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J Biol Chem, Vol. 273, Issue 30, 18881-18890, July 24, 1998

Purification and Characterization of a Protein Binding to the SP6  Promoter
A POTENTIAL ROLE FOR CArG-BOX BINDING FACTOR-A IN  TRANSCRIPTION

Mats Bemark, Henric Olsson^§, Dick Heinegård^§, and Tomas Leanderson

From the  Immunology and ^§ Connective Tissue Biology Groups, Department of Cellular and Molecular Biology, Lund University, S-220 07 Lund, Sweden

A protein interacting with an A-T-rich region that is a positive control element within the SP6  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.

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