS-LRR proteins

    Regulation of phytochrome B nuclear localization through light-dependent unmasking of nuclear-localization signals

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    Phytochromes are red and far-red photoreceptors that regulate plant growth and development in response to environmental light cues. Phytochromes exist in two photo-interconvertible conformational states: an inactive Pr form and an active Pfr form. The alteration of phytochromes' subcellular location functions as a major regulatory mechanism of their biological activities [1-3]. Whereas phytochromes in the Pr form localize in the cytoplasm, phytochromes in the Pfr form accumulate in the nucleus, where they interact with transcription factors to regulate gene expression [1, 4]. The molecular details of the regulation of phytochrome translocation by light are poorly understood. Using Arabidopsis phyB as a model, we demonstrate that the C-terminal PAS-related domain (PRD) is both necessary and sufficient for phyB nuclear import and that the entire C terminus is required for nuclear-body (NB) localization. We also show that phyB's N-terminal bilin lyase domain (BILD) and PHY domain interact directly with the PRD in a light-dependent manner. In vivo localization studies indicate that BLD-PHY is sufficient to regulate phyB's nuclear accumulation. For phyB nuclear localization, our results suggest a molecular mechanism in which the nuclear-localization signal in the PRD is masked by interactions with phyB's chromophore-attachment domains and unmasked by light-dependent conformational changes

    A new class of transcription factors mediates brassinosteroid-regulated gene expression in Arabidopsis

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    Brassinosteroids (BRs) signal through a plasma membrane-localized receptor kinase to regulate plant growth and development. We showed previously that a novel protein, BES1, accumulates in the nucleus in response to BRs, where it plays a role in BR-regulated gene expression; however, the mechanism by which BES1 regulates gene expression is unknown. In this study, we dissect BES1 subdomains and establish that BES1 is a transcription factor that binds to and activates BR target gene promoters both in vitro and in vivo. BES1 interacts with a basic helix-loop-helix protein, BIM1, to synergistically bind to E box (CANNTG) sequences present in many BR-induced promoters. Loss-of-function and gain-of-function mutants of BIM1 and its close family members display BR response phenotypes. Thus, BES1 defines a new class of plant-specific transcription factors that cooperate with transcription factors such as BIM1 to regulate BR-induced genes
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