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Mol Cell Biol, March 1998, p. 1322-1330, Vol. 18, No. 3
Rosenstiel Research Center and Department of
Biology, Brandeis University, Waltham, Massachusetts
02254,1 and
Department of Biochemistry,
Dartmouth Medical School, Hanover, New Hampshire
037552
Received 15 August 1997/Returned for modification 23 September
1997/Accepted 9 December 1997
A tripartite domain of the murine immunoglobulin µ heavy-chain
enhancer contains the µA and µB elements that bind ETS
proteins and the µE3 element that binds leucine zipper-containing
basic helix-loop-helix (bHLH-zip) factors. Analysis of the
corresponding region of the human µ enhancer revealed high
conservation of the µA and µB motifs but a striking absence of the
µE3 element. Instead of bHLH-zip proteins, we found that the human
enhancer bound core binding factor (CBF) between the µA and µB
elements; CBF binding was shown to be a common feature of both murine
and human enhancers. Furthermore, mutant enhancers that bound
prototypic bHLH-zip proteins but not CBF did not activate transcription
in B cells, and conversely, CBF transactivated the murine enhancer in
nonlymphoid cells. Taking these data together with the earlier analysis
of T-cell-specific enhancers, we propose that ETS-CBF is a common
composite element in the regulation of antigen receptor genes.
In addition, these studies identify the first B-cell target of CBF, a
protein that has been implicated in the development of childhood
pre-B-cell leukemias.
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
ETS-Core Binding Factor: a Common Composite Motif
in Antigen Receptor Gene Enhancers
*
Corresponding author. Mailing address: Rosenstiel
Research Center and Department of Biology, Brandeis University,
Waltham, MA 02254. Phone: (781) 736-2455. Fax: (781) 736-2405. E-mail: sen{at}binah.cc.brandeis.edu.
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