The transcriptional factor GATA-4 negatively regulates Hsp70 transcription in Crassostrea hongkongensis
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ORIGINAL ARTICLE
The transcriptional factor GATA-4 negatively regulates Hsp70 transcription in Crassostrea hongkongensis Tinglong Hou1 · Delin Xu1 · Miao Cui1 · Huiru Liu1 · Yaowu Fu1 · Lingli Zhang1 · Lei Tang1 · Yanmeng Liu1 · Qizhong Zhang1 Received: 16 April 2020 / Accepted: 28 August 2020 © Springer Nature B.V. 2020
Abstract To better explore the application potential of heat shock protein Hsp70s in diverse areas including biomonitoring, a further investigation of the details of the regulatory mechanism governing Hsp70 transcription is required. A transcriptional factor ChGATA-4 that displayed affinity to the ChHsp70 promoter of Crassostrea hongkongensis was isolated and identified by DNA affinity purification as well as mass spectrometry analysis. The ChGATA-4 cDNA is 2162 bp in length and the open reading frame encodes a polypeptide containing 482 amino acids with a conserved zinc finger domain. The over-expression of ChGATA-4 significantly inhibited the expression of ChHsp70 promoter in heterologous HEK293T cells. However, the depletion of ChGATA-4 mRNA by RNAi technique resulted in significant increase of ChHsp70 transcription in oyster hemocytes. The RT-PCR results demonstrated that the transcription of both ChHsp70 and ChGATA-4 were induced by heat, Cd, or NP (Nonyl phenol) stress. This suggested a potential correlation between ChHsp70 and ChGATA-4 in the stress-mediated genetic regulatory cascade. This study demonstrated that ChGATA-4 acts in a negative manner in controlling ChHsp70 transcription in C. hongkongensis and promotes to further understand the mechanisms leading Hsp70 transcription. Keywords GATA-4 · Hsp70 · Crassostrea hongkongensis · Transcriptional regulator · Negative regulation
Introduction Heat shock proteins (Hsps) are a group of stress-inducible, well conserved molecular chaperones that universally exist in all living organisms from prokaryotes to eukaryotes [1]. Hsps devote in promoting the three-dimensional folding of freshly produced proteins and repairing/eliminating the injured or aggregated proteins caused by various intense Tinglong Hou and Delin Xu have contributed equally to this work. Electronic supplementary material The online version of this article (https://doi.org/10.1007/s11033-020-05778-9) contains supplementary material, which is available to authorized users. * Qizhong Zhang [email protected] 1
Department of Ecology, Institute of Hydrobiology, School of Life Science and Technology, Key Laboratory of Eutrophication and Red Tide Prevention of Guangdong Higher Education Institutes, Engineering Research Center of Tropical and Subtropical Aquatic Ecological Engineering, Ministry of Education, Jinan University, Guangzhou 510632, People’s Republic of China
stresses [2]. They therefore play critical roles in protein homeostasis as well as cell physiology sustaining. Among the Hsps members, the 70-kDa heat shock proteins (Hsp70s) are currently the most comprehensively characterized family, comprising both stress-inducible (Hsp70s) and constitutive (Hsc70s) form
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