6533b821fe1ef96bd127c29b

RESEARCH PRODUCT

RNA-binding ability of PIPP in requires the entire protein

Matilde D'asaroItalia Di LiegroPatrizia ProiaTommaso NastasiLavinia Raimondi

subject

Protein FoldingNerve Tissue ProteinsSequence alignmentRNA-binding proteinPlasma protein bindingArticleRNA-binding proteinscold-shock domainPIPPinhistone variantsHistonesSettore BIO/10 - BiochimicaComplementary DNAHistone H2AAnimalsRNA MessengerGeneticsMessenger RNAbiologyRNA-Binding ProteinsRNACell BiologyRecombinant ProteinsProtein Structure TertiaryRatsCell biologyHistoneGene Expression Regulationbiology.proteinMolecular MedicineSequence AlignmentProtein Binding

description

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 degrees 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.

yearjournalcountryeditionlanguage
2003-05-28Journal of Cellular and Molecular Medicine
https://doi.org/10.1111/j.1582-4934.2003.tb00200.x