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Nucleic Acids Research Advance Access originally published online on November 25, 2008
Nucleic Acids Research 2009 37(1):129-143; doi:10.1093/nar/gkn894
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Nucleic Acids Research, 2009, Vol. 37, No. 1 129-143
© 2008 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.

Structural Biology

Structure of the yeast Pml1 splicing factor and its integration into the RES complex

Mark A. Brooks1, Andrzej Dziembowski2,3,4, Sophie Quevillon-Cheruel1, Véronique Henriot2,3,4, Céline Faux2,3,4, Herman van Tilbeurgh1 and Bertrand Séraphin2,3,4,*

1IBBMC-CNRS UMR8619, IFR 115, Bât. 430, Université Paris-Sud, 91405 Orsay, 2Equipe Labelisée La Ligue, CGM, CNRS UPR2167, Avenue de la Terrasse, 91198 Gif-sur-Yvette Cedex, 3Univ Paris-Sud, Orsay, F-91405 and 4Université Pierre et Marie Curie- Paris 6, Paris, F-75005, France

*To whom correspondence should be addressed. Tel: + 33 1 69 82 38 84; Fax: + 33 1 69 82 38 77; Email: seraphin{at}cgm.cnrs-gif.fr

Received July 28, 2008. Revised October 20, 2008. Accepted October 23, 2008.

The RES complex was previously identified in yeast as a splicing factor affecting nuclear pre-mRNA retention. This complex was shown to contain three subunits, namely Snu17, Bud13 and Pml1, but its mode of action remains ill-defined. To obtain insights into its function, we have performed a structural investigation of this factor. Production of a short N-terminal truncation of residues that are apparently disordered allowed us to determine the X-ray crystallographic structure of Pml1. This demonstrated that it consists mainly of a FHA domain, a fold which has been shown to mediate interactions with phosphothreonine-containing peptides. Using a new sensitive assay based on alternative splice-site choice, we show, however, that mutation of the putative phosphothreonine-binding pocket of Pml1 does not affect pre-mRNA splicing. We have also investigated how Pml1 integrates into the RES complex. Production of recombinant complexes, combined with serial truncation and mutagenesis of their subunits, indicated that Pml1 binds to Snu17, which itself contacts Bud13. This analysis allowed us to demarcate the binding sites involved in the formation of this assembly. We propose a model of the organization of the RES complex based on these results, and discuss the functional consequences of this architecture.

Present addresses: Andrzej Dziembowski, Department of Genetics and Biotechnology, Warsaw University, Pawinskiego 5a, 02106 Warsaw, Poland Véronique Henriot, Laboratoire d'Enzymologie et Biochimie Structurale, Avenue de la Terrasse, 91190, Gif-sur-Yvette, France


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