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

Pierre Legrand; Noël Pinaud; Lionel Minvielle-Sébastia; Sébastien Fribourg

doi:10.1093/nar/gkm458

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

Nucleic Acids Res. 2007;35(13):4515-22. doi: 10.1093/nar/gkm458. Epub 2007 Jun 21.

Authors

Pierre Legrand¹, Noël Pinaud, Lionel Minvielle-Sébastia, Sébastien Fribourg

Affiliation

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Cleavage Stimulation Factor / chemistry*
Cleavage Stimulation Factor / metabolism
Crystallography, X-Ray
Dimerization
Encephalitozoon cuniculi
Fungal Proteins / chemistry
Fungal Proteins / metabolism
Models, Molecular
Molecular Sequence Data
Saccharomyces cerevisiae Proteins / chemistry
Saccharomyces cerevisiae Proteins / metabolism
Sequence Alignment
mRNA Cleavage and Polyadenylation Factors / chemistry
mRNA Cleavage and Polyadenylation Factors / metabolism

Substances

Cleavage Stimulation Factor
Fungal Proteins
Saccharomyces cerevisiae Proteins
mRNA Cleavage and Polyadenylation Factors
RNA14 protein, S cerevisiae
RNA15 protein, S cerevisiae