@article{MTMT:31097090,
	title = {Dehydrin ERD14 activates glutathione transferase Phi9 in Arabidopsis thaliana under osmotic stress.},
	url = {https://m2.mtmt.hu/api/publication/31097090},
	author = {Nguyen, Phuong N and Tossounian, Maria-Armineh and Kovacs, Denes S and Thu, Tran T and Stijlemans, Benoit and Vertommen, Didier and Pauwels, Jarne and Gevaert, Kris and Angenon, Geert and Messens, Joris and Tompa, Péter},
	doi = {10.1016/j.bbagen.2019.129506},
	journal-iso = {BBA-GEN SUBJECTS},
	journal = {BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS},
	volume = {1864},
	unique-id = {31097090},
	issn = {0304-4165},
	abstract = {Fully intrinsically disordered plant dehydrin ERD14 can protect enzymes via its chaperone-like activity, but it was not formally linked with enzymes of the plant redox system yet. This is of particular interest, as the level of H2O2 in Arabidopsis plants increases during osmotic stress, which can be counteracted by overexpression of ERD14.The proteomic mass-spectrometry analysis of stressed plants was performed to find the candidates affected by ERD14. With cross-linking, microscale thermophoresis, and active-site titration kinetics, the interaction and influence of ERD14 on the function of two target proteins: glutathione transferase Phi9 and catalase was examined.Under osmotic stress, redox enzymes, specifically the glutathione transferase Phi enzymes, are upregulated. Using microscale thermophoresis, we showed that ERD14 directly interacts with GSTF9 with a KD of ~25 μM. ERD14 activates the inactive GSTF9 molecules, protects GSTF9 from oxidation, and can also increases the activity of the enzyme. Aside from GSTF9, we found that ERD14 can also interact with catalase, an important cellular H2O2 scavenging enzyme, with a KD of ~0.13 μM, and protects it from dehydration-induced loss of activity.We propose that fully intrinsically disordered dehydrin ERD14 might protect and even activate redox enzymes, helping plants to survive oxidative stress under dehydration conditions.ERD14 has a direct effect on the activity of redox enzymes.},
	keywords = {enzyme activation; hydrogen peroxide; chaperone; Intrinsically disordered protein; Active site titration; Oxidative stress},
	year = {2020},
	eissn = {1872-8006}
}

@article{MTMT:31471519,
	title = {Ethylene: A Master Regulator of Salinity Stress Tolerance in Plants},
	url = {https://m2.mtmt.hu/api/publication/31471519},
	author = {Riyazuddin, Riyazuddin and Verma, Radhika and Singh, Kalpita and Nisha, Nisha and Keisham, Monika and Bhati, Kaushal Kumar and Kim, Sun Tae and Gupta, Ravi},
	doi = {10.3390/biom10060959},
	journal-iso = {BIOMOLECULES},
	journal = {BIOMOLECULES},
	volume = {10},
	unique-id = {31471519},
	issn = {2218-273X},
	abstract = {Salinity stress is one of the major threats to agricultural productivity across the globe. Research in the past three decades, therefore, has focused on analyzing the effects of salinity stress on the plants. Evidence gathered over the years supports the role of ethylene as a key regulator of salinity stress tolerance in plants. This gaseous plant hormone regulates many vital cellular processes starting from seed germination to photosynthesis for maintaining the plants' growth and yield under salinity stress. Ethylene modulates salinity stress responses largely via maintaining the homeostasis of Na+/K+, nutrients, and reactive oxygen species (ROS) by inducing antioxidant defense in addition to elevating the assimilation of nitrates and sulfates. Moreover, a cross-talk of ethylene signaling with other phytohormones has also been observed, which collectively regulate the salinity stress responses in plants. The present review provides a comprehensive update on the prospects of ethylene signaling and its cross-talk with other phytohormones to regulate salinity stress tolerance in plants.},
	keywords = {antioxidants; PHOTOSYNTHESIS; ETHYLENE; Programmed cell death; SALINITY STRESS; ROS; Seed germination; Hormone cross-talk},
	year = {2020},
	eissn = {2218-273X},
	orcid-numbers = {Bhati, Kaushal Kumar/0000-0002-2322-0431}
}

@article{MTMT:30779044,
	title = {Overexpression of the Arabidopsis glutathione peroxidase-like 5 gene (AtGPXL5) resulted in altered plant development and redox status},
	url = {https://m2.mtmt.hu/api/publication/30779044},
	author = {Riyazuddin, Riyazuddin and Bela, Krisztina and Horváth, Edit and Rigó, Gábor and Gallé, Ágnes and Szabados, László and Fehér, Attila and Csiszár, Jolán},
	doi = {10.1016/j.envexpbot.2019.103849},
	journal-iso = {ENVIRON EXP BOT},
	journal = {ENVIRONMENTAL AND EXPERIMENTAL BOTANY},
	volume = {167},
	unique-id = {30779044},
	issn = {0098-8472},
	abstract = {Plant's glutathione peroxidase-like (GPXL) enzymes are thiol-based peroxidases catalysing the reduction of H2O2 or hydroperoxides to water or alcohols using reduced glutathione (GSH) or thioredoxin as an electron donor. Arabidopsis thaliana possess eight isoenzymes having different roles in redox-dependent processes. AtGPXL5 is a poorly known plasma membrane associated enzyme. We have investigated the role of AtGPXL5 in development and responses to salt using AtGPXL5-overexpressing lines (OX-AtGPXL5) and Atgpxl5 mutants. Constitutive overexpression of AtGPXL5 increased the transcription of the gene by 17–24 times in 6-week-old plants. In OX-AtGPXL5 plants, the activity of glutathione peroxidase, thioredoxin peroxidase and most of the main antioxidant enzymes were like in the wild type Col-0, but the amount of GSH was increased, thus the redox potential became more negative compared to the wild type. The well-preserved germination rate, seedling growth and chlorophyll content of the OX-AtGPXL5 seedlings in the presence of 100 mM NaCl indicated the increased salt tolerance of AtGPXL5-overexpressing plants. In agreement, the Atgpxl5 knockdown mutants had enhanced salt stress sensitivity in comparison to the wild type. Our results indicate that AtGPXL5 may have function in the fine-tuning of ROS levels and redox status during salt stress. © 2019 Elsevier B.V.},
	keywords = {ARABIDOPSIS; SALT STRESS; Reactive oxygen species; Arabidopsis thaliana; Arabidopsis thaliana; Redox homeostasis; Antioxidant mechanisms; Glutathione peroxidase-like},
	year = {2019},
	eissn = {1873-7307},
	orcid-numbers = {Bela, Krisztina/0000-0003-0124-4552; Horváth, Edit/0000-0002-7501-2060; Gallé, Ágnes/0000-0002-8347-8469; Fehér, Attila/0000-0002-4183-3696; Csiszár, Jolán/0000-0001-7250-3000}
}