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Related Experiment Videos

Glutathione transferases: new functions.

Aaron J Oakley1

  • 1Research School of Chemistry, Australian National University, Canberra, ACT 0200, Australia. oakley@rsc.anu.edu.au

Current Opinion in Structural Biology
|November 3, 2005
PubMed
Summary
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Glutathione transferases (GSTs) are known for detoxification but also play roles in hormone synthesis. Recent studies reveal diverse functions and structures for GSTs, including transcription factors and ion channels, expanding their known biological significance.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Glutathione transferases (GSTs) are primarily recognized for their role in cellular detoxification.
  • Emerging evidence suggests GSTs are involved in prostaglandin and steroid hormone synthesis.
  • The canonical GST fold is found in proteins beyond traditional detoxification roles.

Purpose of the Study:

  • To explore novel functions and structural characteristics of glutathione transferases.
  • To investigate the structural basis of GSTs in diverse cellular processes.
  • To understand the evolutionary relationships and structural diversity of GST enzymes.

Main Methods:

  • X-ray crystallography was employed to determine the structures of various glutathione transferases.

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  • Comparative structural analysis was performed on canonical and non-canonical GST folds.
  • Biochemical assays were utilized to assess functional roles.

    • Main Results:

    • The canonical glutathione transferase fold is present in transcription factors like SspA and Ure2p, though their functions remain unclear.
    • The intracellular chloride channel CLIC1 utilizes the GST fold, undergoing structural changes during membrane insertion.
    • Mitochondrial glutathione transferases exhibit a distinct topology, suggesting independent evolution from canonical GSTs.
    • Integral membrane glutathione S-transferases share common tertiary and quaternary structural patterns.

    Conclusions:

    • Glutathione transferases possess a broader functional repertoire than previously understood, extending to transcriptional regulation and ion transport.
    • Structural studies reveal significant diversity within the GST superfamily, including independent evolutionary paths.
    • The canonical GST fold is a versatile structural motif adaptable to various biological functions.