The RNA dreamtime: modern cells feature proteins that might have supported a prebiotic polypeptide world but nothing indicates that RNA world ever was.
Modern cells present no signs of a putative prebiotic RNA world. However, RNA coding is not a sine qua non for the accumulation of catalytic polypeptides. Thus, cellular proteins spontaneously fold into active structures that are resistant to proteolysis. The law of mass action suggests that binding domains are stabilized by specific interactions with their substrates. Random polypeptide synthesis in a prebiotic world has the potential to initially produce only a very small fraction of polypeptides that can fold spontaneously into catalytic domains. However, that fraction can be enriched by proteolytic activities that destroy the unfolded polypeptides and regenerate amino acids that can be recycled into polypeptides. In this open system scenario the stable domains that accumulate and the chemical environment in which they are accumulated are linked through self coding of polypeptide structure. Such open polypeptide systems may have been the precursors to the cellular ribonucleoprotein (RNP) world that evolved subsequently.
Kurland
Charles G
CG
Department of Microbial Ecology, University of Lund, Sölvegatan, Lund, Sweden. cgkurland@yahoo.se
D000596:Amino Acids / Q000378:metabolism; D010455:Peptides / Q000378:metabolism*; D014176:Protein Biosynthesis; D011506:Proteins / Q000378:metabolism*; D012313:RNA / Q000378:metabolism*; D012261:Ribonucleoproteins / Q000378:metabolism
D000596:Amino Acids; D010455:Peptides; D011506:Proteins; D012261:Ribonucleoproteins; D012313:RNA