Abstract
A mechanism for prebiotic translation is proposed in which primeval transfer-RNA (adaptors) are assumed to be permanently associated with messenger nucleic acid molecules. Residual 'fossil' evidences are found to be present within the base sequences of contemporary tRNAs, suggesting the existence of inter-primal-tRNA interactions necessary for the mechanism. The structure of proposed primal-tRNA is such that it can not only choose its own amino acid in the absence of aminoacyl synthetase, but can also associate nonspecifically with adjacent primal-tRNA molecules attached to the neighbouring codons. Such associations can give rise, through cooperative binding between message and adaptors to the 'static template surfaces' which can direct translation of nucleotide sequences into those of amino acids. The origins of ribosomes and contemporary genetic code are suggested by this hypothesis. Proposed structures and processes are thermodynamically compatible. The approximate date of occurrence of the proposed system is calculated, which is consistent with the period of occurrence of the earliest organism with ribosomes.
MeSH Terms
Amino Acids
Anticodon
Bacillus subtilis/analysis
Base Composition
Base Sequence
Biological Evolution
Escherichia coli/analysis
Models, Biological
Nucleic Acid Conformation
Origin of Life
Protein Biosynthesis
RNA, Transfer/physiology
Templates, Genetic
Thermodynamics
Chemicals
Amino Acids
Anticodon
RNA, Transfer
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Tyagi S
References (19)
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