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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.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.

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Copyright © 1998 by the American Society for Biochemistry and Molecular Biology.
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