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1.
Article in English | MEDLINE | ID: mdl-36078388

ABSTRACT

Boron overabundance in aquatic environment raises severe concerns about the environment and human health because it is toxic to various crops and induces many human and animal diseases with long-term consequences. In response to the boron pollution of water resources and the difficulty of eliminating boron from water for production and living purposes, this article summarizes the progress in research on boron removal technology, addressing the following aspects: (1) the reasons for the difficulty of removing boron from water (boron chemistry); (2) ecological/biological toxicity and established regulations; (3) analysis of different existing processes (membrane processes, resin, adsorption, chemical precipitation, (electric) coagulation, extraction, and combined methods) in terms of their mechanisms, effectiveness, and limitations; (4) prospects for future studies and possible improvements in applicability and recyclability. The focus of this paper is thus to provide a comprehensive summary of reported deboronation processes to date, which will definitely identify directions for the development of boron removal technology in the future.


Subject(s)
Water Pollutants, Chemical , Water Purification , Adsorption , Boron/analysis , Humans , Technology , Water , Water Pollutants, Chemical/analysis , Water Purification/methods
2.
Environ Microbiol ; 23(2): 791-809, 2021 02.
Article in English | MEDLINE | ID: mdl-32564502

ABSTRACT

The type 2A (PP2A) and type 2A-like (PP4 and PP6) serine/threonine phosphatases participate in a variety of cellular processes, such as cell cycle progression, signal transduction and apoptosis. Previously, we reported that the PP6 catalytic subunit MoPpe1, which interacts with and is suppressed by type 2A associated protein of 42 kDa (MoTap42), an essential protein involved in the target of rapamycin (TOR) signalling pathway, has important roles in development, virulence and activation of the cell wall integrity (CWI) pathway in the rice blast fungus Magnaporthe oryzae. Here, we show that Tap42-interacting protein 41 (MoTip41) mediates crosstalk between the TOR and CWI signalling pathways; and participates in the TOR pathway via interaction with MoPpe1, but not MoTap42. The deletion of MoTIP41 resulted in disruption of CWI signalling, autophagy, vegetative growth, appressorium function and plant infection, as well as increased sensitivity to rapamycin. Further investigation revealed that MoTip41 modulates activation of the CWI pathway in response to infection by interfering with the interaction between MoTap42 and MoPpe1. These findings enhance our understanding of how crosstalk between TOR and CWI signalling modulates the development and pathogenicity of M. oryzae.


Subject(s)
Ascomycota/metabolism , Cell Wall/metabolism , Phosphoprotein Phosphatases/metabolism , Sirolimus/metabolism , Ascomycota/pathogenicity , Autophagy , Cell Cycle Proteins/metabolism , Fungal Proteins/metabolism , Intracellular Signaling Peptides and Proteins/metabolism , Oryza/microbiology , Phosphoprotein Phosphatases/genetics , Plant Diseases/microbiology , Signal Transduction/physiology , Virulence
3.
Elife ; 92020 12 04.
Article in English | MEDLINE | ID: mdl-33275098

ABSTRACT

The production of reactive oxygen species (ROS) is a ubiquitous defense response in plants. Adapted pathogens evolved mechanisms to counteract the deleterious effects of host-derived ROS and promote infection. How plant pathogens regulate this elaborate response against ROS burst remains unclear. Using the rice blast fungus Magnaporthe oryzae, we uncovered a self-balancing circuit controlling response to ROS in planta and virulence. During infection, ROS induces phosphorylation of the high osmolarity glycerol pathway kinase MoOsm1 and its nuclear translocation. There, MoOsm1 phosphorylates transcription factor MoAtf1 and dissociates MoAtf1-MoTup1 complex. This releases MoTup1-mediated transcriptional repression on oxidoreduction-pathway genes and activates the transcription of MoPtp1/2 protein phosphatases. In turn, MoPtp1/2 dephosphorylate MoOsm1, restoring the circuit to its initial state. Balanced interactions among proteins centered on MoOsm1 provide a means to counter host-derived ROS. Our findings thereby reveal new insights into how M. oryzae utilizes a phosphor-regulatory circuitry to face plant immunity during infection.


Subject(s)
Ascomycota/enzymology , Fungal Proteins/metabolism , Gene Expression Regulation, Enzymologic/physiology , Gene Expression Regulation, Fungal/physiology , Oryza/microbiology , Reactive Oxygen Species , Adaptation, Physiological , Ascomycota/genetics , Fungal Proteins/genetics , Oryza/metabolism , Oxidation-Reduction , Oxidative Stress/physiology , Phosphorylation , Plant Diseases/microbiology
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