Affiliation:
1. N. N. Blokhin National Medical Research Center of Oncology, Ministry of Health of Russia
Abstract
A special hypothetical mechanism of variable Individual Epitope Reverse Translation (at least 2 types) of eukaryotic cell is probably capable of reproducing primary linear (sens- / antisense-, CRISPR-, repeat-like, etc.) and secondary conformational (similar to quadruplexs, RNA-hairpins, RNA-ring-structures; etc.) oligonucleotide structures formed in the mitochondrial membrane-bound supramolecular and containing nanomolecular inclusions hypothetical particle of the retranslosome. This is the so-called nucleic acid equivalents of protein epitope, oligo-NEs, monomeric in ~15–30 and oligomeric in ~(15–30)n nucleotides, potentially capable of participating in the regulation of expression (activation, termination, switching) and modification of genes / genome, as well as in the creation protein / enzyme-containing nucleoprotein platform- / module- / complex-like formations in normal, pathologically altered (in particular, tumor) and virus-infected cells. Recently, in the GenBank databases, they are shown realistically and built / calculated bioinformatically in silico so-called minimum theoretical of 22 nucleotides and longer RNAring (stem-loop) structures, the composition of which depends, firstly, on constantly occurring chemical and enzymatic processes (including deamination mutations), and the properties of which, secondly, link, respectively, with the early (era of the so-called circular code) and later (era of modern universal coding, including the circular code as a component) evolutionary periods of the formation of the whole genetic code. It is generally accepted that the emergence and formation, respectively, of early evolutionary (proto-tRNA, proto-rRNA) and modern variants of molecules of the translational machine of mitochondria and cytoplasm is associated with stem-loop RNA-ring structures, similar to independently proposed oligo-NEs, such as tRNA, rRNA and gene products of ribosomal and other proteins.
Publisher
Publishing House ABV Press