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Nucleic Acids Res. 2007;35(13):4515-22. Epub 2007 Jun 21.

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

Author information

1
Institut Européen de Chimie et Biologie, INSERM U869, 2 rue Robert Escarpit Pessac, F-33607, Université Victor Segalen, Bordeaux 2.

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.

PMID:
17584787
PMCID:
PMC1935011
DOI:
10.1093/nar/gkm458
[Indexed for MEDLINE]
Free PMC Article

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