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1.
Plant Cell Rep ; 43(5): 123, 2024 Apr 20.
Article in English | MEDLINE | ID: mdl-38642148

ABSTRACT

KEY MESSAGE: CitCAT1 and CitCAT2 were cloned and highly expressed in mature leaves. High temperatures up-regulated CitCAT1 expression, while low temperatures and Diversispora versiformis up-regulated CitCAT2 expression, maintaining a low oxidative damage. Catalase (CAT), a tetrameric heme-containing enzyme, removes hydrogen peroxide (H2O2) to maintain low oxidative damage in plants exposed to environmental stress. This study aimed to clone CAT genes from Citrus sinensis cv. "Oita 4" and analyze their expression patterns in response to environmental stress, exogenous abscisic acid (ABA), and arbuscular mycorrhizal fungal inoculation. Two CAT genes, CitCAT1 (NCBI accession: PP067858) and CitCAT2 (NCBI accession: PP061394) were cloned, and the open reading frames of their proteins were 1479 bp and 1539 bp, respectively, each encoding 492 and 512 amino acids predicted to be localized in the peroxisome, with CitCAT1 being a stable hydrophilic protein and CitCAT2 being an unstable hydrophilic protein. The similarity of their amino acid sequences reached 83.24%, and the two genes were distantly related. Both genes were expressed in stems, leaves, flowers, and fruits, accompanied by the highest expression in mature leaves. In addition, CitCAT1 expression was mainly up-regulated by high temperatures (37 °C), exogenous ABA, and PEG stress within a short period of time, whereas CitCAT2 expression was up-regulated by exogenous ABA and low-temperature (4 °C) stress. Low temperatures (0 °C) for 12 h just up-regulated CitCAT2 expression in Diversispora versiformis-inoculated plants, and D. versiformis inoculation up-regulated CitCAT2 expression, along with lower hydrogen peroxide and malondialdehyde levels in mycorrhizal plants at low temperatures. It is concluded that CitCAT2 has an important role in resistance to low temperatures as well as mycorrhizal enhancement of host resistance to low temperatures.


Subject(s)
Fungi , Mycorrhizae , Mycorrhizae/physiology , Hydrogen Peroxide , Stress, Physiological/genetics , Cloning, Molecular
2.
J Fungi (Basel) ; 8(8)2022 Jul 29.
Article in English | MEDLINE | ID: mdl-36012789

ABSTRACT

Plant roots can be colonized by many symbiotic fungi, whereas it is unclear whether and how symbiotic fungi including arbuscular mycorrhizal fungi and endophytic fungi promote phosphorus (P) uptake in Camellia oleifera plants. The objective of the present study was to analyze the effect of inoculation with a culturable endophytic fungus (Piriformospora indica), three arbuscular mycorrhizal fungi (Funneliformis mosseae, Diversispora versiformis, and Rhizophagus intraradices), and mixture of F. mosseae, D. versiformis and R. intraradices on plant growth, root architecture, soil Olsen-P, soil phosphatase activities, leaf and root P concentrations, and phosphate transporter gene expressions, in order to explore the potential and mechanism of these symbiotic fungi on P acquisition. All the symbiotic fungi colonized roots of C. oleifera after 16 weeks, with P. indica showing the best effect on fungal colonization. All the symbiotic fungi significantly increased acid, neutral, and total phosphatase activities in the soil, accompanied with an elevation of soil Olsen-P, of which P. indica presented the best effect. All symbiotic fungal treatments, except D. versiformis, significantly promoted plant growth, coupled with an increase in root total length, area, and volume. Symbiotic fungi almost up-regulated root CoPHO1-3 expressions as well as leaf CoPHO1-1, CoPHO1-3, and CoPHT1;4 expressions. Correlation analysis showed that P concentrations in leaves and roots were significantly positively correlated with root morphological variables (length, volume, and surface area) and soil acid, neutral and total phosphatase activities. It is concluded that symbiotic fungi, especially P. indica, played an important role in P uptake of C. oleifera plants through regulating root architecture, part plant phosphate transporter gene expressions and soil phosphatase activities.

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