Synthetic Biology: A Bridge between Artificial and Natural Cells
Abstract
:1. Introduction
2. Construction of Artificial Cells
3. Gaps between Artificial and Natural Cells
Synergy between Synthetic Biology and Studies of Artificial Cells
4. Using Synthetic Biology to Shrink the Gaps between Artificial and Natural Cells
4.1. The Design of Genetic Circuits to Control Functions of Artificial Cells
4.2. Non-Genetic Factors That Modulate Gene Expression in Artificial Cellular Systems
4.3. Communication between Artificial Cells and Their Environment
4.4. Replication and Division of Artificial Cells
5. Conclusions and Future Outlook
Acknowledgments
Conflicts of Interest
References and Notes
- Hooke, R. Micrographia: Or Some Physiological Descriptions of Minute Bodies Made by Magnifying Glasses With Observations and Inquiries Thereupon; John Martyn, printer to the Royal Society, and are to be sold at his shop at the Bell a little without Temple Barr. Martin and Allestry, London, UK, 1665.
- Schwann, T. Mikroskopische untersuchungen über die übereinstimmung in der struktur und dem wachstum der tiere und pflanzen. In Klassische Schriften zur Zellenlehre, 2nd ed.; Jahn, I., Ed.; Wissenschaftlicher Verlag Harri Deutsch GmbH: Frankfurt, Germany, 2003. [Google Scholar]
- Chang, T.M. 1957 Report on “method for preparing artificial hemoglobin corpuscles”. Available online: http://www.worldscientific.com/doi/pdf/10.1142/9789812770370_bmatter (accessed on 11 December 2014).
- Noireaux, V.; Maeda, Y.T.; Libchaber, A. Development of an artificial cell, from self-organization to computation and self-reproduction. Proc. Natl. Acad. Sci. USA 2011, 108, 3473–3480. [Google Scholar] [CrossRef] [PubMed]
- Zhang, Y.; Ruder, W.C.; LeDuc, P.R. Artificial cells: Building bioinspired systems using small-scale biology. Trends Biotechnol. 2008, 26, 14–20. [Google Scholar] [CrossRef] [PubMed]
- Wu, F.; Tan, C. The engineering of artificial cellular nanosystems using synthetic biology approaches. Wiley Interdiscip. Rev. Nanomed. Nanobiotechnol. 2014, 6, 369–383. [Google Scholar] [CrossRef] [PubMed]
- Chang, T.M. 50th anniversary of artificial cells: Their role in biotechnology, nanomedicine, regenerative medicine, blood substitutes, bioencapsulation, cell/stem cell therapy and nanorobotics. Artif. Cells Blood Substit. Biotechnol. 2007, 35, 545–554. [Google Scholar] [CrossRef]
- Chang, T.M. From artificial red blood cells, oxygen carriers, and oxygen therapeutics to artificial cells, nanomedicine, and beyond. Artif. Cells Blood Substit. Biotechnol. 2012, 40, 197–199. [Google Scholar] [CrossRef]
- Nomura, S.M.; Kondoh, S.; Asayama, W.; Asada, A.; Nishikawa, S.; Akiyoshi, K. Direct preparation of giant proteo-liposomes by in vitro membrane protein synthesis. J. Biotechnol. 2008, 133, 190–195. [Google Scholar] [CrossRef] [PubMed]
- Kaneda, M.; Nomura, S.M.; Ichinose, S.; Kondo, S.; Nakahama, K.; Akiyoshi, K.; Morita, I. Direct formation of proteo-liposomes by in vitro synthesis and cellular cytosolic delivery with connexin-expressing liposomes. Biomaterials 2009, 30, 3971–3977. [Google Scholar] [CrossRef] [PubMed]
- Moritani, Y.; Nomura, S.M.; Morita, I.; Akiyoshi, K. Direct integration of cell-free-synthesized connexin-43 into liposomes and hemichannel formation. FEBS J. 2010, 277, 3343–3352. [Google Scholar] [CrossRef] [PubMed]
