NDLI: Identification of a transcriptionally active peroxisome proliferator-activated receptor α-interacting cofactor complex in rat liver and characterization of PRIC285 as a coactivator

Content Provider	PubMed Central
Author	Sailesh, Surapureddi Yu, Songtao Bu, Hengfu Hashimoto, Takashi Yeldandi, Anjana V. Kashireddy, Papreddy Mustapha, Cherkaoui-malki Qi, Chao Zhu, Yi-jun Rao, M. Sambasiva Reddy, Janardan K.
Copyright Year	2002
Abstract	Peroxisome proliferator-activated receptor α (PPARα) plays a central role in the cell-specific pleiotropic responses induced by structurally diverse synthetic chemicals designated as peroxisome proliferators. Transcriptional regulation by liganded nuclear receptors involves the participation of cofactors that form multiprotein complexes to achieve cell- and gene-specific transcription. Here we report the identification of such a transcriptionally active PPARα-interacting cofactor (PRIC) complex from rat liver nuclear extracts that interacts with full-length PPARα in the presence of ciprofibrate, a synthetic ligand, and leukotriene B4, a natural ligand. The liganded PPARα-PRIC complex enhanced transcription from a peroxisomal enoyl-CoA hydratase/l-3-hydroxyacyl-CoA dehydrogenase bifunctional enzyme gene promoter template that contains peroxisome proliferator response elements. Rat liver PRIC complex comprises some 25 polypeptides, and their identities were established by mass spectrometry and limited sequence analysis. Eighteen of these peptides contain one or more LXXLL motifs necessary for interacting with nuclear receptors. PRIC complex includes known coactivators or coactivator-binding proteins (CBP, SRC-1, PBP, PRIP, PIMT, TRAP100, SUR-2, and PGC-1), other proteins that have not previously been described in association with transcription complexes (CHD5, TOG, and MORF), and a few novel polypeptides designated PRIC300, -285, -215, -177, and -145. We describe the cDNA for PRIC285, which contains five LXXLL motifs. It interacts with PPARα and acts as a coactivator by moderately stimulating PPARα-mediated transcription in transfected cells. We conclude that liganded PPARα recruits a distinctive multiprotein complex from rat liver nuclear extracts. The composition of this complex may provide insight into the basis of tissue and species sensitivity to peroxisome proliferators.
Related Links	http://dx.doi.org/10.1073/pnas.182426699
Ending Page	11841
Page Count	6
Starting Page	11836
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	18
Volume Number	99
Language	English
Publisher	The National Academy of Sciences
Publisher Date	2002-09-03
Access Restriction	Open
Rights Holder	The National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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