Journal of Nutraceuticals and Food Science

Editorial

The macromolecular partnership that has ruled the biological planet for over 4 billion years is based on the translation of mRNA to protein, which offers a template for the shared origin and interconnectedness of all living systems. Three-dimensional structures of ribosomes from throughout the tree of life show macromolecules from deep biological history and serve as a guide to biopolymer pre-biological evolution. Ribosomal RNAs (rRNAs) and ribosomal Proteins (rProteins) are molecular fossils that date back to before the last universal common ancestor of life. rRNA recursively accreted and froze, growing in bulk over time, according to the previously established Accretion Model of ribosomal development. RNA folding, noncoded condensation of amino acids to create peptides, subunit association, correlated subunit evolution and decoding, and energy transduction were all gained progressively by the ribosome. In prokaryotes, rRNA growth is divided into six stages, with two extra eukaryotic phases. The most ancient rRNA is found in the first phase, whereas the most recent rRNA is found in the last phase. The expansion and development of the exit tunnel is a recurring motif in ribosome evolution Phases 1-6.

• By showing temporal connections between acquisition of rRNA elements and acquisition of rProtein segments, we include rProteins into the Accretion Model of ribosomal evolution. The age of a particular segment of rProtein is assumed to be the same as the age of the rRNA with which it interacts in these relationships. The results are used to put the Accretion Model to the test. This expansion of the Accretion Model allows us to create a “movie” of protein evolution at the molecular level. The temporal mapping of rRNA to rProtein gives frames of a movie that imply gradual and hierarchical protein evolution. The animation depicts the development of protein domains one by one

• Short Random Coil (RC) peptides bind to rRNA at first

• Peptides lengthened and consolidated into secondary components, with b–b structures outnumbering a-helices

• Secondary elements of polypeptides accumulated and compressed into domains predominantly made up of b-strands

• Protein domains developed progressively complicated supersecondary structures made up of a combination of a-helices and b-strands

Interactions with rRNA directed and accelerated the development of proteins. The polypeptide was submerged in rRNA throughout the procedure. RNA folding developed at the same time as protein folding.

Many people have pointed out how unlikely it is for two fundamentally distinct biopolymers like RNA and protein to arise concurrently and independently. It appears that either RNA or protein originated first. With a single polymer, the RNA World gives one answer to the issue of who came first. The findings suggest that RNA and protein evolution did not occur independently; rather, they co-evolved. The near-simultaneous development of RNA and protein in an emergent environment in which one polymer chaperoned the evolution of the other. The chicken and egg problem is solved by linking the development of RNA and protein backbone and side-chain elements.