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THE BINDING ACTIVITY OF YEAST RNAs TO YEAST hek2p AND MAMMALIAN hnRNP K PROTEINS, DETERMINED USING THE

By Three-hybrid System, Agnieszka Paziewska, Lucjan S. Wyrwicz and Jerzy Ostrowski

Abstract

Abstract: K homology (KH) domains are scaffolds for the binding of RNAs by the heterogeneous nuclear ribonucleoprotein (hnRNP) K protein and its yeast ortholog, Hek2p. KH domains are remarkably conserved between mammals and yeast. To assess the binding activity for yeast RNA of the two proteins, we used full-length K protein and Hek2p as baits in the yeast three-hybrid system. All the unique RNA sequences bound by Hek2p and all but two bound by K protein represented different fragments of only two transcripts, encoded by the 18S and 25S ribosomal RNA genes. Most of them were transcribed from the antisense strand. The RNA-binding activity of K protein was significantly higher than that of Hek2p. These results and those from our previously published reports demonstrate that the specificity of target RNA recognition by both the K protein and Hek2p depends on both RNA-specific sequences and the structure of the protein. Both mammalian K protein and its yeast ortholog may be involved in the regulation of gene expression

Topics: Key Words, Three-Hybrid System, hnRNP K Protein, Yeast Hek2p, Ribosomal RNA, Antisense Transcript
Year: 2005
OAI identifier: oai:CiteSeerX.psu:10.1.1.416.9779
Provided by: CiteSeerX
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