Open AccessRNA‐binding ability of PIPP in requires the entire protein
Author(s) -
Raimondi Lavinia,
D'Asaro Matilde,
Proia Patrizia,
Nastasi Tommaso,
Liegro Italia
Publication year - 2003
Publication title -
journal of cellular and molecular medicine
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.44
H-Index - 130
eISSN - 1582-4934
pISSN - 1582-1838
DOI - 10.1111/j.1582-4934.2003.tb00200.x
Subject(s) - rna binding protein , rna , biology , microbiology and biotechnology , genetics , messenger rna , complementary dna , cold shock domain , recombinant dna , computational biology , gene
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 (PIP 1 and PIP 2 ) 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.