Abstrait

Molecular priming of a ribosome-inactivating protein sequence and identification of its structural homologywithRNA-binding proteins

Ashraf Gholizadeh

A partial cDNA containing putative conserved sequence of ribosomeinactivating proteinswas primed fromCelosia cristata leaf cDNApopulation and its structure was compared with that of RNA-binding proteins by using bioinformatics tools. As an initial report, the significant homology was identified between the primary and tertiary structures of the isolated RIP domain containing cDNA fragment and RBP. Based on the structural homology results as well as the functional similarity between RIP and RBP in relation to RNA molecule processing and translational gene regulation and inhibition, it was proposed that RIPs may be a specific group of RBPs which target 23s ribosomal RNA and inhibit translation process possibly through the overlappingmechanisms or by exhibiting the differentmode of actions but with the same outcomes. The amplified cDNA sequence was submitted to EMBL databases under accession number HF562933.