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Exploring soil microbial and plant parasitic nematode communities involved in the apple replant disease complex in Nova Scotia
Abstract Apple replant disease (ARD) is incited by a complex of causal agents including various fungi, oomycetes, and plant parasitic nematodes. These causal agents can differ significantly in abundance between orchard sites within a geographic region. Knowledge of the specific etiology of ARD is required in order to develop commercially viable soil management strategies to combat specific/individual components of the pathogen complex. In this study, we analyzed soil from six ARD affected orchard sites to assess the presence and composition of fungal, bacterial and oomycetes communities, as well as the prevalence of plant parasitic nematodes. Five fungal, and 17 bacterial classes were differentially represented in the soil microbiomes across the different locations. Mortierellomycetes was the most abundant fungal taxa represented followed by Sordariomycetes. Mortierella exigua , a fungal endophyte, was the most abundant fungal amplicon sequence variant (ASV) in the core microbiome. Among bacteria, Proteobacteria was the most prevalent phylum identified in these orchard soils. Several potential phytopathogenic fungi associated with ARD, as well as endophytes including Fusarium oxysporum , F. solani , Nectria ramulariae , Ilyonectria robusta and Nectriaceae , were identified in ARD soils. Among oomycetes, Pythium attrantheridium ( Globisporangium attrantheridium ), and P. irregulare ( Globisporangium irregulare ) were the most abundant taxa. Additionally, six different groups of plant-parasitic nematodes were found across the ARD orchard soils. Root-lesion nematodes, Pratylenchus spp., which are commonly associated with ARD, were identified in all orchard soils at population densities range from 12 to 33/100 cm 3 soil. This research enhances our understanding of the ARD pathogen complex and provide important insights for developing alternative disease management strategies in the apple industry.
How to get the best night’s sleep: what the science says
High power, dual SWIR-MIR OPCPA source for high-order harmonics generation
Direct shoot regeneration and gene expression profiling for optimized picroside-I biosynthesis in Picrorhiza Kurroa
Early efforts to understand the processes underlying bird migration
The mediating effect of serum total testosterone in the association between the ZJU index and PCOS
Probing the heterogeneous nature of LiF in solid–electrolyte interphases
Assessing Teucrium polium L. from chemical profiling to antioxidant, anticancer, α-amylase, and lipase activities
AI tools could reduce the appeal of predatory journals
Performance and suitability of wastewater based-surveillance for SARS-CoV-2 RNA in public schools
Rare skeletal condition caused by enzyme’s failure to rescue a catalytic cycle
Transient APC/C inactivation by mTOR boosts glycolysis during cell cycle entry
Abstract Mammalian cells entering the cell cycle favour glycolysis to rapidly generate ATP and produce the biosynthetic intermediates that are required for rapid biomass accumulation1. Simultaneously, the ubiquitin-ligase anaphase-promoting complex/cyclosome and its coactivator CDH1 (APC/CCDH1) remains active, allowing origin licensing and blocking premature DNA replication. Paradoxically, glycolysis is reduced by APC/CCDH1 through the degradation of key glycolytic enzymes2, raising the question of how cells coordinate these mutually exclusive events to ensure proper cell division. Here we show that cells resolve this paradox by transiently inactivating the APC/C during cell cycle entry, which allows a transient metabolic shift favouring glycolysis. After mitogen stimulation, rapid mTOR-mediated phosphorylation of the APC/C adapter protein CDH1 at the amino terminus causes it to partially dissociate from the APC/C. This partial inactivation of the APC/C leads to the accumulation of PFKFB3, a rate-limiting enzyme for glycolysis, promoting a metabolic shift towards glycolysis. Delayed accumulation of phosphatase activity later removes CDH1 phosphorylation, restoring full APC/C activity, and shifting cells back to favouring oxidative phosphorylation. Thus, cells coordinate the simultaneous demands of cell cycle progression and metabolism through an incoherent feedforward loop, which transiently inhibits APC/C activity to generate a pulse of glycolysis that is required for mammalian cell cycle entry.
The recipe similarity network: a new algorithm to extract relevant information from cookbooks
India and Pakistan share flood risks and must combine solutions
Acoustic water display
Tuning of dynamic solvation structures via click chemistry for PEO-based solid polymer electrolytes
Abstract The Li+-transport mechanisms in both solid polymer electrolytes (SPEs) and liquid electrolytes (LEs) are fundamentally governed by solvation dynamics, requiring an optimal balance between continuous coordination and moderate binding strength. Poly(ethylene oxide) (PEO) is a classic SPE matrix that leverages its –CH2–CH2–O– (EO) segments to provide continuous oxygen coordination for Li+ transport via amorphous regions. While continuous EO segments facilitate the intra-chain Li+-transport, their strong multidentate solvation of Li+ through a chelate effect – each Li+ chelates with 4–6 ethylene oxide (EO) units – significantly hinders the inter-chain Li+ mobility. This effect creates rigid solvation cages that both immobilize Li+ and resist modification by alternative moieties (e.g. carbonate or nitrile groups), resulting in poor room-temperature ionic conductivity (σ) and low Li+ transference number (t Li+). To address these challenges, we developed a series of precise Li+-transport models (LTMs) through click chemistry, strategically combining acrylate-PEG and acrylonitrile to engineer balanced interactions between multidentate (EO) and monodentate (C = O, C ≡ N) coordination sites. This design achieved synergistic enhancement of both inter- and intra-chain transport pathways, demonstrated by significantly improved performance with σ = 6.40 × 10− 5 S/cm and t Li+ = 0.44 at 25 °C. This approach permits tailored control of dynamic solvation structures, offering new opportunities to enhance Li+ transport in PEO-based solid polymer electrolytes.