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Molecular and Cellular Biology, January 1999, p. 284-295, Vol. 19, No. 1
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Cux/CDP Homeoprotein Is a Component of NF-µNR and Represses the Immunoglobulin Heavy Chain Intronic Enhancer by Antagonizing the Bright Transcription Activator

Zhiyong Wang,1,dagger Adrian Goldstein,1 Rui-Ting Zong,2 Danjun Lin,2 Ellis J. Neufeld,3 Richard H. Scheuermann,1,* and Philip W. Tucker2

Department of Pathology and Laboratory of Molecular Pathology, The University of Texas Southwestern Medical Center, Dallas, Texas 75235-90721; Department of Microbiology and Institute for Cellular & Molecular Biology, University of Texas at Austin, Austin, Texas 78712-10952; and Division of Pediatric Hematology/Oncology, Children's Hospital, Dana Farber Cancer Institute and Harvard Medical School, Boston, Massachusetts 021153

Received 12 May 1998/Returned for modification 21 July 1998/Accepted 22 September 1998

Nuclear matrix attachment regions (MARs) flanking the immunoglobulin heavy chain intronic enhancer (Eµ) are the targets of the negative regulator, NF-µNR, found in non-B and early pre-B cells. Expression library screening with NF-µNR binding sites yielded a cDNA clone encoding an alternatively spliced form of the Cux/CDP homeodomain protein. Cux/CDP fulfills criteria required for NF-µNR identity. It is expressed in non-B and early pre-B cells but not mature B cells. It binds to NF-µNR binding sites within Eµ with appropriate differential affinities. Antiserum specific for Cux/CDP recognizes a polypeptide of the predicted size in affinity-purified NF-µNR preparations and binds NF-µNR complexed with DNA. Cotransfection with Cux/CDP represses the activity of Eµ via the MAR sequences in both B and non-B cells. Cux/CDP antagonizes the effects of the Bright transcription activator at both the DNA binding and functional levels. We propose that Cux/CDP regulates cell-type-restricted, differentiation stage-specific Eµ enhancer activity by interfering with the function of nuclear matrix-bound transcription activators.

* Corresponding author. Mailing address: Department of Pathology, UT Southwestern Medical Center, 5323 Harry Hines Blvd., Dallas, TX 75235-9072. Phone: (214) 648-4115. Fax: (214) 648-4070. E-mail: scheuerm{at}utsw.swmed.edu.

dagger Present address: Howard Hughes Medical Institute, University of California at San Diego, La Jolla, CA 92093-0648.

Molecular and Cellular Biology, January 1999, p. 284-295, Vol. 19, No. 1
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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