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Updated: Aug 10, 2026

High Sensitivity Measurement of Transcription Factor-DNA Binding Affinities by Competitive Titration Using Fluorescence Microscopy
Published on: February 7, 2019
The zinc finger protein ZNF297B interacts with BDP1, a subunit of TFIIIB
Frank Schoenen1, Brunhilde Wirth
1Institute of Human Genetics, University of Cologne, D-50674 Cologne, Germany.
Abstract:
The human gene BDP1, localized on chromosome 5q13 in close proximity to the spinal muscular atrophy determining gene SMN, encodes a large protein consisting of 2254 amino acids (aa). In the first third of the gene, the subunit of the RNA polymerase III (Pol III) transcription factor complex (TFIIIB alpha/beta) is encoded. To further characterize the function of BDP1, we carried out a yeast two-hybrid screen using various parts of BDP1. With the clone BDP1-(1-640) we identified a novel interaction partner, ZNF297B. The ZNF297B gene is localized on chromosome 9q24 and encodes a zinc finger protein of 467 aa possessing the typical structure of a transcription factor. The interaction found in yeast was confirmed by co-immunoprecipitation and refined to the N-terminal region of ZNF297B-(1-127) containing the BTB/POZ domain and the N-terminal end of BDP1-(1-299). The ZNF297B transcript is 5.7 kb in length and ubiquitously expressed, with highest levels found in muscles. Immunofluorescence staining revealed a speckled pattern in the nuclei of HEK293 cells. Due to the essential role of BDP1 in Pol III transcription, we propose that ZNF297B may also regulate these transcriptional pathways.
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