TY - JOUR AU - Gierczik, Krisztián AU - Vukusic, T AU - Kovács, László AU - Székely, András AU - Szalai, Gabriella AU - Milosevic, S AU - Kocsy, Gábor AU - Kutasi, Kinga AU - Galiba, Gábor TI - Plasma-activated water to improve the stress tolerance of barley JF - PLASMA PROCESSES AND POLYMERS J2 - PLASMA PROCESS POLYM VL - 17 PY - 2020 IS - 3 PG - 16 SN - 1612-8850 DO - 10.1002/ppap.201900123 UR - https://m2.mtmt.hu/api/publication/31128306 ID - 31128306 N1 - Export Date: 29 February 2024 LA - English DB - MTMT ER - TY - JOUR AU - Salamo Perez, Immaculada AU - Papdi, Csaba AU - Rigó, Gábor AU - Zsigmond, Laura AU - Vilela, B AU - Lumbreras, V AU - Nagy, István AU - Horváth, Balázs AU - Domoki, Mónika AU - Darula, Zsuzsanna AU - Medzihradszky F., Katalin AU - Koncz, Csaba AU - Bogre, L AU - Szabados, László TI - The Heat Shock Factor A4A Confers SaltTolerance and Is Regulated by OxidativeStress and the Mitogen-Activated ProteinKinases MPK3 and MPK6 JF - PLANT PHYSIOLOGY J2 - PLANT PHYSIOL VL - 165 PY - 2014 IS - 1 SP - 319 EP - 334 PG - 16 SN - 0032-0889 DO - 10.1104/pp.114.237891 UR - https://m2.mtmt.hu/api/publication/2570455 ID - 2570455 N1 - open access Megjegyzés-24204835 N1 Molecular Sequence Numbers: GENBANK: GSE40735 Megjegyzés-24205144 N1 Molecular Sequence Numbers: GENBANK: GSE40735 WoS:hiba:000335906300025 2020-08-29 12:59 cím nem egyezik AB - Heat-shock factors (HSFs) are principal regulators of plant responses to several abiotic stresses. Here we show that estradiol-dependent induction of HSFA4A confers enhanced tolerance to salt and oxidative agents, whereas inactivation of HSFA4A results in hypersensitivity to salt stress in Arabidopsis. Estradiol-induction of HSFA4A in transgenic plants decreases, while the knockout hsfa4a mutation elevates hydrogen peroxide accumulation and lipid peroxidation. Overexpression of HSFA4A alters the transcription of a large set of genes regulated by oxidative stress. In yeast two-hybrid and bimolecular fluorescence complementation (BiFC) assays HSFA4A shows homomeric interaction which is reduced by alanine replacement of three conserved cysteine residues. HSFA4A interacts with mitogen-activated protein kinases MPK3 and MPK6 in yeast and plant cells. MPK3 and MPK6 phosphorylate HSFA4A in vitro on three distinct sites, Ser309 being the major phosphorylation site. Activation of the MPK3 and MPK6 MAPK pathway led to the transcriptional activation of the heat-shock protein gene HSP17.6A. In agreement that mutation of Ser309 to alanine strongly diminished phosphorylation of HSFA4A, it also strongly reduced the transcriptional activation of HSP17.6A. These data suggest that HSFA4A is a substrate of the MPK3/6 signalling and it regulates stress responses in Arabidopsis. LA - English DB - MTMT ER -