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HERO ID
1330119
Reference Type
Journal Article
Title
Heme oxygenase-1 induction by NRF2 requires inactivation of the transcriptional repressor BACH1
Author(s)
Reichard, JF; Motz, GT; Puga, A
Year
2007
Is Peer Reviewed?
1
Journal
Nucleic Acids Research
ISSN:
0305-1048
EISSN:
1362-4962
Volume
35
Issue
21
Page Numbers
7074-7086
Language
English
PMID
17942419
DOI
10.1093/nar/gkm638
Web of Science Id
WOS:000251868800014
Abstract
Oxidative stress activates the transcription factor NRF2, which in turn binds cis-acting antioxidant response element (ARE) enhancers and induces expression of protective antioxidant genes. In contrast, the transcriptional repressor BACH1 binds ARE-like enhancers in cells naïve to oxidative stress and antagonizes NRF2 binding until it becomes inactivated by pro-oxidants. Here, we describe the dynamic roles of BACH1 and NRF2 in the transcription of the heme oxygenase-1 (HMOX1) gene. HMOX1 induction, elicited by arsenite-mediated oxidative stress, follows inactivation of BACH1 and precedes activation of NRF2. BACH1 repression is dominant over NRF2-mediated HMOX1 transcription and inactivation of BACH1 is a prerequisite for HMOX1 induction. In contrast, thioredoxin reductase 1 (TXNRD1) is regulated by NRF2 but not by BACH1. By comparing the expression levels of HMOX1 with TXNRD1, we show that nuclear accumulation of NRF2 is not necessary for HMOX1 induction; rather, BACH1 inactivation permits NRF2 already present in the nucleus at low basal levels to bind the HMOX1 promoter and elicit HMOX1 induction. Thus, BACH1 confers an additional level of regulation to ARE-dependent genes that reveals a new dimension to the oxidative stress response.
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