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J Biol Chem, Vol. 273, Issue 30, 19251-19259, July 24, 1998
From the Division of Molecular Medicine, Tax-1, the transcriptional activation protein of
human T-cell leukemia virus-1, increases transcription from the human
T-cell leukemia virus-1 long terminal repeat and specific cellular
promoters through interactions with cellular DNA-binding proteins. The
Tax response elements (TxREs) of the long terminal repeat resemble cAMP
response elements (CREs), the target of cAMP-responsive element-binding protein (CREB). CREB binds the TxRE with reduced affinity; however, the
interaction is specifically enhanced by Tax. Using a fluorescence quenching method, we determined that CREB dimerizes in the absence of
DNA, and that Tax does not enhance dimerization. DNA footprinting of
the TxRE with 1,10-phenanthroline-copper complex demonstrates that Tax
contacts DNA and extends the footprint of CREB to GC-rich sequences
flanking the core CRE-like element. The minor groove-binding drug
chromomycin A3, but not distamycin A, disrupted
Tax-enhanced CREB binding to the TxRE. Substitution of the guanine-rich
sequences flanking the core of the TxRE with inosine residues also
blocked the Tax effect. Finally, the IC-substituted TxRE binds CREB
with increased affinity, suggesting flanking DNA influences the binding of CREB to the core CRE-like element. These data indicate that Tax does
not regulate DNA binding of CREB by altering dimerization, but rather
enhances DNA binding by additionally interacting with the minor groove
of flanking DNA sequences.
The Human T-cell Leukemia Virus-1 Transcriptional Activator Tax
Enhances cAMP-responsive Element-binding Protein (CREB) Binding
Activity through Interactions with the DNA Minor Groove
,
, Department
of Medicine, ** Department of Biochemistry and Molecular Biology,
Division of Hematology/Oncology,
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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