11 September 2015 Ribosome dynamics and the evolutionary history of ribosomes
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The ribosome is a dynamic nanomachine responsible for coded protein synthesis. Its major subsystems were essentially in place at the time of the last universal common ancestor (LUCA). Ribosome evolutionary history thus potentially provides a window into the pre- LUCA world. This history begins with the origins of the peptidyl transferase center where the actual peptide is synthesized and then continues over an extended timeframe as additional functional centers including the GTPase center are added. The large ribosomal RNAs (rRNAs) have grown over time by an accretion process and a model exists that proposes a relative age of each accreted element. We have compared atomic resolution ribosome structures before and after EF-G bound GTP hydrolysis and thereby identified the location of 23 pivot points in the large rRNAs that facilitate ribosome dynamics. Pivots in small subunit helices h28 and h44 appear to be especially central to the process and according to the accretion model significantly older than the other helices containing pivots. Overall, the results suggest that ribosomal dynamics occurred in two phases. In the first phase, an inherently mobile h28/h44 combination provided the flexibility needed to create a dynamic ribosome that was essentially a Brownian machine. This addition likely made coded peptide synthesis possible by facilitating movement of a primitive mRNA. During the second phase, addition of pivoting elements and the creation of a factor binding site allowed the regulation of the inherent motion created by h28/h44. All of these events likely occurred before LUCA.
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George E. Fox, George E. Fox, Maxim Paci, Maxim Paci, Quyen Tran, Quyen Tran, Anton S. Petrov, Anton S. Petrov, Loren D. Williams, Loren D. Williams, } "Ribosome dynamics and the evolutionary history of ribosomes", Proc. SPIE 9606, Instruments, Methods, and Missions for Astrobiology XVII, 96060G (11 September 2015); doi: 10.1117/12.2187098; https://doi.org/10.1117/12.2187098


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