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Originally published In Press as doi:10.1074/jbc.M101517200 on July 6, 2001

J. Biol. Chem., Vol. 276, Issue 36, 33375-33383, September 7, 2001
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Identification and Characterization of RRM-containing Coactivator Activator (CoAA) as TRBP-interacting Protein, and Its Splice Variant as a Coactivator Modulator (CoAM)*

Toshiharu Iwasaki, William W. Chin, and Lan KoDagger

From the Lilly Research Laboratories, Department of Gene Regulation, Bone and Inflammation Research, Eli Lilly and Company, Indianapolis, Indiana 46285

We previously cloned and characterized thyroid hormone receptor-binding protein (TRBP) as an LXXLL-containing general coactivator that associates with coactivator complexes through its C terminus. To identify protein cofactors for TRBP action, a Sos-Ras yeast two-hybrid cDNA library was screened using TRBP C terminus as bait. A novel coactivator was isolated, coactivator activator (CoAA), that specifically associates with TRBP. Human CoAA is composed of 669 amino acids with a TRBP-interacting domain and two highly conserved RNA recognition motifs (RRM) commonly found in ribonucleoproteins. A splice variant lacking the entire TRBP-interacting domain was also isolated as a coactivator modulator (CoAM), a 156-amino acid protein containing only the RRM region. Human CoAA and CoAM mRNAs are encoded by a single gene located on chromosome 11q13; alternative splicing in exon 2 of CoAA yields CoAM. CoAA interacts with both TRBP and p300 in vitro. In addition, CoAA potently coactivates transcription mediated by multiple hormone-response elements and acts synergistically with TRBP and CREB-binding protein (CBP). Furthermore, CoAA is associated with the DNA-dependent protein kinase-poly(ADP-ribose) polymerase complex. Strikingly, CoAM, which lacks a TRBP-interacting domain, strongly represses both TRBP and CBP action suggesting that CoAM may modulate endogenous CoAA function. These data suggest that CoAA may serve as a mediator of coactivators such as TRBP in gene activation.

* This work was supported by Lilly postdoctoral research fellowships.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.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF315632, AF315633, and AF327567.

Dagger To whom correspondence should be addressed: Eli Lilly and Company, Lilly Corporate Center, Bldg. 98/C, Drop Code 0434, Indianapolis, IN 46285. Tel.: 317-433-5237; Fax: 317-276-1414; E-mail: kol@lilly.com.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.


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