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Originally published In Press as doi:10.1074/jbc.M201739200 on March 23, 2002

J. Biol. Chem., Vol. 277, Issue 22, 20011-20019, May 31, 2002
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Interaction of PIMT with Transcriptional Coactivators CBP, p300, and PBP Differential Role in Transcriptional Regulation*

Parimal MisraDagger §, Chao QiDagger , Songtao YuDagger , Sejal H. ShahDagger , Wen-Qing CaoDagger , M. Sambasiva RaoDagger , Bayar Thimmapaya, Yijun ZhuDagger , and Janardan K. ReddyDagger ||

From the Departments of Dagger  Pathology and  Microbiology and Immunology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois 60611-3008

PIMT (PRIP-interacting protein with methyltransferase domain), an RNA-binding protein with a methyltransferase domain capable of binding S-adenosylmethionine, has been shown previously to interact with nuclear receptor coactivator PRIP (peroxisome proliferator-activated receptor (PPAR)-interacting protein) and enhance its coactivator function. We now report that PIMT strongly interacts with transcriptional coactivators, CBP, p300, and PBP but not with SRC-1 and PGC-1alpha under in vitro and in vivo conditions. The PIMT binding sites on CBP and p300 are located in the cysteine-histidine-rich C/H1 and C/H3 domains, and the PIMT binding site on PBP is in the region encompassing amino acids 1101-1560. The N-terminal of PIMT (residues 1-369) containing the RNA binding domain interacts with both C/H1 and C/H3 domains of CBP and p300 and with the C-terminal portion of PBP that encompasses amino acids 1371-1560. The C-terminal of PIMT (residues 611-852), which binds S-adenosyl-L-methionine, interacts respectively with the C/H3 domain of CBP/p300 and with a region encompassing amino acids 1101-1370 of PBP. Immunoprecipitation data showed that PIMT forms a complex in vivo with CBP, p300, PBP, and PRIP. PIMT appeared to be co-localized in the nucleus with CBP, p300, and PBP. PIMT enhanced PBP-mediated transcriptional activity of the PPARgamma , as it did for PRIP, indicating synergism between PIMT and PBP. In contrast, PIMT functioned as a repressor of CBP/p300-mediated transactivation of PPARgamma . Based on these observations, we suggest that PIMT bridges the CBP/p300-anchored coactivator complex with the PBP-anchored coactivator complex but differentially modulates coactivator function such that inhibition of the CBP/p300 effect may be designed to enhance the activity of PBP and PRIP.

* This work was supported by National Institutes of Health Grants GM23750 (to J. K. R.), CA84472 (to M. S. R.), R01 CA74403 (to B. T.), K08 ES00356 and CA 88898 (to Y. Z.) and the Joseph L. Mayberry, Sr. Endowment Fund.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.

§ Supported by the Dr. Reddy Research Foundation, Miyapur, Hyderabad 500050 India.

|| To whom correspondence should be addressed: Dept. of Pathology, Feinberg School of Medicine, Northwestern University, 303 E. Chicago Ave., Chicago, IL 60611-3008. Tel.: 312-503-8144; Fax: 312-503-8249; E-mail: jkreddy@northwestern.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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