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Reference: Legrand P, et al. (2007) The structure of the CstF-77 homodimer provides insights into CstF assembly. Nucleic Acids Res 35(13):4515-22

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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.

Reference Type
Journal Article | Research Support, Non-U.S. Gov't
Authors
Legrand P, Pinaud N, Minvielle-Sébastia L, Fribourg S
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