- Liu, Y.J.; Hansen, G.P.; Venancio-Marques, A.; Baigl, D. Cell-free preparation of functional and triggerable giant proteoliposomes. Chembiochem 2013, 14, 2243–2247. [Google Scholar] [CrossRef] [PubMed]
- Yanagisawa, M.; Iwamoto, M.; Kato, A.; Yoshikawa, K.; Oiki, S. Oriented reconstitution of a membrane protein in a giant unilamellar vesicle: Experimental verification with the potassium channel kcsa. J. Am. Chem. Soc. 2011, 133, 11774–11779. [Google Scholar] [CrossRef] [PubMed]
- Long, A.R.; O’Brien, C.C.; Alder, N.N. The cell-free integration of a polytopic mitochondrial membrane protein into liposomes occurs cotranslationally and in a lipid-dependent manner. PLOS ONE 2012, 7. [Google Scholar] [CrossRef] [PubMed]
- Tanaka-Takiguchi, Y.; Itoh, T.; Tsujita, K.; Yamada, S.; Yanagisawa, M.; Fujiwara, K.; Yamamoto, A.; Ichikawa, M.; Takiguchi, K. Physicochemical analysis from real-time imaging of liposome tubulation reveals the characteristics of individual f-bar domain proteins. Langmuir 2013, 29, 328–336. [Google Scholar] [CrossRef] [PubMed]
- Matsubayashi, H.; Kuruma, Y.; Ueda, T. In vitro synthesis of the E. Coli sec translocon from DNA. Angew. Chem. 2014, 53, 7535–7538. [Google Scholar] [CrossRef]
- Hovijitra, N.T.; Wuu, J.J.; Peaker, B.; Swartz, J.R. Cell-free synthesis of functional aquaporin Z in synthetic liposomes. Biotechnol. Bioeng. 2009, 104, 40–49. [Google Scholar] [CrossRef] [PubMed]
- Ritz, S.; Hulko, M.; Zerfass, C.; May, S.; Hospach, I.; Krasteva, N.; Nelles, G.; Sinner, E.K. Cell-free expression of a mammalian olfactory receptor and unidirectional insertion into small unilamellar vesicles (suvs). Biochimie 2013, 95, 1909–1916. [Google Scholar] [CrossRef] [PubMed]
- Kuruma, Y.; Stano, P.; Ueda, T.; Luisi, P.L. A synthetic biology approach to the construction of membrane proteins in semi-synthetic minimal cells. Biochim. Biophys. Acta 2009, 1788, 567–574. [Google Scholar] [CrossRef] [PubMed]
- Tawfik, D.S.; Griffiths, A.D. Man-made cell-like compartments for molecular evolution. Nat. Biotechnol. 1998, 16, 652–656. [Google Scholar] [CrossRef] [PubMed]
- Miller, O.J.; Bernath, K.; Agresti, J.J.; Amitai, G.; Kelly, B.T.; Mastrobattista, E.; Taly, V.; Magdassi, S.; Tawfik, D.S.; Griffiths, A.D. Directed evolution by in vitro compartmentalization. Nat. Methods 2006, 3, 561–570. [Google Scholar] [CrossRef] [PubMed]
- Blain, J.C.; Szostak, J.W. Progress toward synthetic cells. Annu. Rev. Biochem. 2014, 83, 615–640. [Google Scholar] [CrossRef] [PubMed]
- Dzieciol, A.J.; Mann, S. Designs for life: Protocell models in the laboratory. Chem. Soc. Rev. 2012, 41, 79–85. [Google Scholar] [CrossRef] [PubMed]
- Mansy, S.S.; Schrum, J.P.; Krishnamurthy, M.; Tobe, S.; Treco, D.A.; Szostak, J.W. Template-directed synthesis of a genetic polymer in a model protocell. Nature 2008, 454, 122–125. [Google Scholar] [CrossRef] [PubMed]
- Zhu, T.F.; Szostak, J.W. Coupled growth and division of model protocell membranes. J. Am. Chem. Soc. 2009, 131, 5705–5713. [Google Scholar] [CrossRef] [PubMed]
- Schroeder, A.; Goldberg, M.S.; Kastrup, C.; Wang, Y.; Jiang, S.; Joseph, B.J.; Levins, C.G.; Kannan, S.T.; Langer, R.; Anderson, D.G. Remotely activated protein-producing nanoparticles. Nano Lett. 2012, 12, 2685–2689. [Google Scholar] [CrossRef] [PubMed]
