title: 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.
authors.affiliation: Institut Européen de Chimie et Biologie, INSERM U869, 2 rue Robert Escarpit Pessac, F-33607, Université Victor Segalen, Bordeaux 2.
authors.forename: Pierre
authors.initials: P
authors.lastname: Legrand
authors.forename: Noël
authors.initials: N
authors.lastname: Pinaud
authors.forename: Lionel
authors.initials: L
authors.lastname: Minvielle-Sébastia
authors.forename: Sébastien
authors.initials: S
authors.lastname: Fribourg
mesh_terms: D000595:Amino Acid Sequence; D039241:Cleavage Stimulation Factor / Q000737:chemistry* / Q000378:metabolism; D018360:Crystallography, X-Ray; D019281:Dimerization; D009670:Encephalitozoon cuniculi; D005656:Fungal Proteins / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000378:metabolism; D016415:Sequence Alignment; D039221:mRNA Cleavage and Polyadenylation Factors / Q000737:chemistry / Q000378:metabolism
chemical_list: D039241:Cleavage Stimulation Factor; D005656:Fungal Proteins; D029701:Saccharomyces cerevisiae Proteins; D039221:mRNA Cleavage and Polyadenylation Factors; C512638:RNA14 protein, S cerevisiae; C512635:RNA15 protein, S cerevisiae