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Human MafG is a functional partner for p45 NF-E2 in activating globin gene
expression
V Blank, MJ Kim and NC Andrews
Howard Hughes Medical Institute, Children's Hospital, and Harvard Medical
School, Boston, MA 02115, USA.
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.
Volume 89,
Issue 11,
pp. 3925-3935,
06/01/1997
Copyright © 1997 by The American Society of Hematology
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