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Human MafG is a functional partner for p45 NF-E2 in activating globin gene expression.

Blood | Jun 1, 1997

http://www.ncbi.nlm.nih.gov/pubmed/9166829

Mammalian globin gene expression is activated through NF-E2 elements recognized by basic-leucine zipper proteins of the AP-1 superfamily. The specificity of NF-E2 DNA binding is determined by several nucleotides adjacent to a core AP-1 motif, comprising a recognition site for transcription factors of the Maf subfamily. Earlier work proposed that p18(MafK) forms a heterodimer with hematopoietic-specific protein p45 NF-E2 to activate transcription through NF-E2 sites. However, there was no direct evidence that p18(MafK) serves this function in vivo; in fact, mice lacking p18(MafK) have no phenotype. Here we describe a novel cDNA clone that encodes the human homolog of chicken MafG. Human MafG heterodimerizes with p45 NF-E2 and binds DNA with specificity identical to that of purified NF-E2 DNA binding activity. A tethered heterodimer of p45 and MafG is fully functional in supporting expression of alpha- and beta-globin, and in promoting erythroid differentiation in CB3, a p45-deficient mouse erythroleukemia cell line. These results indicate that human MafG can serve as a functional partner for p45 NF-E2, and suggest that the p45/MafG heterodimer plays a role in the regulation of erythropoiesis.

Pubmed ID: 9166829 RIS Download

Mesh terms: Amino Acid Sequence | Animals | Base Sequence | Cloning, Molecular | DNA, Complementary | DNA-Binding Proteins | Dimerization | Erythroid-Specific DNA-Binding Factors | Gene Expression Regulation | Globins | Humans | MafG Transcription Factor | MafK Transcription Factor | Mice | Molecular Sequence Data | NF-E2 Transcription Factor | NF-E2 Transcription Factor, p45 Subunit | Nuclear Proteins | Polymerase Chain Reaction | Repressor Proteins | Sequence Alignment | Transcription Factors | Zinc Fingers