- Samad, A.; Sultana, Y.; Aqil, M. Liposomal drug delivery systems: An update review. Curr. Drug Deliv. 2007, 4, 297–305. [Google Scholar] [CrossRef] [PubMed]
- Ganta, S.; Devalapally, H.; Shahiwala, A.; Amiji, M. A review of stimuli-responsive nanocarriers for drug and gene delivery. J. Control. Release 2008, 126, 187–204. [Google Scholar] [CrossRef] [PubMed]
- Agarwal, R.; Iezhitsa, I.; Agarwal, P.; Abdul Nasir, N.A.; Razali, N.; Alyautdin, R.; Ismail, N.M. Liposomes in topical ophthalmic drug delivery: An update. Drug Deliv. 2014. [Google Scholar] [CrossRef]
- Jewett, M.C.; Calhoun, K.A.; Voloshin, A.; Wuu, J.J.; Swartz, J.R. An integrated cell-free metabolic platform for protein production and synthetic biology. Mol. Syst. Biol. 2008, 4. [Google Scholar] [CrossRef]
- Monnard, P.A.; DeClue, M.S.; Ziock, H.J. Organic nano-compartments as biomimetic reactors and protocells. Curr. Nanosci. 2008, 4, 71–87. [Google Scholar] [CrossRef]
- Hammer, D.A.; Kamat, N.P. Towards an artificial cell. FEBS Lett. 2012, 586, 2882–2890. [Google Scholar] [CrossRef] [PubMed]
- Szostak, J.W.; Bartel, D.P.; Luisi, P.L. Synthesizing life. Nature 2001, 409, 387–390. [Google Scholar] [CrossRef] [PubMed]
- Koonin, E.V.; Mushegian, A.R. Complete genome sequences of cellular life forms: Glimpses of theoretical evolutionary genomics. Curr. Opin. Genet. Dev. 1996, 6, 757–762. [Google Scholar] [CrossRef] [PubMed]
- Kolisnychenko, V.; Plunkett, G.; Herring, C.D.; Feher, T.; Posfai, J.; Blattner, F.R.; Posfai, G. Engineering a reduced escherichia coli genome. Genome Res. 2002, 12, 640–647. [Google Scholar] [CrossRef] [PubMed]
- Gil, R.; Sabater-Munoz, B.; Latorre, A.; Silva, F.J.; Moya, A. Extreme genome reduction in buchnera spp.: Toward the minimal genome needed for symbiotic life. Proc. Natl. Acad. Sci. USA 2002, 99, 4454–4458. [Google Scholar] [CrossRef] [PubMed]
- Gil, R.; Silva, F.J.; Pereto, J.; Moya, A. Determination of the core of a minimal bacterial gene set. Microbiol. Mol. Biol. Rev. 2004, 68, 518–537. [Google Scholar] [CrossRef] [PubMed]
- Glass, J.I.; Assad-Garcia, N.; Alperovich, N.; Yooseph, S.; Lewis, M.R.; Maruf, M.; Hutchison, C.A., III; Smith, H.O.; Venter, J.C. Essential genes of a minimal bacterium. Proc. Natl. Acad. Sci. USA 2006, 103, 425–430. [Google Scholar] [CrossRef]
- Luisi, P.L. Chemical aspects of synthetic biology. Chem. Biodivers. 2007, 4, 603–621. [Google Scholar] [CrossRef] [PubMed]
- Vemuri, S.; Rhodes, C.T. Preparation and characterization of liposomes as therapeutic delivery systems: A review. Pharm. Acta Helv. 1995, 70, 95–111. [Google Scholar] [CrossRef] [PubMed]
- Szoka, F., Jr.; Papahadjopoulos, D. Comparative properties and methods of preparation of lipid vesicles (liposomes). Annu. Rev. Biophys. Bioeng. 1980, 9, 467–508. [Google Scholar] [CrossRef] [PubMed]
- Forster, A.C.; Church, G.M. Towards synthesis of a minimal cell. Mol. Syst. Biol. 2006, 2. [Google Scholar] [CrossRef]
- Guido, N.J.; Wang, X.; Adalsteinsson, D.; McMillen, D.; Hasty, J.; Cantor, C.R.; Elston, T.C.; Collins, J.J. A bottom-up approach to gene regulation. Nature 2006, 439, 856–860. [Google Scholar] [CrossRef] [PubMed]
