Abstract
Whitepaper #247 submitted to the Planetary Science and Astrobiology Decadal Survey 2023-2032. Topics: life and prebiotic organics; other science themes: Early Evolution; theory, computation, and modeling
Highlights
Can we infer the role of analogy and homology in the fold repertoire of the translation system at and before last universal common ancestor (LUCA); can we infer the basic principle of the sequence regularities, required to form the simplest folds; can we estimate the amount of information required to code for them; can we propose a model for a simple translation system, which is capable of this task? Our understanding of the evolution of the ribosome, and inspection of universal ribosomal proteins reveals a reaction coordinate for the evolution of protein folding that appears imprinted within the ribosome with ribosomal rRNA acting as a molecular cast
Co-evolution of rProteins and tRNA synthetase: Can we identify correlations between evolution of the translational machinery and tRNA synthetases? Can we develop a synchronized evolutionary model for both coding and decoding and map it onto a single timeline? A small number of protein families have a detectable homology tracing back before LUCA, through the presence of related protein families that evolved by gene duplication in the pre-LUCA lineage
Most compellingly, better methods for accurate phylogenetic reconstruction of very ancient protein families may allow the study of pre-LUCA protein families to be extended to protein domains, which would open up an entirely new window into the evolutionary history of life before the LUCA
Summary
Understanding the early biosphere gives us an extended set of features which may be informative of biological processes across a broader time window; currently, we cannot distinguish universal features of life in the universe from those that are quirks of evolutionary history as it occurred on Earth. While the sequence and structure of protein families within each class varies considerably, elements of sequence and structure homology are detectably conserved, and can provide the basis for comparative evolutionary studies, and reconstructing the pre-LUCA history of aminoacylation [O’Donoghue & Luthey-Schulten, 2003].
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