RAPID COMMUNICATION Human MafG Is a Functional Partner for p45 NF-E2 in Activating Globin Gene Expression

Mammalian globin gene expression is activated through NFthat encodes the human homolog of chicken MafG. Human MafG heterodimerizes with p45 NF-E2 and binds DNA with E2 elements recognized by basic-leucine zipper proteins of the AP-1 superfamily. The specificity of NF-E2 DNA binding specificity identical to that of purified NF-E2 DNA binding activity. A tethered heterodimer of p45 and MafG is fully is determined by several nucleotides adjacent to a core AP1 motif, comprising a recognition site for transcription facfunctional in supporting expression of aand b-globin, and in promoting erythroid differentiation in CB3, a p45-deficient tors of the Maf subfamily. Earlier work proposed that p18(MafK) forms a heterodimer with hematopoietic-specific mouse erythroleukemia cell line. These results indicate that human MafG can serve as a functional partner for p45 NFprotein p45 NF-E2 to activate transcription through NF-E2 sites. However, there was no direct evidence that p18(MafK) E2, and suggest that the p45/MafG heterodimer plays a role in the regulation of erythropoiesis. serves this function in vivo; in fact, mice lacking p18(MafK) have no phenotype. Here we describe a novel cDNA clone q 1997 by The American Society of Hematology.