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Nucleic Acids Research Advance Access originally published online on June 8, 2009
Nucleic Acids Research 2009 37(14):4672-4683; doi:10.1093/nar/gkp470
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Nucleic Acids Research, 2009, Vol. 37, No. 14 4672-4683
© 2009 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

RNA

A physical and functional link between splicing factors promotes pre-mRNA 3' end processing

Stefania Millevoi1,2,3,*, Adrien Decorsière1,2,3, Clarisse Loulergue1,2,3, Jason Iacovoni2,4, Sandra Bernat1,2,3, Michael Antoniou5 and Stéphan Vagner1,2,3,*

1INSERM, U563, Toulouse, 2Université de Toulouse, UPS, Centre de Physiopathologie de Toulouse Purpan, Toulouse, F-31300, 3Institut Claudius Regaud, Toulouse, F-31052, 4INSERM, IFR31, Bioinformatic Plateau, 1, Avenue Jean Poulhes, BP 84225, 31432 Toulouse Cedex 4, France and 5Nuclear Biology Group, Department of Medical and Molecular Genetics, King's College London School of Medicine, 8th Floor Tower Wing, Guy's Hospital, London, SE1 9RT, UK

*To whom correspondence should be addressed. Tel: +33 5 61 42 42 42. Ext: 4431; Fax: +33 5 61 42 46 31; Email: stefania.millevoi{at}inserm.fr

Correspondence may also be addressed to Stéphan Vagner. Tel: +33 5 67 69 63 11; Fax: +33 5 61 42 46 31; Email: stephan.vagner{at}inserm.fr

Received April 22, 2009. Revised May 15, 2009. Accepted May 15, 2009.

Polypyrimidine tract-binding protein (PTB) is a splicing regulator that also plays a positive role in pre-mRNA 3' end processing when bound upstream of the polyadenylation signal (pA signal). Here, we address the mechanism of PTB stimulatory function in mRNA 3' end formation. We identify PTB as the protein factor whose binding to the human β-globin (HBB) 3' UTR is abrogated by a 3' end processing-inactivating mutation. We show that PTB promotes both in vitro 3' end cleavage and polyadenylation and recruits directly the splicing factor hnRNP H to G-rich sequences associated with several pA signals. Increased binding of hnRNP H results in stimulation of polyadenylation through a direct interaction with poly(A) polymerase. Therefore, our results provide evidence of a concerted regulation of pA signal recognition by splicing factors bound to auxiliary polyadenylation sequence elements.

The authors wish it to be known that, in their opinion, the second and third authors should be regarded as joint Second Authors.


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