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Nucleic Acids Research 2004 32(11):3364-3375; doi:10.1093/nar/gkh664
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Published online 23 June 2004

Nucleic Acids Research, Vol. 32 No. 11 © Oxford University Press 2004; all rights reserved

Rna14–Rna15 assembly mediates the RNA-binding capability of Saccharomyces cerevisiae cleavage factor IA

Christian G. Noble, Philip A. Walker, Lesley J. Calder1 and Ian A. Taylor*

Division of Protein Structure and 1 Division of Virology, National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK

* To whom correspondence should be addressed. Tel: +44 020 88162552; Fax: +44 020 88162580; Email: itaylor{at}nimr.mrc.ac.uk

Received April 20, 2004; Revised May 13, 2004; Accepted June 4, 2004

The Rna14–Rna15 complex is a core component of the cleavage factor IA RNA-processing complex from Saccharomyces cerevisiae. To understand the assembly and RNA-binding properties, we have isolated and characterized the Rna14–Rna15 complex using a combination of biochemical and biophysical methods. Analysis of the purified complex, using transmission electron microscopy, reveals that the two proteins assemble into a kinked rod-shaped structure and that these rods are able to further self-associate. Analytical ultracentrifugation reveals that Rna14 mediates this association and facilitates assembly of an A2B2 tetramer (Mr 230 000), where relatively compact Rna14–Rna15 heterodimers are in rapid equilibrium with tetramers that have a more extended shape. The Rna14–Rna15 complex, unlike the individual components, binds to an RNA oligonucleotide derived from the 3'-untranslated region of the S.cerevisiae GAL7 gene. Based on these structural and thermodynamic data, we propose that CFIA assembly regulates RNA-binding activity.


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