Volume 13, Issue 3 pp. 221-224
Brief Communication
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BCL6 encodes a sequence-specific DNA-binding Protein

Beverly W. Baron

Corresponding Author

Beverly W. Baron

Department of Pathology, University of Chicago, Chicago, Illinois

Blood Bank, MC0007, University of Chicago, 5841 S. Mavland Avenue, Chicago, IL 60637, U.S.A.Search for more papers by this author
Regan R Stanger

Regan R Stanger

Department of Pathology, University of Chicago, Chicago, Illinois

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Ellen Hume

Ellen Hume

Department of Pathology, University of Chicago, Chicago, Illinois

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Annamma Sadhu

Annamma Sadhu

Department of Pathology, University of Chicago, Chicago, Illinois

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Rosemarie Mick

Rosemarie Mick

Department of Medicine, Section of Hematology/Oncology, University of Chicago, Chicago, Illinois

Committee on Clinical Pharmacology and Cancer Research Center, University of Chicago, Chicago, Illinois

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Jean-Pierre Kerckaert

Jean-Pierre Kerckaert

U 124 INSERM LILLE, Lille, France

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Clotilde Deweindt

Clotilde Deweindt

U 124 INSERM LILLE, Lille, France

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Christian Bastard

Christian Bastard

Centre Regional de Transfusion Sanguine, Bois-Guillaume, France

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Giuseppina Nucifora

Giuseppina Nucifora

Department of Medicine, Section of Hematology/Oncology, University of Chicago, Chicago, Illinois

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Nancy Zeleznik-Le

Nancy Zeleznik-Le

Department of Medicine, Section of Hematology/Oncology, University of Chicago, Chicago, Illinois

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Timothy W. McKeithan

Timothy W. McKeithan

Department of Radiation-Oncology, University of Chicago, Chicago, Illinois

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First published: July 1995
Citations: 43

Abstract

Chromosomal rearrangements of BCL6 are commonly associated with diffuse large-cell lymphomas. We set out to determine the DNA-binding site of a glutathione-S-tranderase fusion protein containing the BCL6 zinc finger region by employing cyclic amplification and selection of targets (CASTing). From oligonucleotides containing 16 central random bases, sequences binding to the protein on glutathione-coated beads were repeatedly selected and amplified by polymerase chain reaction (PCR). The binding sites were cloned and sequenced. A consensus, TTTNNNGNNATNCTTT, was obtained. Protein binding studies of double-stranded oligomen containing point mutations within the 3′ CTTT confirmed the binding specificity of this part of the consensus. In addition, evidence indicated that some of the base pairs held constant in the oligonucleotides used for CASTing also contributed to binding. © 1995 Wiley-Liss, Inc.

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