- Chin, J.W. Modular approaches to expanding the functions of living matter. Nat. Chem. Biol. 2006, 2, 304–311. [Google Scholar] [CrossRef] [PubMed]
- Buchler, N.E.; Gerland, U.; Hwa, T. On schemes of combinatorial transcription logic. Proc. Natl. Acad. Sci. USA 2003, 100, 5136–5141. [Google Scholar] [CrossRef] [PubMed]
- Karzbrun, E.; Tayar, A.M.; Noireaux, V.; Bar-Ziv, R.H. Synthetic biology. Programmable on-chip DNA compartments as artificial cells. Science 2014, 345, 829–832. [Google Scholar] [CrossRef] [PubMed]
- Hao, N.; Budnik, B.A.; Gunawardena, J.; O’Shea, E.K. Tunable signal processing through modular control of transcription factor translocation. Science 2013, 339, 460–464. [Google Scholar] [CrossRef] [PubMed]
- Moon, T.S.; Lou, C.; Tamsir, A.; Stanton, B.C.; Voigt, C.A. Genetic programs constructed from layered logic gates in single cells. Nature 2012, 491, 249–253. [Google Scholar] [CrossRef] [PubMed]
- Gibson, D.G.; Glass, J.I.; Lartigue, C.; Noskov, V.N.; Chuang, R.Y.; Algire, M.A.; Benders, G.A.; Montague, M.G.; Ma, L.; Moodie, M.M.; et al. Creation of a bacterial cell controlled by a chemically synthesized genome. Science 2010, 329, 52–56. [Google Scholar] [CrossRef] [PubMed]
- Levskaya, A.; Weiner, O.D.; Lim, W.A.; Voigt, C.A. Spatiotemporal control of cell signalling using a light-switchable protein interaction. Nature 2009, 461, 997–1001. [Google Scholar] [CrossRef] [PubMed]
- Ellis, T.; Wang, X.; Collins, J.J. Diversity-based, model-guided construction of synthetic gene networks with predicted functions. Nat. Biotechnol. 2009, 27, 465–471. [Google Scholar] [CrossRef] [PubMed]
- Nandagopal, N.; Elowitz, M.B. Synthetic biology: Integrated gene circuits. Science 2011, 333, 1244–1248. [Google Scholar] [CrossRef] [PubMed]
- Slusarczyk, A.L.; Lin, A.; Weiss, R. Foundations for the design and implementation of synthetic genetic circuits. Nat. Rev. Genet. 2012, 13, 406–420. [Google Scholar] [CrossRef] [PubMed]
- Brophy, J.A.; Voigt, C.A. Principles of genetic circuit design. Nat. Methods 2014, 11, 508–520. [Google Scholar] [CrossRef] [PubMed]
- Canton, B.; Labno, A.; Endy, D. Refinement and standardization of synthetic biological parts and devices. Nat. Biotechnol. 2008, 26, 787–793. [Google Scholar] [CrossRef] [PubMed]
- Kim, D.M.; Swartz, J.R. Prolonging cell-free protein synthesis with a novel atp regeneration system. Biotechnol. Bioeng. 1999, 66, 180–188. [Google Scholar] [CrossRef] [PubMed]
- Shimizu, Y.; Inoue, A.; Tomari, Y.; Suzuki, T.; Yokogawa, T.; Nishikawa, K.; Ueda, T. Cell-free translation reconstituted with purified components. Nat. Biotechnol. 2001, 19, 751–755. [Google Scholar] [CrossRef] [PubMed]
- Kim, D.M.; Swartz, J.R. Efficient production of a bioactive, multiple disulfide-bonded protein using modified extracts of escherichia coli. Biotechnol. Bioeng. 2004, 85, 122–129. [Google Scholar] [CrossRef] [PubMed]
- Jewett, M.C.; Swartz, J.R. Mimicking the escherichia coli cytoplasmic environment activates long-lived and efficient cell-free protein synthesis. Biotechnol. Bioeng. 2004, 86, 19–26. [Google Scholar] [CrossRef] [PubMed]
- Jewett, M.C.; Swartz, J.R. Substrate replenishment extends protein synthesis with an in vitro translation system designed to mimic the cytoplasm. Biotechnol. Bioeng. 2004, 87, 465–472. [Google Scholar] [CrossRef] [PubMed]
