The genetic code, responsible for guiding living organisms in constructing proteins according to their genetic blueprints, might have evolved differently from what researchers previously thought. A newly published research delves into the initial phases of life and proposes an updated schedule for when the components of proteins—known as amino acids—were incorporated into this coding system. Understanding this order is crucial for piecing together the origins of life itself.
Professor Joanna Masel and her colleagues from the University of Arizona introduced a new approach to figure out the order in which amino acids became part of the system that all life uses to make proteins. Their research, published in the scientific journal Proceedings of the National Academy of Sciences, avoids earlier guesses based on the chemicals found on early Earth. Instead, the team looked directly at the protein makeup of very old genetic material that dates back to the earliest known life forms.
Rather than relying on experiments that try to recreate early Earth conditions, Professor Masel's team studied ancient genetic patterns likely shared by the very first organisms. These protein pieces are essential to many life processes and provide clues about how biology functioned billions of years ago. The researchers discovered that simpler, smaller amino acids were used first, while more complex ones came later. Surprisingly, types like methionine and cysteine, which include sulfur, and histidine, which interacts with metals, were added earlier than previously thought.
"Methionine and histidine joined the genetic code sooner than anticipated based on their molecular weights, followed by glutamine," clarified Professor Masel. This suggests that methionine probably had an important function in initial energy-driven activities, whereas histidine's potential for facilitating metallic chemical reactions might have rendered it essential right from the start.
The research outcomes extend past fundamental chemistry; they back up the notion that life originated in mineral- and sulfur-abundant settings like deep-sea hydrothermal vents. Such locations likely offered ideal circumstances for sulfur and metallic chemical reactions. Additionally, Professor Masel’s group discovered evidence indicating that earlier genetic mechanisms predate the common predecessor of all living organisms. This implies that early life forms explored various methods to synthesize proteins prior to adopting the protein-making process used currently.
In order to arrive at their findings, Professor Masel’s group classified segments of proteins based on when they first emerged throughout evolutionary history. These segments, known as domains, represent portions of proteins responsible for executing particular functions within cells. The research team subsequently analyzed the frequency with which various types of amino acids occurred in both more archaic and relatively recent collections of proteins. For instance, they discovered that glutamine might have been incorporated into the genetic blueprint quite tardily, challenging previous beliefs about its timeline. Additionally, certain primordial proteins were observed to possess unusually high concentrations of specific amino acids like tryptophan and tyrosine, suggesting early genetic configurations could function distinctly from what we understand today.
Professor Masel's research offers more than a new view of Earth’s history. It also opens up possibilities for studying life beyond our planet. If sulfur and metal-based amino acids were important in early life here, they could be signs of life in other worlds too. “Our results offer an improved approximation of the order of recruitment of the twenty amino acids into the genetic code,” Professor Masel said, giving scientists a better way to trace how life might start in other parts of the universe.
Journal Reference
Wehbi S., Wheeler A., Morel B., Manepalli N., Minh B.Q., Lauretta D.S., Masel J. “Order of amino acid recruitment into the genetic code resolved by last universal common ancestor's protein domains.” Proceedings of the National Academy of Sciences, 2024. DOI: https://doi.org/10.1073/pnas.2410311121
About the Author

Professor Joanna Masel is a theoretical biologist affiliated with the University of Arizona, renowned for pioneering studies into the development of life’s core mechanisms. Specializing in the genesis of genetic systems, evolutionary principles, and foundational aspects of ancient organisms, they integrate sophisticated mathematical tools with empirical inquiries to reveal historical trends influencing contemporary life forms. As an authority blending expertise in mathematics and evolutionary biology, this professor contributes significantly to unraveling the complexities behind gene function adaptation and change using advanced modeling techniques. Professor Masel has extensively documented advancements across various domains including protein progression and resilience against mutations leading to distinct characteristics. Recognized globally for disrupting conventional beliefs and proposing groundbreaking theories about system modifications throughout species' histories, their scholarly efforts extend beyond publishing; mentoring young scientists and fostering analytical reasoning skills through multidisciplinary collaborations remains equally vital within their professional ethos. Notably, current investigations concerning integration strategies among basic building blocks like amino acids provide insightful clues regarding initial configurations of our present-day coding framework.
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