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

Abstract : 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 A. 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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https://www.hal.inserm.fr/inserm-00175609
Contributor : Sebastien Fribourg <>
Submitted on : Friday, September 28, 2007 - 5:48:06 PM
Last modification on : Tuesday, May 14, 2019 - 3:08:07 PM
Long-term archiving on: : Friday, April 9, 2010 - 3:07:35 AM

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Pierre Legrand, Noël Pinaud, Lionel Minvielle-Sébastia, Sébastien Fribourg. The structure of the CstF-77 homodimer provides insights into CstF assembly.. Nucleic Acids Research, Oxford University Press, 2007, 35 (13), pp.4515-22. ⟨10.1093/nar/gkm458⟩. ⟨inserm-00175609⟩

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