Molecular and Cellular Biology, October 2000, p. 7662-7672, Vol. 20, No. 20
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Rotary Bone Marrow Research Laboratory, Royal Melbourne Hospital Research Foundation, Parkville, Victoria, Australia,1 and Division of Experimental Hematology, St. Jude Children's Research Hospital, Memphis, Tennessee2
Received 23 May 2000/Returned for modification 21 June 2000/Accepted 18 July 2000
The stage selector protein (SSP) is a heteromeric complex involved
in preferential expression of the human
-globin genes in
fetal-erythroid cells. We have previously identified the ubiquitous transcription factor CP2 as a component of this complex. Using the
protein dimerization domain of CP2 in a yeast two-hybrid screen, we
have cloned a novel gene, NF-E4, encoding the tissue-restricted component of the SSP. NF-E4 and CP2 coimmunoprecipitate from extract derived from a fetal-erythroid cell line, and antiserum to NF-E4 ablates binding of the SSP to the
promoter. NF-E4 is expressed in
fetal liver, cord blood, and bone marrow and in the K562 and HEL cell
lines, which constitutively express the fetal globin genes. Enforced
expression of NF-E4 in K562 cells and primary erythroid progenitors
induces endogenous fetal globin gene expression, suggesting a possible
strategy for therapeutic intervention in the hemoglobinopathies.
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