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1.
Plant Physiol ; 187(4): 2763-2784, 2021 12 04.
Article in English | MEDLINE | ID: mdl-34890461

ABSTRACT

Jasmonic acid (JA) and ethylene (ET) signaling modulate plant defense against necrotrophic pathogens in a synergistic and interdependent manner, while JA and ET also have independent roles in certain processes, e.g. in responses to wounding and flooding, respectively. These hormone pathways lead to transcriptional reprogramming, which is a major part of plant immunity and requires the roles of transcription factors. ET response factors are responsible for the transcriptional regulation of JA/ET-responsive defense genes, of which ORA59 functions as a key regulator of this process and has been implicated in the JA-ET crosstalk. We previously demonstrated that Arabidopsis (Arabidopsis thaliana) GDSL LIPASE 1 (GLIP1) depends on ET for gene expression and pathogen resistance. Here, promoter analysis of GLIP1 revealed ERELEE4 as the critical cis-element for ET-responsive GLIP1 expression. In a yeast one-hybrid screening, ORA59 was isolated as a specific transcription factor that binds to the ERELEE4 element, in addition to the well-characterized GCC box. We found that ORA59 regulates JA/ET-responsive genes through direct binding to these elements in gene promoters. Notably, ORA59 exhibited a differential preference for GCC box and ERELEE4, depending on whether ORA59 activation is achieved by JA and ET, respectively. JA and ET induced ORA59 phosphorylation, which was required for both activity and specificity of ORA59. Furthermore, RNA-seq and virus-induced gene silencing analyses led to the identification of ORA59 target genes of distinct functional categories in JA and ET pathways. Our results provide insights into how ORA59 can generate specific patterns of gene expression dynamics through JA and ET hormone pathways.


Subject(s)
Arabidopsis Proteins/genetics , Arabidopsis/genetics , Cyclopentanes/metabolism , Ethylenes/metabolism , Oxylipins/metabolism , Plant Immunity/genetics , Transcription Factors/genetics , Arabidopsis/immunology , Arabidopsis Proteins/metabolism , DNA, Plant/metabolism , DNA-Binding Proteins/genetics , DNA-Binding Proteins/metabolism , Transcription Factors/metabolism
2.
Int J Mol Sci ; 23(5)2022 Feb 28.
Article in English | MEDLINE | ID: mdl-35269832

ABSTRACT

The photosystem II PsbS protein of thylakoid membranes is responsible for regulating the energy-dependent, non-photochemical quenching of excess chlorophyll excited states as a short-term mechanism for protection against high light (HL) stress. However, the role of PsbS protein in long-term HL acclimation processes remains poorly understood. Here we investigate the role of PsbS protein during long-term HL acclimation processes in wild-type (WT) and npq4-1 mutants of Arabidopsis which lack the PsbS protein. During long-term HL illumination, photosystem II photochemical efficiency initially dropped, followed by a recovery of electron transport and photochemical quenching (qL) in WT, but not in npq4-1 mutants. In addition, we observed a reduction in light-harvesting antenna size during HL treatment that ceased after HL treatment in WT, but not in npq4-1 mutants. When plants were adapted to HL, more reactive oxygen species (ROS) were accumulated in npq4-1 mutants compared to WT. Gene expression studies indicated that npq4-1 mutants failed to express genes involved in plastoquinone biosynthesis. These results suggest that the PsbS protein regulates recovery processes such as electron transport and qL during long-term HL acclimation by maintaining plastoquinone biosynthetic gene expression and enhancing ROS homeostasis.


Subject(s)
Arabidopsis Proteins , Arabidopsis , Acclimatization/genetics , Arabidopsis/genetics , Arabidopsis/metabolism , Arabidopsis Proteins/genetics , Arabidopsis Proteins/metabolism , Chlorophyll/metabolism , Light , Light-Harvesting Protein Complexes/genetics , Light-Harvesting Protein Complexes/metabolism , Photosynthesis/genetics , Photosystem II Protein Complex/genetics , Photosystem II Protein Complex/metabolism , Plastoquinone , Reactive Oxygen Species/metabolism
3.
Photosynth Res ; 114(1): 1-13, 2012 Oct.
Article in English | MEDLINE | ID: mdl-22941557

ABSTRACT

The resolution of Photosystem II (PS II) crystals has been improved using isolated PS II from the thermophilic cyanobacterium Thermosynechococcus vulcanus. The new 1.9 Å resolution data have provided detailed information on the structure of the water-oxidizing complex (Umena et al. Nature 473: 55-61, 2011). The atomic level structure of the manganese-calcium cluster is important for understanding the mechanism of water oxidation and to design an efficient catalyst for water oxidation in artificial photosynthetic systems. Here, we have briefly reviewed our knowledge of the structure and function of the cluster.


Subject(s)
Calcium/chemistry , Cyanobacteria/metabolism , Manganese/chemistry , Photosynthetic Reaction Center Complex Proteins/chemistry , Photosystem II Protein Complex/chemistry , Water/chemistry , Crystallography, X-Ray , Hydrogen Bonding , Models, Chemical , Oxidation-Reduction , Oxides , Oxygen/chemistry
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