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Nucleic Acids Research Advance Access originally published online on June 21, 2007
Nucleic Acids Research 2007 35(13):4515-4522; doi:10.1093/nar/gkm458
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Nucleic Acids Research, 2007, Vol. 35, No. 13 4515-4522
© 2007 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

The structure of the CstF-77 homodimer provides insights into CstF assembly

Pierre Legrand3, Noël Pinaud1,2, Lionel Minvielle-Sébastia2,4 and Sébastien Fribourg1,2,*

1Institut Européen de Chimie et Biologie, INSERM U869, 2 rue Robert Escarpit Pessac, F-33607, 2Université Victor Segalen, Bordeaux 2, 146 rue Léo Saignat, F-33076, 3Synchrotron SOLEIL, L’Orme des Merisiers, Saint-Aubin, B.P. 48, 91192 Gif-sur-Yvette Cedex, and 4Institut de Biochimie et Génétique Cellulaires, CNRS UMR 5095, 1 rue Camille Saint-Saëns, F-33077 Bordeaux cedex

*To whom correspondence should be addressed. Tel: 00 33 (0)5 40 00 30 63; Fax: 00 33 (0)5 40 00 30 68; Email: s.fribourg{at}iecb.u-bordeaux.fr

Received April 10, 2007. Revised May 21, 2007. Accepted May 22, 2007.

The cleavage stimulation factor (CstF) is essential for the first step of poly(A) tail formation at the 3' ends of mRNAs. This heterotrimeric complex is built around the 77-kDa protein bridging both CstF-64 and CstF-50 subunits. We have solved the crystal structure of the 77-kDa protein from Encephalitozoon cuniculi at a resolution of 2 Å. The structure folds around 11 Half-a-TPR repeats defining two domains. The crystal structure reveals a tight homodimer exposing phylogenetically conserved areas for interaction with protein partners. Mapping experiments identify the C-terminal region of Rna14p, the yeast counterpart of CstF-77, as the docking domain for Rna15p, the yeast CstF-64 homologue.


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