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Molecular and Cellular Biology, January 2004, p. 442-453, Vol. 24, No. 1
0270-7306/04/$08.00+0     DOI: 10.1128/MCB.24.1.442-453.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

CoAA, a Nuclear Receptor Coactivator Protein at the Interface of Transcriptional Coactivation and RNA Splicing

Didier Auboeuf,1,{dagger} Dennis H. Dowhan,1 Xiaotao Li,1 Kimberly Larkin,1 Lan Ko,2 Susan M. Berget,3 and Bert W. O'Malley1*

Department of Molecular and Cellular Biology,1 Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, Texas 77030,3 Department of Pathology, Medical College of Georgia, Augusta, Georgia 309122

Received 25 June 2003/ Returned for modification 3 September 2003/ Accepted 30 September 2003

We have shown that steroid hormones coordinately control gene transcriptional activity and splicing decisions in a promoter-dependent manner. Our hypothesis is that a subset of hormonally recruited coregulators involved in regulation of promoter transcriptional activity also directly participate in alternative RNA splicing decisions. To gain insight into the molecular mechanisms by which transcriptional coregulators could control splicing decisions, we focused our attention on a recently identified coactivator, CoAA. This heterogeneous nuclear ribonucleoprotein (hnRNP)-like protein interacts with the transcriptional coregulator TRBP, a protein recruited to target promoters through interactions with activated nuclear receptors. Using transcriptional and splicing reporter genes driven by different promoters, we observed that CoAA mediates transcriptional and splicing effects in a promoter-preferential manner. We compared the activity of CoAA to the activity of other hnRNP-related proteins that, like CoAA, contain two N-terminal RNA recognition motifs (RRMs) followed by a C-terminal auxiliary domain and either have or have not been implicated in transcriptional control. By swapping either CoAA RRMs or the CoAA auxiliary domain with the corresponding domains of the proteins selected, we showed that depending on the promoter, the RRMs and the auxiliary domain of CoAA are differentially engaged in transcription. This contributes to the promoter-preferential effects mediated by CoAA on RNA splicing during the course of steroid hormone action.

* Corresponding author. Mailing address: Department of Molecular and Cellular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030. Phone: (713) 798-6205. Fax: (713) 798-5599. E-mail: berto{at}bcm.tmc.edu.

{dagger} Present address: Equipe AVENIR-INSERM U496, Centre G. Hayem, Hopital Saint-Louis, 75010 Paris, France.

Molecular and Cellular Biology, January 2004, p. 442-453, Vol. 24, No. 1
0022-538X/04/$08.00+0     DOI: 10.1128/MCB.24.1.442-453.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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