- Noireaux, V.; Bar-Ziv, R.; Godefroy, J.; Salman, H.; Libchaber, A. Toward an artificial cell based on gene expression in vesicles. Phys. Biol. 2005, 2, 1–8. [Google Scholar] [CrossRef] [PubMed]
- Pedersen, A.; Hellberg, K.; Enberg, J.; Karlsson, B.G. Rational improvement of cell-free protein synthesis. New Biotechnol. 2011, 28, 218–224. [Google Scholar] [CrossRef]
- Ichihashi, N.; Matsuura, T.; Kita, H.; Sunami, T.; Suzuki, H.; Yomo, T. Constructing partial models of cells. Cold Spring Harb Perspect Biol. 2010, 2. [Google Scholar] [CrossRef]
- Komili, S.; Silver, P.A. Coupling and coordination in gene expression processes: A systems biology view. Nat. Rev. Genet. 2008, 9, 38–48. [Google Scholar] [CrossRef] [PubMed]
- Li, G.-W.; Berg, O.G.; Elf, J. Effects of macromolecular crowding and DNA looping on gene regulation kinetics. Nat. Phys. 2009, 5, 294–297. [Google Scholar] [CrossRef]
- Tan, C.; Saurabh, S.; Bruchez, M.P.; Schwartz, R.; Leduc, P. Molecular crowding shapes gene expression in synthetic cellular nanosystems. Nat. Nanotechnol. 2013, 8, 602–608. [Google Scholar] [CrossRef] [PubMed]
- Matsuda, H.; Putzel, G.G.; Backman, V.; Szleifer, I. Macromolecular crowding as a regulator of gene transcription. Biophys. J. 2014, 106, 1801–1810. [Google Scholar] [CrossRef] [PubMed]
- Zubay, G. In vitro synthesis of protein in microbial systems. Annu. Rev. Genet. 1973, 7, 267–287. [Google Scholar] [CrossRef] [PubMed]
- Harris, D.C.; Jewett, M.C. Cell-free biology: Exploiting the interface between synthetic biology and synthetic chemistry. Curr. Opin. Biotechnol. 2012, 23, 672–678. [Google Scholar] [CrossRef] [PubMed]
- Oberholzer, T.; Nierhaus, K.H.; Luisi, P.L. Protein expression in liposomes. Biochem. Biophys. Res. Commun. 1999, 261, 238–241. [Google Scholar] [CrossRef] [PubMed]
- Noireaux, V.; Libchaber, A. A vesicle bioreactor as a step toward an artificial cell assembly. Proc. Natl. Acad. Sci. USA 2004, 101, 17669–17674. [Google Scholar] [CrossRef] [PubMed]
- Hamada, S.; Tabuchi, M.; Toyota, T.; Sakurai, T.; Hosoi, T.; Nomoto, T.; Nakatani, K.; Fujinami, M.; Kanzaki, R. Giant vesicles functionally expressing membrane receptors for an insect pheromone. Chem. Commun. 2014, 50, 2958–2961. [Google Scholar] [CrossRef]
- Lentini, R.; Santero, S.P.; Chizzolini, F.; Cecchi, D.; Fontana, J.; Marchioretto, M.; Del Bianco, C.; Terrell, J.L.; Spencer, A.C.; Martini, L.; et al. Integrating artificial with natural cells to translate chemical messages that direct E. Coli behaviour. Nat. Commun. 2014, 5. [Google Scholar] [CrossRef] [PubMed]
- Ishikawa, K.; Sato, K.; Shima, Y.; Urabe, I.; Yomo, T. Expression of a cascading genetic network within liposomes. FEBS Lett. 2004, 576, 387–390. [Google Scholar] [CrossRef] [PubMed]
- Matosevic, S.; Paegel, B.M. Layer-by-layer cell membrane assembly. Nat. Chem. 2013, 5, 958–963. [Google Scholar] [CrossRef] [PubMed]
- Blattner, F.R.; Plunkett, G., III; Bloch, C.A.; Perna, N.T.; Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; Rode, C.K.; Mayhew, G.F.; et al. The complete genome sequence of escherichia coli k-12. Science 1997, 277, 1453–1462. [Google Scholar] [CrossRef] [PubMed]
