High mobility group protein DSP1 negatively regulates HSP70 transcription in Crassostrea hongkongensis

Miao, Zongyu; Xu, Delin; Cui, Miao; Zhang, Qizhong

doi:10.1016/J.BBRC.2016.03.163

Title: High mobility group protein DSP1 negatively regulates HSP70 transcription in Crassostrea hongkongensis

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Abstract

HSP70 acts mostly as a molecular chaperone and plays important roles in facilitating the folding of nascent peptides as well as the refolding or degradation of the denatured proteins. Under stressed conditions, the expression level of HSP70 is upregulated significantly and rapidly, as is known to be achieved by various regulatory factors controlling the transcriptional level. In this study, a high mobility group protein DSP1 was identified by DNA-affinity purification from the nuclear extracts of Crassostrea hongkongensis using the ChHSP70 promoter as a bait. The specific interaction between the prokaryotically expressed ChDSP1 and the FITC-labeled ChHSP70 promoter was confirmed by EMSA analysis. ChDSP1 was shown to negatively regulate ChHSP70 promoter expression by Luciferase Reporter Assay in the heterologous HEK293T cells. Both ChHSP70 and ChDSP1 transcriptions were induced by either thermal or CdCl{sub 2} stress, while the accumulated expression peaks of ChDSP1 were always slightly delayed when compared with that of ChHSP70. This indicates that ChDSP1 is involved, very likely to exert its suppressive role, in the recovery of the ChHSP70 expression from the induced level to its original state. This study is the first to report negative regulator of HSP70 gene transcription, and provides novel insights into the mechanisms controllingmore »« less

Authors:: Miao, Zongyu; Xu, Delin; Cui, Miao; Zhang, Qizhong

Publication Date:: Fri Jun 10 00:00:00 EDT 2016

OSTI Identifier:: 22598762

Resource Type:: Journal Article

Journal Name:: Biochemical and Biophysical Research Communications

Additional Journal Information:: Journal Volume: 474; Journal Issue: 4; Other Information: Copyright (c) 2016 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0006-291X

Country of Publication:: United States

Language:: English

Subject:: 60 APPLIED LIFE SCIENCES; DNA; GENES; HEAT-SHOCK PROTEINS; LUCIFERASE; PEPTIDES; PROMOTERS; TRANSCRIPTION

Citation Formats


                    Miao, Zongyu, Xu, Delin, Cui, Miao, and Zhang, Qizhong. High mobility group protein DSP1 negatively regulates HSP70 transcription in Crassostrea hongkongensis.  United States: N. p., 2016. 
        Web.  doi:10.1016/J.BBRC.2016.03.163.

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                    Miao, Zongyu, Xu, Delin, Cui, Miao, & Zhang, Qizhong. High mobility group protein DSP1 negatively regulates HSP70 transcription in Crassostrea hongkongensis.  United States.  https://doi.org/10.1016/J.BBRC.2016.03.163

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                    Miao, Zongyu, Xu, Delin, Cui, Miao, and Zhang, Qizhong. 2016.  
        "High mobility group protein DSP1 negatively regulates HSP70 transcription in Crassostrea hongkongensis".  United States.  https://doi.org/10.1016/J.BBRC.2016.03.163.

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@article{osti_22598762,

  title        = {High mobility group protein DSP1 negatively regulates HSP70 transcription in Crassostrea hongkongensis},

  author       = {Miao, Zongyu and Xu, Delin and Cui, Miao and Zhang, Qizhong},

  abstractNote = {HSP70 acts mostly as a molecular chaperone and plays important roles in facilitating the folding of nascent peptides as well as the refolding or degradation of the denatured proteins. Under stressed conditions, the expression level of HSP70 is upregulated significantly and rapidly, as is known to be achieved by various regulatory factors controlling the transcriptional level. In this study, a high mobility group protein DSP1 was identified by DNA-affinity purification from the nuclear extracts of Crassostrea hongkongensis using the ChHSP70 promoter as a bait. The specific interaction between the prokaryotically expressed ChDSP1 and the FITC-labeled ChHSP70 promoter was confirmed by EMSA analysis. ChDSP1 was shown to negatively regulate ChHSP70 promoter expression by Luciferase Reporter Assay in the heterologous HEK293T cells. Both ChHSP70 and ChDSP1 transcriptions were induced by either thermal or CdCl{sub 2} stress, while the accumulated expression peaks of ChDSP1 were always slightly delayed when compared with that of ChHSP70. This indicates that ChDSP1 is involved, very likely to exert its suppressive role, in the recovery of the ChHSP70 expression from the induced level to its original state. This study is the first to report negative regulator of HSP70 gene transcription, and provides novel insights into the mechanisms controlling heat shock protein expression. -- Highlights: •HMG protein ChDSP1 shows affinity to ChHSP70 promoter in Crassostrea hongkongensis. •ChDSP1 negatively regulates ChHSP70 transcription. •ChHSP70 and ChDSP1 transcriptions were coordinately induced by thermal/Cd stress. •ChDSP1 may contribute to the recovery of the induced ChHSP70 to its original state. •This is the first report regarding negative regulator of HSP70 transcription.},

  doi          = {10.1016/J.BBRC.2016.03.163},

  url          = {https://www.osti.gov/biblio/22598762},
  journal      = {Biochemical and Biophysical Research Communications},

  issn         = {0006-291X},

  number       = 4,

  volume       = 474,

  place        = {United States},

  year         = {Fri Jun 10 00:00:00 EDT 2016},

  month        = {Fri Jun 10 00:00:00 EDT 2016}

}

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