Transcription factor CaHDZ15 promotes pepper basal thermotolerance by activating HEAT SHOCK FACTORA6a

Author:

Mou Shaoliang123ORCID,He Weihong123,Jiang Haitao123ORCID,Meng Qianqian123ORCID,Zhang Tingting123ORCID,Liu Zhiqin234ORCID,Qiu Ailian123ORCID,He Shuilin234ORCID

Affiliation:

1. College of Life Science, Fujian Agriculture and Forestry University , Fuzhou, Fujian 350002 , PR China

2. Key Laboratory of Applied Genetics of Universities in Fujian Province, Fujian Agriculture and Forestry University , Fuzhou, Fujian 350002 , PR China

3. National Education Minister, Key Laboratory of Plant Genetic Improvement and Comprehensive Utilization, Fujian Agriculture and Forestry University , Fuzhou, Fujian 350002 , PR China

4. College of Agriculture Science, Fujian Agriculture and Forestry University , Fuzhou, Fujian 350002 , PR China

Abstract

Abstract High temperature stress (HTS) is a serious threat to plant growth and development and to crop production in the context of global warming, and plant response to HTS is largely regulated at the transcriptional level by the actions of various transcription factors (TFs). However, whether and how homeodomain-leucine zipper (HD-Zip) TFs are involved in thermotolerance are unclear. Herein, we functionally characterized a pepper (Capsicum annuum) HD-Zip I TF CaHDZ15. CaHDZ15 expression was upregulated by HTS and abscisic acid in basal thermotolerance via loss- and gain-of-function assays by virus-induced gene silencing in pepper and overexpression in Nicotiana benthamiana plants. CaHDZ15 acted positively in pepper basal thermotolerance by directly targeting and activating HEAT SHOCK FACTORA6a (HSFA6a), which further activated CaHSFA2. In addition, CaHDZ15 interacted with HEAT SHOCK PROTEIN 70-2 (CaHsp70-2) and glyceraldehyde-3-phosphate dehydrogenase1 (CaGAPC1), both of which positively affected pepper thermotolerance. CaHsp70-2 and CaGAPC1 promoted CaHDZ15 binding to the promoter of CaHSFA6a, thus enhancing its transcription. Furthermore, CaHDZ15 and CaGAPC1 were protected from 26S proteasome-mediated degradation by CaHsp70-2 via physical interaction. These results collectively indicate that CaHDZ15, modulated by the interacting partners CaGAPC1 and CaHsp70-2, promotes basal thermotolerance by directly activating the transcript of CaHSFA6a. Thus, a molecular linkage is established among CaHsp70-2, CaGAPC1, and CaHDZ15 to transcriptionally modulate CaHSFA6a in pepper thermotolerance.

Funder

National Natural Science Foundation of China

Natural Science Foundation of Fujian Province

Development Fund Project of Fujian Agriculture and Forestry University

Publisher

Oxford University Press (OUP)

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