Rna14–Rna15 assembly mediates the RNA-binding capability of Saccharomyces cerevisiae cleavage factor IA
AUTOR(ES)
Noble, Christian G.
FONTE
Oxford University Press
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=443540Documentos Relacionados
- Saccharomyces cerevisiae SSB1 protein and its relationship to nucleolar RNA-binding proteins.
- Structure of Hsp15 reveals a novel RNA-binding motif
- The multiple RNA-binding domains of the mRNA poly(A)-binding protein have different RNA-binding activities.
- PUB1 is a major nuclear and cytoplasmic polyadenylated RNA-binding protein in Saccharomyces cerevisiae.
- RNA-binding proteins and their role in the regulation of gene expression in Trypanosoma cruzi and Saccharomyces cerevisiae