Self-propagating beta-sheet polypeptide structures as prebiotic informational molecular entities: the amyloid world.
The idea is advanced that under the extreme earth conditions for ~3.9 billions years ago, protein-based beta-sheet molecular structures were the first self-propagating and information-processing biomolecules that evolved. The amyloid structure of these aggregates provided an effective protection against the harsh conditions known to decompose both polyribonucleotides and natively folded polypeptides. In the prebiotic amyloid world, both the replicative and informational functions were carried out by structurally stable beta-sheet protein aggregates in a prion-like mode involving templated self-propagation and storage of information in the beta-sheet conformation. In this amyloid (protein)-first, hybrid replication-metabolism view, the synthesis of RNA, and the evolvement of an RNA-protein world, were later, but necessary events for further biomolecular evolution to occur. I further argue that in our contemporary DNA<-->RNA-->protein world, the primordial beta-conformation-based information system is preserved in the form of a cytoplasmic epigenetic memory.
Maury
C P J
CP
Department of Medicine, University of Helsinki, Kasarmikatu 11-13, Helsinki FI-00130, Finland. peter.maury@hus.fi
D000682:Amyloid / Q000737:chemistry*; D019143:Evolution, Molecular; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D011328:Prions / Q000737:chemistry; D011487:Protein Conformation
D000682:Amyloid; D010455:Peptides; D011328:Prions