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J. Biol. Chem., Vol. 282, Issue 34, 25067-25075, August 24, 2007

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Poly(A) Nuclease Interacts with the C-terminal Domain of Polyadenylate-binding Protein Domain from Poly(A)-binding Protein^*

Nadeem Siddiqui¹, David A. Mangus, Tsung-Cheng Chang^¶, Jeanne-Marie Palermino, Ann-Bin Shyu^¶, and Kalle Gehring, Chercheur National of the Fonds de la Recherche en Santé du Québec²

From the Department of Biochemistry, McGill University, Montréal, Quebec H3G 1Y6, Canada, the Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, Worcester, Massachusetts 01655, and the ^¶Department of Biochemistry and Molecular Biology, University of Texas Medical School, Houston, Texas 77030

The poly(A)-binding protein (PABP) is an essential protein found in all eukaryotes and is involved in an extensive range of cellular functions, including translation, mRNA metabolism, and mRNA export. Its C-terminal region contains a peptide-interacting PABC domain that recruits proteins containing a highly specific PAM-2 sequence motif to the messenger ribonucleoprotein complex. In humans, these proteins, including Paip1, Paip2, eRF3 (eukaryotic release factor 3), Ataxin-2, and Tob2, are all found to regulate translation through varying mechanisms. The following reports poly(A) nuclease (PAN) as a PABC-interacting partner in both yeast and humans. Their interaction is mediated by a PAM-2 motif identified within the PAN3 subunit. This site was identified in various fungal and animal species suggesting that the interaction is conserved throughout evolution. Our results indicate that PABP is directly involved in recruiting a deadenylase to the messenger ribonucleoprotein complex. This demonstrates a novel role for the PABC domain in mRNA metabolic processes and gives further insight into the function of PABP in mRNA maturation, export, and turnover.

Received for publication, February 12, 2007 , and in revised form, June 26, 2007.

^* This work was supported in part by Canadian Institutes of Health Research Grant MOP-14219 (to K. G.), National Institutes of Health Grant GM46454, and Houston Endowment, Inc., grants (to A.-B. S.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ Recipient of a McGill Graduate Study and Faculty of Medicine Internal Fellowship. Present address: Institute of Research in Immunology and Cancer, Université de Montréal, Pavilion Marcelle-Coutu, 2950 Chemin Polytechnique, Montréal, Quebec, Canada.

² To whom correspondence should be addressed. Fax: 514-398-7384; E-mail: kalle.gehring{at}mcgill.ca.

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