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J. Biol. Chem., Vol. 277, Issue 25, 22484-22490, June 21, 2002
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From the Faculty of Bioscience and Biotechnology and
The transcription factor hGABP/E4TF1 is a
heterotetrameric complex composed of two DNA-binding subunits
(hGABP
YEAF1/RYBP and YAF-2 Are Functionally Distinct Members of a
Cofactor Family for the YY1 and E4TF1/hGABP Transcription
Factors*
,
, and**
Frontier Collaborative Research Center, Tokyo Institute of
Technology, 4259 Nagatsuta-cho, Midori-ku, Yokohama 226-8501 and
§ National Institute for Basic Biology, Okazaki National
Research Institutes, 38 Myodaiji, Okazaki 444-8585, Japan
/E4TF1-60) and two transactivating subunits
(hGABP
/E4TF1-53). In order to understand the molecular mechanism of
transcriptional regulation by hGABP, we searched for proteins that
interact with the non-DNA-binding subunit, hGABP, using yeast
two-hybrid screening. We identified a human cDNA encoding a protein
related to YAF-2 (YY1-associated factor 2), which was previously
isolated as an interacting partner of the Ying-Yang-1 (YY1)
transcription factor. Reflecting this similarity, both YAF-2 and this
novel protein (named YEAF1 for YY1- and
E4TF1/hGABP-associated
factor-1) interacted with hGABP and YY1
in vitro and in vivo, indicating that YEAF1 and
YAF-2 constitute a cofactor family for these two structurally distinct transcription factors. By using yeast three-hybrid assay, we
demonstrated that hGABP and YY1 formed a complex only in the
presence of YEAF1, indicating that YEAF1 is a bridging factor of these
two transcription factors. These cofactors are functionally different
in that YAF-2 positively regulates the transcriptional activity of
hGABP but YEAF1 negatively regulates this activity. Also,
YAF-2 mRNA is highly expressed in skeletal muscle,
whereas YEAF1 mRNA is highly expressed in placenta. We
speculate that the transcriptional activity of hGABP is in part
regulated by the expression levels of these tissue-specific cofactors.
These results provide a novel mechanism of transcriptional regulation
by functionally distinct cofactor family members.
*
This work was supported by a grant-in-aid for Scientific
Research on Priority Areas from the Ministry of Education, Culture, Sports, Science and Technology and by a grant for Research and Development Projects in cooperation with Academic Institutions from the
New Energy and Industrial Technology and Development Organization.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.
Present address: Dept. of Biological Chemistry and Molecular
Pharmacology, Harvard Medical School, 240 Longwood Ave., Boston, MA 02115.
¶
Present address: Dept. of Cancer Biology, Dana-Farber Cancer
Institute, Boston, MA 02115.
**
To whom correspondence should be addressed: Frontier Collaborative
Research Center, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midori-ku, Yokohama 226-8501, Japan. Tel.: 81-45-924-5872; Fax: 81-45-924-5145; E-mail: hhanda@bio.titech.ac.jp.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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