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Vol. 273, Issue 1, 392-397, January 2, 1998
From the The reversible oxidative inactivation of
transcription factors has been proposed to be important in cellular
responses to oxidant stress and in several signal transduction
pathways. The nuclear factor I (NFI) family of transcription factors is
sensitive to oxidative inactivation due to the presence of a conserved, oxidation-sensitive cysteine residue within the NFI DNA-binding domain.
Here we show that restoration of the DNA-binding activity of oxidized
NFI-C can be catalyzed in vitro by the cellular enzyme thioltransferase (glutaredoxin) coupled to GSH and GSSG reductase. To
test whether GSH-dependent pathways play a role in the
maintenance of NFI activity in vivo, we used buthionine
sulfoximine, an agent that inhibits GSH synthesis, and
N-acetylcysteine, an agent that can replenish intracellular
GSH. Pretreatment of HeLa cells with buthionine sulfoximine greatly
potentiated the inactivation of NFI by the oxidizing agent diamide.
Inclusion of N-acetylcysteine in the culture medium during
the recovery period following diamide treatment increased the extent of
restoration of NFI activity. These results suggest that maintenance of
the DNA-binding activity of NFI proteins during oxidant stress in
vivo requires a GSH-dependent pathway, likely
involving thioltransferase-catalyzed reduction of the
oxidation-sensitive cysteine residue on NFI.
Thioltransferase (Glutaredoxin) Reactivates the DNA-binding
Activity of Oxidation-inactivated Nuclear Factor I
,¶
Lerner Research Institute, Department of
Cancer Biology, Cleveland Clinic Foundation, Cleveland, Ohio 44195 and
the Departments of § Pharmacology and ¶ Biochemistry,
Case Western Reserve University, Cleveland, Ohio 44106
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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