384 research outputs found

    The phagocytosis oxidase/Bem1p domain-containing protein PB1CP negatively regulates the NADPH oxidase RBOHD in plant immunity

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    Perception of pathogen-associated molecular patterns (PAMPs) by surface-localized pattern recognition receptors activates RESPIRATORY BURST OXIDASE HOMOLOG D (RBOHD) through direct phosphorylation by BOTRYTIS-INDUCED KINASE 1 (BIK1) and induces the production of reactive oxygen species (ROS). RBOHD activity must be tightly controlled to avoid the detrimental effects of ROS, but little is known about RBOHD downregulation. To understand the regulation of RBOHD, we used co-immunoprecipitation of RBOHD with mass spectrometry analysis and identified PHAGOCYTOSIS OXIDASE/BEM1P (PB1) DOMAIN-CONTAINING PROTEIN (PB1CP). PB1CP negatively regulates RBOHD and the resistance against the fungal pathogen Colletotrichum higginsianum. PB1CP competes with BIK1 for binding to RBOHD in vitro. Furthermore, PAMP treatment enhances the PB1CP-RBOHD interaction, thereby leading to the dissociation of phosphorylated BIK1 from RBOHD in vivo. PB1CP localizes at the cell periphery and PAMP treatment induces relocalization of PB1CP and RBOHD to the same small endomembrane compartments. Additionally, overexpression of PB1CP in Arabidopsis leads to a reduction in the abundance of RBOHD protein, suggesting the possible involvement of PB1CP in RBOHD endocytosis. We found PB1CP, a novel negative regulator of RBOHD, and revealed its possible regulatory mechanisms involving the removal of phosphorylated BIK1 from RBOHD and the promotion of RBOHD endocytosis

    Anti-rat myoglobin antisera in the immunocytochemical diagnosis of rhabdomyosarcomas of rats. Vet

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    Abstract. Anti-rat myoglobin (Mb) was prepared and used in the avidin-biotin-peroxidase complex (ABC) method on paraffin-embedded sections of nine soft tissue tumors (including two rhabdomyosarcomas) of rats. Distribution and nature of the reactive substance to Mb antiserum were compared to those of desmin antiserum. Rat Mb was isolated from the skeletal muscle; monospecificity of the rat antiserum was confirmed by the immunoblotting procedures. The Mb antiserum reacted specifically to normal and neoplastic striated muscle cells. Mb-staining reactions were present diffusely in the cytoplasm, while desmin-staining substances were localized at Z-bands or were diffuse in the cytoplasm as separated aggregates. Reaction to the Mb serum was also detected in cells of thick portions of Henle's loop and distal convoluted tubules

    Performance optimisation of the MAC protocol with multiple contention slots in MIMO ad hoc networks

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    The multiple-input multiple-output (MIMO) technique can be used to improve the performance of ad hoc networks. Various medium access control (MAC) protocols with multiple contention slots have been proposed to exploit spatial multiplexing for increasing the transport throughput of MIMO ad hoc networks. However, the existence of multiple request-to-send/clear-to-send (RTS/CTS) contention slots represents a severe overhead that limits the improvement on transport throughput achieved by spatial multiplexing. In addition, when the number of contention slots is fixed, the efficiency of RTS/CTS contention is affected by the transmitting power of network nodes. In this study, a joint optimisation scheme on both transmitting power and contention slots number for maximising the transport throughput is presented. This includes the establishment of an analytical model of a simplified MAC protocol with multiple contention slots, the derivation of transport throughput as a function of both transmitting power and the number of contention slots, and the optimisation process based on the transport throughput formula derived. The analytical results obtained, verified by simulation, show that much higher transport throughput can be achieved using the joint optimisation scheme proposed, compared with the non-optimised cases and the results previously reported

    The effect of environmental heterogeneity on RPW8-mediated resistance to powdery mildews in Arabidopsis thaliana

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    Background and Aims: The biotic and abiotic environment of interacting hosts and parasites may vary considerably over small spatial and temporal scales. It is essential to understand how different environments affect host disease resistance because this determines frequency of disease and, importantly, heterogeneous environments can retard direct selection and potentially maintain genetic variation for resistance in natural populations. Methods: The effect of different temperatures and soil nutrient conditions on the outcome of infection by a pathogen was quantified in Arabidopsis thaliana. Expression levels of a gene conferring resistance to powdery mildews, RPW8, were compared with levels of disease to test a possible mechanism behind variation in resistance. Key Results: Most host genotypes changed from susceptible to resistant across environments with the ranking of genotypes differing between treatments. Transcription levels of RPW8 increased after infection and varied between environments, but there was no tight association between transcription and resistance levels. Conclusions: There is a strong potential for a heterogeneous environment to change the resistance capacity of A. thaliana genotypes and hence the direction and magnitude of selection in the presence of the pathogen. Possible causative links between resistance gene expression and disease resistance are discussed in light of the present results on RPW8

    The phagocytosis oxidase/Bem1p domain-containing protein PB1CP negatively regulates the NADPH oxidase RBOHD in plant immunity

    Get PDF
    Perception of pathogen-associated molecular patterns (PAMPs) by surface-localized pattern recognition receptors activates RESPIRATORY BURST OXIDASE HOMOLOG D (RBOHD) through direct phosphorylation by BOTRYTIS-INDUCED KINASE 1 (BIK1) and induces the production of reactive oxygen species (ROS). RBOHD activity must be tightly controlled to avoid the detrimental effects of ROS, but little is known about RBOHD downregulation. To understand the regulation of RBOHD, we used co-immunoprecipitation of RBOHD with mass spectrometry analysis and identified PHAGOCYTOSIS OXIDASE/BEM1P (PB1) DOMAIN-CONTAINING PROTEIN (PB1CP). PB1CP negatively regulates RBOHD and the resistance against the fungal pathogen Colletotrichum higginsianum. PB1CP competes with BIK1 for binding to RBOHD in vitro. Furthermore, PAMP treatment enhances the PB1CP-RBOHD interaction, thereby leading to the dissociation of phosphorylated BIK1 from RBOHD in vivo. PB1CP localizes at the cell periphery and PAMP treatment induces relocalization of PB1CP and RBOHD to the same small endomembrane compartments. Additionally, overexpression of PB1CP in Arabidopsis leads to a reduction in the abundance of RBOHD protein, suggesting the possible involvement of PB1CP in RBOHD endocytosis. We found PB1CP, a novel negative regulator of RBOHD, and revealed its possible regulatory mechanisms involving the removal of phosphorylated BIK1 from RBOHD and the promotion of RBOHD endocytosis
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