Nrf2 acetylation

Stimulation of NF-E2 DNA Binding by CREB-binding Protein (CBP)-mediated AcetylationFind It @ MUgroup of 2 »
HL Hung, AY Kim, W Hong, C Rakowski, GA Blobel – Journal of Biological Chemistry, 2001 – jbc.org
DNA binding activity of NF-E2, and mutations at the major acetylation sites markedly
Other members of the CNC family, including Nrf1 (8), Nrf2 (9), Nrf3 (10
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The basic-zipper (bZip)1 transcription factor NF-E2 plays a critical role in erythroid and megakaryocytic gene expression (for review see Ref. 1). NF-E2 binds to an extended AP-1-like element, TGCTGA(G/C)TCA, which is found in the locus control regions (LCRs) of the alpha – and beta -globin genes and in the promoters of several heme biosynthetic enzyme genes (for review see Refs. 2 and 3)). NF-E2 binding sites in the DNase I hypersensitive site 2 (HS2) of the beta -globin LCR are essential for its enhancer activity (4-6).

NF-E2 is a heterodimer consisting of a hematopoietic-specific subunit p45, which is a member of the cap and collar (CNC) family, and a more widely expressed small subunit, which is a member of the small Maf protein family (MafG, MafK, and MafF) (for review see Refs. 2 and 3)). MafG and MafK are the predominant small Maf molecules in erythroid cells and megakaryocytes (7). p45 and a small Maf protein dimerize through their leucine zipper domains to generate a composite DNA binding domain that consists of the basic regions of both molecules. Other members of the CNC family, including Nrf1 (8), Nrf2 (9), Nrf3 (10), Bach1, and Bach2 (11) can also dimerize with small Maf proteins. Despite the high levels of p45 expression in erythroid cells, mice that are null for p45 displayed a surprisingly mild defect in globin gene expression, suggesting that other members of the CNC protein family can substitute for p45 function in vivo (12).

 Its also known that NRF2 can interact with Maf proteins(as negative regulators?). How much similiarity do p45 and NRF2 have?

Null Mutants indicate that other CNC TF’s can substitute?

NM_006163 Reports   Links
Homo sapiens nuclear factor (erythroid-derived 2), 45kDa (NFE2), mRNA
gi|5453773|ref|NM_006163.1|[5453773]

The N terminus of p45 contains an activation domain that is important for the biological activity of p45 (13, 14). Several molecules interact with this domain and are candidate mediators of p45 activity. These include TAFII130 (a component of the TFIID complex) (15), cAMP-response element-binding protein (CREB)-binding protein (CBP) (16), and several ubiquitin ligases (17, 18). The small Maf proteins lack a typical activation domain and are believed to activate transcription as heterodimers with members of the CNC family of proteins. Small Maf proteins can also form homodimers and repress transcription (19).

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