Gordon J, et al. (2011) Reconstitution of CF IA from overexpressed subunits reveals stoichiometry and provides insights into molecular topology. Biochemistry 50(47):10203-14
Abstract: Yeast cleavage factor I (CF I) is an essential complex of five proteins that binds signal sequences at the 3' end of yeast mRNA. CF I is required for correct positioning of a larger protein complex, CPF, which contains the catalytic subunits executing mRNA cleavage and polyadenylation. CF I is composed of two parts, CF IA and Hrp1. The CF IA has only four subunits, Rna14, Rna15, Pcf11, and Clp1, but the structural organization has not been fully established. Using biochemical and biophysical methods, we demonstrate that CF IA can be reconstituted from bacterially expressed proteins and that it has 2:2:1:1 stoichiometry of its four proteins, respectively. We also describe mutations that disrupt the dimer interface of Rna14 while preserving the other subunit interactions. On the basis of our results and existing interaction data, we present a topological model for heterohexameric CF IA and its association with RNA and Hrp1.
|Status: Published||Type: Journal Article | Research Support, N.I.H., Extramural | Research Support, U.S. Gov't, Non-P.H.S.||PubMed ID: 22026644|
Topics addressed in this paper
Number of different genes curated to this paper: 4
- To go to the Locus page for a gene, click on the gene name.
|Topics||Topics not linked to Genes||Genes|
|Non-Fungal Related Genes/Proteins|
|Protein Physical Properties|
|Protein Sequence Features|
|Protein-Nucleic Acid Interactions|
|Protein/Nucleic Acid Structure|