Purification and characterization of a protein binding to the SP6 kappa promoter. A potential role for CArG-box binding factor-A in kappa transcription.

A protein interacting with an A-T-rich region that is a positive control element within the SP6 kappa promoter was purified and identified as CArG-box binding factor-A. The purified protein was shown to interact specifically with the coding strand of single-stranded DNA and, with lower affinity, with double-stranded DNA. A mutation ...
that inhibited binding of the protein to the A-T-rich region also aborted the transcriptional stimulatory effect of the region. Two Ets proteins, PU.1 and elf-1, that have previously been shown to bind to an adjacent DNA element were shown to physically interact with CArG-box binding factor-A. An antiserum raised against the protein recognized two different forms indicating either that different splice-forms of CArG-box binding factor-A are expressed, or that the protein is subject to post-translational modification.
Mesh Terms:
Alternative Splicing, Animals, Base Sequence, DNA, DNA-Binding Proteins, DNA-Directed RNA Polymerases, Immunoglobulin kappa-Chains, Molecular Sequence Data, Promoter Regions, Genetic, Protein Binding, Repressor Proteins, Transcription Factors, Tumor Cells, Cultured
J. Biol. Chem.
Date: Jul. 24, 1998
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