{"title":"Temperature-dependent conformational changes in Arabidopsis DEHYDRATION-RESPONSIVE ELEMENT BINDING PROTEIN 2A","authors":"Petri Tähtinen, Hiroaki Fujii","doi":"10.1007/s11738-025-03799-0","DOIUrl":null,"url":null,"abstract":"<div><p>With the recent rise in global temperatures, understanding plant heat stress responses has become an urgent challenge. The DEHYDRATION-RESPONSIVE ELEMENT BINDING PROTEIN 2A (DREB2A) is one of the key transcription factors involved in plant responses to heat stress. Previous studies show that DREB2A degrades at 23 °C, while it accumulates at 37 °C in <i>Arabidopsis</i>, leading to heat-induced gene expression. However, the direct impact of temperature on DREB2A protein itself remains insufficiently understood. This study investigates the effect of temperature on the DREB2A protein by expressing recombinant DREB2A in <i>Escherichia coli</i>. Results demonstrate that DREB2A accumulates in <i>E. coli</i> at 37 °C but not at 23 °C, a pattern also observed in <i>Arabidopsis</i>, despite the differences between these organisms. Circular dichroism (CD) spectroscopy further revealed structural alterations in DREB2A between 23 °C and 37 °C, though specific details remain unclear. Taken together, these findings suggest that temperature-induced conformational changes occur in DREB2A between 23 °C and 37 °C, which may play a role in regulating its stability. This knowledge also indicates that 37 °C-induced stability is a contributing factor to successful purification of full-length recombinant DREB2A protein.</p></div>","PeriodicalId":6973,"journal":{"name":"Acta Physiologiae Plantarum","volume":"47 5","pages":""},"PeriodicalIF":2.4000,"publicationDate":"2025-04-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s11738-025-03799-0.pdf","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Acta Physiologiae Plantarum","FirstCategoryId":"99","ListUrlMain":"https://link.springer.com/article/10.1007/s11738-025-03799-0","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"PLANT SCIENCES","Score":null,"Total":0}
引用次数: 0
摘要
随着近年来全球气温的升高,了解植物的热胁迫反应已成为一项紧迫的挑战。脱氢-反应元件结合蛋白 2A(DREB2A)是参与植物热胁迫反应的关键转录因子之一。先前的研究表明,拟南芥中的 DREB2A 在 23 °C 时降解,而在 37 °C 时积累,导致热诱导基因表达。然而,温度对 DREB2A 蛋白本身的直接影响仍未得到充分了解。本研究通过在大肠杆菌中表达重组 DREB2A,研究温度对 DREB2A 蛋白的影响。结果表明,DREB2A 在 37 °C 时会在大肠杆菌中积累,而在 23 °C 时则不会,尽管拟南芥和大肠杆菌之间存在差异,但在拟南芥中也观察到了这种模式。圆二色性(CD)光谱进一步揭示了 DREB2A 在 23 °C 和 37 °C 之间的结构变化,但具体细节仍不清楚。综上所述,这些发现表明 DREB2A 在 23 ℃ 和 37 ℃ 之间会发生温度诱导的构象变化,这可能在调节其稳定性方面发挥作用。这些知识还表明,37 °C诱导的稳定性是成功纯化全长重组 DREB2A 蛋白的一个因素。
Temperature-dependent conformational changes in Arabidopsis DEHYDRATION-RESPONSIVE ELEMENT BINDING PROTEIN 2A
With the recent rise in global temperatures, understanding plant heat stress responses has become an urgent challenge. The DEHYDRATION-RESPONSIVE ELEMENT BINDING PROTEIN 2A (DREB2A) is one of the key transcription factors involved in plant responses to heat stress. Previous studies show that DREB2A degrades at 23 °C, while it accumulates at 37 °C in Arabidopsis, leading to heat-induced gene expression. However, the direct impact of temperature on DREB2A protein itself remains insufficiently understood. This study investigates the effect of temperature on the DREB2A protein by expressing recombinant DREB2A in Escherichia coli. Results demonstrate that DREB2A accumulates in E. coli at 37 °C but not at 23 °C, a pattern also observed in Arabidopsis, despite the differences between these organisms. Circular dichroism (CD) spectroscopy further revealed structural alterations in DREB2A between 23 °C and 37 °C, though specific details remain unclear. Taken together, these findings suggest that temperature-induced conformational changes occur in DREB2A between 23 °C and 37 °C, which may play a role in regulating its stability. This knowledge also indicates that 37 °C-induced stability is a contributing factor to successful purification of full-length recombinant DREB2A protein.
期刊介绍:
Acta Physiologiae Plantarum is an international journal established in 1978 that publishes peer-reviewed articles on all aspects of plant physiology. The coverage ranges across this research field at various levels of biological organization, from relevant aspects in molecular and cell biology to biochemistry.
The coverage is global in scope, offering articles of interest from experts around the world. The range of topics includes measuring effects of environmental pollution on crop species; analysis of genomic organization; effects of drought and climatic conditions on plants; studies of photosynthesis in ornamental plants, and more.