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Related Experiment Videos

[Redox-dependent changes in structure and function of hHSF1].

Zheng Lin1, Fan Huang, Zhong-Fu Ma

  • 1The First Hospital Affiliated to Sun Yat-Sen University, Guangzhou, 510080 China. zhenglin2@hotmail.com

Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao Acta Biochimica Et Biophysica Sinica
|June 11, 2003
PubMed
Summary
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Redox reagents like diamide stabilize human heat shock transcription factor 1 (hHSF1) in a monomeric form, blocking its activation. This effect is reversible with dithiothreitol, revealing redox control over hHSF1 conformation.

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Cell Biology

Background:

  • Human heat shock transcription factor 1 (hHSF1) regulates cellular stress responses.
  • The redox status of proteins can influence their structure and function.
  • Understanding hHSF1 regulation is crucial for cellular stress response mechanisms.

Purpose of the Study:

  • To investigate the impact of cysteine-SH-directed reagents on hHSF1's redox status, structure, and function.
  • To elucidate the role of redox-dependent thiol-disulfide exchange in hHSF1 regulation.

Main Methods:

  • In vitro treatment of purified hHSF1 with diamide (DM).
  • In vivo treatment of HeLa cells with buthionine sulfoximine (BSO).
  • Computer modeling of hHSF1 monomer and trimer structures.

Related Experiment Videos

  • Reversal experiments using dithiothreitol (DTT).

    • Main Results:

    • Oxidizing reagents (DM, BSO) induced a compact, disulfide-crosslinked, monomeric ox-hHSF1.
    • This crosslinking blocked hHSF1 trimerization and activation in a dose-dependent manner.
    • The effects were fully reversible upon addition of the reducing agent DTT.
    • Computer modeling supported the possibility of intramolecular disulfide bond formation.

    Conclusions:

    • Redox-dependent thiol-disulfide exchange is a key mechanism regulating hHSF1 conformation and activity.
    • Specific cysteine residues (Cys153, Cys373, Cys378) are likely involved in redox-sensitive disulfide bond formation.
    • This provides a novel insight into the post-translational modification and control of hHSF1 function.