RNA‐binding ability of PIPP in requires the entire protein

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Abstract
Post‐transcriptional fate of eukaryotic mRNAs depends on association with different classes of RNA‐binding proteins (RBPs). Among these proteins, the cold‐shock domain (CSD)‐containing proteins, also called Y‐box proteins, play a key role in controlling the recruitment of mRNA to the translational machinery, in response to environmental cues, both in development and in differentiated cells. We recently cloned a rat cDNA encoding a new CSD‐protein that we called PIPPin. This protein also contains two putative double‐stranded RNA‐binding motifs (PIP1 and PIP2) flanking the central CSD, and is able to bind mRNAs encoding H1° and H3.3 histone variants. In order to clarify the role of each domain in the RNA‐binding activity of PIPPin, we constructed a number of different recombinant vectors, encoding different regions of the protein. Here we report that only recombinant proteins that contain all the putative PIPPin domains show RNA‐binding ability.