Researchers at University College London discovered that aminoacyl-thiols can link amino acids to RNA without enzymes, offering insights into the origins of life [date of publication not available].
The study, published in Nature, demonstrates that this process occurs in water, mimicking conditions on early Earth.
Aminoacyl-thiol chemistry surprisingly favors RNA over more reactive molecules, showcasing unexpected selectivity.
A simple chemical switch can separate the two key stages of modern protein synthesis: RNA-charging and peptide-linking.
Detailed Insights:
The discovery addresses the chicken-and-egg problem of how RNA and proteins partnered in early life, given that enzymes (proteins) are needed to load amino acids onto RNA, but enzymes themselves are proteins.
Aminoacyl-thiols may have provided RNA with a chemical advantage, paving the way for the first steps of protein synthesis.
The reaction's precision allows amino acids to attach to RNA ends in a manner similar to how life functions today.
Thioesters may have played a role in guiding amino acids onto RNA, rather than directly creating peptides.
Aminoacyl-thiols can form from simple precursors like nitriles and thiols even in frigid conditions, suggesting the process could have occurred in various environments on early Earth.
Converting thioesters into thioacids flips the chemistry, favoring the formation of peptide bonds, enabling both RNA-charging and peptide-linking in the same solution under different chemical modes.
Scientific/Technical Concepts Involved:
RNA (Ribonucleic Acid): A molecule that stores instructions for building proteins and plays various roles in gene expression.
Amino Acids: The building blocks of proteins, linked together in a specific order determined by RNA.
Enzymes: Proteins that catalyze (speed up) biochemical reactions in cells.