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Molecular and Cellular Biology, October 2009, p. 5327-5338, Vol. 29, No. 19
0270-7306/09/$08.00+0     doi:10.1128/MCB.00468-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Assembly of an Export-Competent mRNP Is Needed for Efficient Release of the 3'-End Processing Complex after Polyadenylation {triangledown}

Xiangping Qu,1 Søren Lykke-Andersen,2 Tommy Nasser,2 Cyril Saguez,2 Edouard Bertrand,3 Torben Heick Jensen,2* and Claire Moore1*

Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, Massachusetts 02111,1 Centre for mRNP Biogenesis and Metabolism, Department of Molecular Biology, Aarhus University, DK-8000 Aarhus C, Denmark,2 Institute of Molecular Genetics of Montpellier, Unité Mixte de Recherche 5535, C.N.R.S., 34293 Montpellier, France3

Received 10 April 2009/ Returned for modification 22 May 2009/ Accepted 20 July 2009

Before polyadenylated mRNA is exported from the nucleus, the 3'-end processing complex is removed by a poorly described mechanism. In this study, we asked whether factors involved in mRNP maturation and export are also required for disassembly of the cleavage and polyadenylation complex. An RNA immunoprecipitation assay monitoring the amount of the cleavage factor (CF) IA component Rna15p associated with poly(A)+ RNA reveals defective removal of Rna15p in mutants of the nuclear export receptor Mex67p as well as other factors important for assembly of an export-competent mRNP. In contrast, Rna15p is not retained in mutants of export factors that function primarily on the cytoplasmic side of the nuclear pore. Consistent with a functional interaction between Mex67p and the 3'-end processing complex, a mex67 mutant accumulates unprocessed SSA4 transcripts and exhibits a severe growth defect when this mutation is combined with mutation of Rna15p or another CF IA subunit, Rna14p. RNAs that become processed in a mex67 mutant have longer poly(A) tails both in vivo and in vitro. This influence of Mex67p on 3'-end processing is conserved, as depletion of its human homolog, TAP/NXF1, triggers mRNA hyperadenylation. Our results indicate a function for nuclear mRNP assembly factors in releasing the 3'-end processing complex once polyadenylation is complete.

* Corresponding author. Mailing address for Torben Heick Jensen: Centre for mRNP Biogenesis and Metabolism, Department of Molecular Biology, Aarhus University, DK-8000 Aarhus C., Denmark. Phone: 45-8942-2609. Fax: 45-8619-6500. E-mail: thj{at}mb.au.dk. Mailing address for Claire Moore: Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, Massachusetts 02111. Phone: (617) 636-6935. Fax: (617) 636-0337. E-mail: claire.moore{at}tufts.edu

{triangledown} Published ahead of print on 27 July 2009.

Molecular and Cellular Biology, October 2009, p. 5327-5338, Vol. 29, No. 19
0270-7306/09/$08.00+0     doi:10.1128/MCB.00468-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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