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Updated: Aug 6, 2026

Combined Immunofluorescence and DNA FISH on 3D-preserved Interphase Nuclei to Study Changes in 3D Nuclear Organization
Published on: February 3, 2013
CArG box-binding factor-A interacts with multiple motifs in immunoglobulin promoters and has a regulated subcellular
Alaitz Aranburu1, David Liberg, Bent Honoré
1Immunology Group, Lund University, Lund, Sweden.
Abstract:
CArG box-binding factor-A (CBF-A) is a protein involved in transcriptional control and interacts specifically with the penta-decameric (pd) element in kappa promoters. We show here that CBF-A will also bind specifically to a second region in the kappa promoter that overlaps with an early B cell factor binding site. Furthermore, the same region is present in multiple Ig promoters and we show that CBF-A can bind to several of these. Mitogenic stimulation of untransformed B lymphocytes promoted nuclear localisation of CBF-A. Using enhanced GFP (EGFP)-tagged constructs and transfection into COS7 cells, a nuclear localisation signal was defined in the C terminus of CBF-A. Deletion of only 13 amino acids from the C terminus of CBF-A led to the accumulation of the protein in bright speckles at the nuclear/cytoplasmic border. We also identified the heterogeneous ribonucleoprotein H as a specific interaction partner of CBF-A, but this interaction could be detected in the cytoplasm only. Thus, CBF-A has the potential to regulate the expression of multiple Ig V genes and has a complex, mitogen-responsive regulation of its intracellular localisation.
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