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J. Biol. Chem., Vol. 275, Issue 38, 29915-29921, September 22, 2000
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From the CTCF is a unique, highly conserved, and
ubiquitously expressed 11 zinc finger (ZF) transcriptional
factor with multiple DNA site specificities. It is able to bind to
varying target sequences to perform different regulatory roles,
including promoter activation or repression, creating
hormone-responsive gene silencing elements, and functional block of
enhancer-promoter interactions. Because different sets of ZFs are
utilized to recognize different CTCF target DNA sites, each of the
diverse DNA·CTCF complexes might engage different essential protein
partners to define distinct functional readouts. To identify such
proteins, we developed an affinity chromatography method based on
matrix-immobilized purified recombinant CTCF. This approach resulted in
isolation of several CTCF protein partners. One of these was identified
as the multifunctional Y-box DNA/RNA-binding factor, YB-1, known to be
involved in transcription, replication, and RNA processing. We examined
CTCF/YB-1 interaction by reciprocal immunoprecipitation experiments
with anti-CTCF and anti-YB-1 antibodies, and found that CTCF and YB-1
form complexes in vivo. We show that the bacterially
expressed ZF domain of CTCF is fully sufficient to retain YB-1 in
vitro. To assess possible functional significance of CTCF/YB-1
binding, we employed the very first identified by us, negatively
regulated, target for CTCF (c-myc oncogene promoter) as a
model in co-transfection assays with both CTCF and YB-1 expression
vectors. Although expression of YB-1 alone had no effect, co-expression
with CTCF resulted in a marked enhancement of CTCF-driven
c-myc transcriptional repression. Thus our findings
demonstrate, for the first time, the biological relevance of the
CTCF/YB-1 interaction.
Physical and Functional Interaction between Two Pluripotent
Proteins, the Y-box DNA/RNA-binding Factor, YB-1, and the Multivalent
Zinc Finger Factor, CTCF*
,,,,
, and**
Genetics Laboratory, Department of
Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom, the
§ Institute of Cancer Research, Haddow Laboratories, Sutton,
Surrey, United Kingdom, and the ¶ Section of Molecular Pathology,
Laboratory of Immunopathology, NIAID, National Institutes of Health,
Bethesda, Maryland 20892
*
This work was supported by a Royal Society research grant
and by a research grant from The Research and Equipment
Committee, University of Oxford.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence may be addressed: Section of Molecular
Pathology, Laboratory of Immunopathology, NIAID, National
Institutes of Health, Bldg. 7, Rm. 303, 7 Center Dr., MSC 0760, Bethesda, MD 20892. Tel.: 301-435-1690; Fax: 301-402-0077;
E-mail: vlobanenkov@niaid.nih.gov.
**
To whom correspondence may be addressed: Genetics Laboratory, Dept.
of Biochemistry, University of Oxford, South Parks Rd., Oxford OX1 3QU,
UK. Tel.: 44-1865-2753-14; Fax: 44-1865-2753-18; E-mail:
klenovae@bioch.ox.ac.uk.
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