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RNA. 2011 Mar;17(3):412-8. doi: 10.1261/rna.2481011. Epub 2011 Jan 13.

Hexameric architecture of CstF supported by CstF-50 homodimerization domain structure.

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1
Institut Européen de Chimie et Biologie, Institut National de la Santé et de la Recherche Médicale (INSERM) U869, Pessac, France.

Abstract

The Cleavage stimulation Factor (CstF) complex is composed of three subunits and is essential for pre-mRNA 3'-end processing. CstF recognizes U and G/U-rich cis-acting RNA sequence elements and helps stabilize the Cleavage and Polyadenylation Specificity Factor (CPSF) at the polyadenylation site as required for productive RNA cleavage. Here, we describe the crystal structure of the N-terminal domain of Drosophila CstF-50 subunit. It forms a compact homodimer that exposes two geometrically opposite, identical, and conserved surfaces that may serve as binding platform. Together with previous data on the structure of CstF-77, homodimerization of CstF-50 N-terminal domain supports the model in which the functional state of CstF is a heterohexamer.

PMID:
21233223
PMCID:
PMC3039141
DOI:
10.1261/rna.2481011
[Indexed for MEDLINE]
Free PMC Article
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