Forskning ved Københavns Universitet - Københavns Universitet


Differential roles of tau class glutathione S-transferases in oxidative stress

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

  • Kimiti G Kilili
  • Neli Atanassova
  • Alla Vardanyan
  • Nicolas Clatot
  • Khaled Al-Sabarna
  • Panagiotis N Kanellopoulos
  • Antonios M Makris
  • Kampranis, Sotirios

The plant glutathione S-transferase BI-GST has been identified as a potent inhibitor of Bax lethality in yeast, a phenotype associated with oxidative stress and disruption of mitochondrial functions. Screening of a tomato two-hybrid library for BI-GST interacting proteins identified five homologous Tau class GSTs, which readily form heterodimers between them and BI-GST. All six LeGSTUs were found to be able to protect yeast cells from prooxidant-induced cell death. The efficiency of each LeGSTU was prooxidant-specific, indicating a different role for each LeGSTU in the oxidative stress-response mechanism. The prooxidant protective effect of all six proteins was suppressed in the absence of YAP1, a transcription factor that regulates hydroperoxide homeostasis in Saccharomyces cerevisiae, suggesting a role for the LeGSTUs in the context of the YAP1-dependent stress-responsive machinery. The different LeGSTUs exhibited varied substrate specificity and showed activity against oxidative stress by-products, indicating that their prooxidant protective function is likely related to the minimization of oxidative damage. Taken together, these results indicate that Tau class GSTs participate in a broad network of catalytic and regulatory functions involved in the oxidative stress response.

TidsskriftThe Journal of Biological Chemistry
Udgave nummer23
Sider (fra-til)24540-51
Antal sider12
StatusUdgivet - 4 jun. 2004

ID: 159085347