An information-dynamics model of protein-templated DNA synthesis: From qualitative observations to quantitative predictions.
TL;DR
Protein-templated synthesis is thus an instance of information-field self-organization in which a fixed rule set in constraint space drives real-space data toward a unique stationary occupation distribution, a principle formally analogous to those previously validated in DNA sequencing by hybridization and RNA inverse folding.
Abstract
Dr.Pujuan Deng et al. (2026) showed that the bacterial anti-phage reverse transcriptase Drt3b synthesizes strictly alternating poly(AC) DNA without any nucleic acid template. We recast this mechanism within an information-dynamics framework in which the active pocket is a two-state automaton in constraint space and the free-nucleotide pool is real space, coupled by Boltzmann-weighted stochastic selection. The framework yields a closed-form master curve for the alternation-defect rate, from which the wild-type strict alternation and the partial fidelity loss of E26A follow directly. The E26A energetic barrier is calibrated to the experimental defect rate (Δ=2.47 kT); the E26Q product-level dG fraction is calibrated to the reported 10.16% value (giving γG=ln4); R253A and the double mutant are presented as assumption-dependent predictions; and the crossover at which the defect rate falls below 5% is an analytical criterion (Δ≈3.7 kT). Order-sensitive entropy measures distinguish fidelity loss that marginal composition cannot: the marginal entropy remains 1 bit for all A/C-symmetric systems, whereas the conditional entropy rises from 0 to 1 bit. Protein-templated synthesis is thus an instance of information-field self-organization in which a fixed rule set in constraint space drives real-space data toward a unique stationary occupation distribution, a principle formally analogous to those previously validated in DNA sequencing by hybridization and RNA inverse folding.
