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krt 62, Hungary; email: szabados.laszlo@brc.mta.hu\nBiological Research Centre, Temesvári krt 62, Szeged, H-6726, Hungary \n Department of Plant Biology, University of Szeged, Szeged, 6726, Hungary \n School of Biological Sciences, Royal Holloway, University of London, Egham Hill, Surrey, TW200EX, United Kingdom \n Department of Biotechnology, Kakatiya University, Warangal, 506009, India \n Export Date: 21 February 2020 \n CODEN: JEBOA \n Correspondence Address: Szabados, L.; Biological Research Centre, Temesvári krt 62, Hungary; email: szabados.laszlo@brc.mta.hu\nWoS:hiba:000493107700026 2020-08-29 22:23 cikkazonosító nem egyezik\nBiological Research Centre, Temesvári krt 62, Szeged, H-6726, Hungary \n Department of Plant Biology, University of Szeged, Szeged, 6726, Hungary \n School of Biological Sciences, Royal Holloway, University of London, Egham Hill, Surrey, TW200EX, United Kingdom \n Department of Biotechnology, Kakatiya University, Warangal, 506009, India \n Cited By :15 \n 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"4903", "lastPage" : "4917", "internalId" : "erz217", "firstPageOrInternalIdForSort" : "4903, erz217", "pageLength" : 15, "publishedYear" : 2019, "abstractText" : "Heat shock factors regulate responses to high temperatures, salinity, water deprivation or heavy metals. Their function in stress combinations is however not known. The Arabidopsis HEAT SHOCK FACTOR A4A (HSFA4A) was previously reported to regulate responses to salt and oxidative stresses. Here we show, that the HSFA4A gene is induced by salt, elevated temperature and combination of these conditions. Fast translocation of HSFA4A-YFP protein from cytosol to nuclei takes place in salt-treated cells. HSFA4A can be phosphorylated not only by MAP kinases MPK3/6 but also by MPK4 and Ser309 is the dominant MAPK phosphorylation site. In vivo data suggest that HSFA4A can be substrate of other kinases as well. Changing Ser309 to Asp or Ala has altered intramolecular multimerization. Chromatin immunoprecipitation assays confirmed binding of HSFA4A to promoters of target genes encoding the small heat shock protein HSP17.6A and transcription factors WRKY30 and ZAT12. HSFA4A overexpression enhanced tolerance to individually and simultaneously applied heat and salt stresses through reduction of oxidative damage. 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