BCL6 encodes a sequence-specific DNA-binding Protein
✍ Scribed by Beverly W. Baron; Regan R Stanger; Ellen Hume; Annamma Sadhu; Rosemarie Mick; Jean-Pierre Kerckaert; Clotilde Deweindt; Christian Bastard; Giuseppina Nucifora; Nancy Zeleznik-Le; Timothy W. McKeithan
- Publisher
- John Wiley and Sons
- Year
- 1995
- Tongue
- English
- Weight
- 402 KB
- Volume
- 13
- Category
- Article
- ISSN
- 1045-2257
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✦ Synopsis
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 6CL6 zinc finger region by employing cyclic amplification and selection of targets (CASTing). From oligonucleotides containing I6 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, TITNNNGNNATNCTIT, was obtained. Protein binding studies of double-stranded oligomen containing point mutations within the 3' C l l T 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. Genes Chromosom Cancer 13221-224 (1995).
📜 SIMILAR VOLUMES
Double-stranded DNA can be viewed as a multifunctional, modular receptor that can be read sequenceselectively in a digital way (base pair per base pair) by a complementary, similarly modular ligand. This principle has been exploited in several approaches to design sequence-specific DNA-binding ligan