Ribosomes are multi-subunit macromolecules that contribute to the formation of many crucial proteins that maintain a balance of function in many living organisms. They primarily function by translating mRNA’s into their corresponding amino acid sequences. A protein’s correct output of amino acid order and consequently its structure are dependent strongly upon the correct formation of the ribosomal subunits in the particular organism’s ribosome. Degradation or incorrect structural formation of the ribosome can all contribute to an aggregation of protein or improper protein folding that can contribute to a multitude of diseases. This invariably varies among eukaryotic ribosomes, prokaryotic ribosomes, and archaea ribosomes. The entities responsible for the correct formation of the different ribosomal subunits rely heavily on various protein factors and other RNA’s, such as small nucleolar RNA’s (snoRNA’s) as well as non-ribosomal proteins that contribute not only to the proper formation of the ribosome, but its …show more content…
It functions as a pseudouridine N1-methyltransferase (4). It has also been shown to be prevalent in eukaryotic organisms mainly localizing in the nucleolus, making the study of the Nep1 function on the ribosomal SSU advantageous in understanding its analogous function in eukaryotic organisms. The primary function of the Nep1 in yeast facilitates the cleavage process at the D site of the 18s rRNA of the SSU (2). A mutation in the Nep1 protein results in an amino acid change from D86 to glycine which subsequently results in a lethal genetic condition called the Bowen-Conradi syndrome, a childhood developmental disorder that can lead to death (4). MALDI-mass spectrometrical analysis reveals that the methyltransferase activity of Nep1 is highly conserved in the human enzyme