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Measurement and Numerical Modeling of Cell-Free Protein Synthesis: Combinatorial Block-Variants of the PURE System

1
Sciences Department, Roma Tre University, V.le G. Marconi 446, I-00146 Rome, Italy
2
Chemistry Department, University of Bari “Aldo Moro”, Via Orabona 4, I-70125 Bari, Italy
3
DiSTeBA, University of Salento, Ecotekne, I-73100 Lecce, Italy
*
Author to whom correspondence should be addressed.
Received: 30 August 2018 / Revised: 25 September 2018 / Accepted: 11 October 2018 / Published: 14 October 2018
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Abstract

Protein synthesis is at the core of bottom-up construction of artificial cellular mimics. Intriguingly, several reports have revealed that when a transcription–translation (TX–TL) kit is encapsulated inside lipid vesicles (or water-in-oil droplets), high between-vesicles diversity is observed in terms of protein synthesis rate and yield. Stochastic solute partition can be a major determinant of these observations. In order to verify that the variation of TX–TL components concentration brings about a variation of produced protein rate and yield, here we directly measure the performances of the ‘PURE system’ TX–TL kit variants. We report and share the kinetic traces of the enhanced Green Fluorescent Protein (eGFP) synthesis in bulk aqueous phase, for 27 combinatorial block-variants. The eGFP production is a sensitive function of TX–TL components concentration in the explored concentration range. Providing direct evidence that protein synthesis yield and rate actually mirror the TX–TL composition, this study supports the above-mentioned hypothesis on stochastic solute partition, without excluding, however, the contribution of other factors (e.g., inactivation of components). View Full-Text
Keywords: synthetic cells; synthetic biology; in vitro protein synthesis; transcription–translation (TX–TL); extrinsic stochastic effects; solute partition; PURE system synthetic cells; synthetic biology; in vitro protein synthesis; transcription–translation (TX–TL); extrinsic stochastic effects; solute partition; PURE system
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

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Carrara, P.; Altamura, E.; D’Angelo, F.; Mavelli, F.; Stano, P. Measurement and Numerical Modeling of Cell-Free Protein Synthesis: Combinatorial Block-Variants of the PURE System. Data 2018, 3, 41.

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