- Arifuzzaman, M.; Maeda, M.; Itoh, A.; Nishikata, K.; Takita, C.; Saito, R.; Ara, T.; Nakahigashi, K.; Huang, H.C.; Hirai, A.; et al. Large-scale identification of protein-protein interaction of escherichia coli k-12. Genome Res. 2006, 16, 686–691. [Google Scholar] [CrossRef] [PubMed]
- Pramanik, J.; Keasling, J.D. Stoichiometric model of escherichia coli metabolism: Incorporation of growth-rate dependent biomass composition and mechanistic energy requirements. Biotechnol. Bioeng. 1997, 56, 398–421. [Google Scholar] [CrossRef] [PubMed]
- Wallin, E.; von Heijne, G. Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms. Protein Sci. 1998, 7, 1029–1038. [Google Scholar] [CrossRef] [PubMed]
- Travers, A.; Muskhelishvili, G. Bacterial chromatin. Curr. Opin. Genet. Dev. 2005, 15, 507–514. [Google Scholar] [CrossRef] [PubMed]
- Lutkenhaus, J.; Pichoff, S.; Du, S. Bacterial cytokinesis: From z ring to divisome. Cytoskeleton 2012, 69, 778–790. [Google Scholar] [CrossRef] [PubMed]
- Bisicchia, P.; Arumugam, S.; Schwille, P.; Sherratt, D. Minc, mind, and mine drive counter-oscillation of early-cell-division proteins prior to escherichia coli septum formation. mBio 2013, 4. [Google Scholar] [CrossRef]
- Kobori, S.; Ichihashi, N.; Kazuta, Y.; Yomo, T. A controllable gene expression system in liposomes that includes a positive feedback loop. Mol. Biosyst. 2013, 9, 1282–1285. [Google Scholar] [CrossRef] [PubMed]
- Elcock, A.H. Models of macromolecular crowding effects and the need for quantitative comparisons with experiment. Curr. Opin. Struct. Biol. 2010, 20, 196–206. [Google Scholar] [CrossRef] [PubMed]
- Valencia-Burton, M.; Shah, A.; Sutin, J.; Borogovac, A.; McCullough, R.M.; Cantor, C.R.; Meller, A.; Broude, N.E. Spatiotemporal patterns and transcription kinetics of induced rna in single bacterial cells. Proc. Natl. Acad. Sci. USA 2009, 106, 16399–16404. [Google Scholar] [CrossRef] [PubMed]
- Russell, J.H.; Keiler, K.C. Subcellular localization of a bacterial regulatory RNA. Proc. Natl. Acad. Sci. USA 2009, 106, 16405–16409. [Google Scholar] [CrossRef] [PubMed]
- Barrangou, R.; Fremaux, C.; Deveau, H.; Richards, M.; Boyaval, P.; Moineau, S.; Romero, D.A.; Horvath, P. Crispr provides acquired resistance against viruses in prokaryotes. Science 2007, 315, 1709–1712. [Google Scholar] [CrossRef] [PubMed]
- Ruder, W.C.; Lu, T.; Collins, J.J. Synthetic biology moving into the clinic. Science 2011, 333, 1248–1252. [Google Scholar] [CrossRef] [PubMed]
- Attwater, J.; Holliger, P. A synthetic approach to abiogenesis. Nat. Methods 2014, 11, 495–498. [Google Scholar] [CrossRef] [PubMed]
- Lu, T.K.; Khalil, A.S.; Collins, J.J. Next-generation synthetic gene networks. Nat. Biotechnol. 2009, 27, 1139–1150. [Google Scholar] [CrossRef] [PubMed]
- Mukherji, S.; van Oudenaarden, A. Synthetic biology: Understanding biological design from synthetic circuits. Nat. Rev. Genet. 2009, 10, 859–871. [Google Scholar] [PubMed]
- Haseltine, E.L.; Arnold, F.H. Synthetic gene circuits: Design with directed evolution. Annu. Rev. Biophys. Biomol. Struct. 2007, 36, 1–19. [Google Scholar] [CrossRef] [PubMed]
- Ro, D.K.; Paradise, E.M.; Ouellet, M.; Fisher, K.J.; Newman, K.L.; Ndungu, J.M.; Ho, K.A.; Eachus, R.A.; Ham, T.S.; Kirby, J.; et al. Production of the antimalarial drug precursor artemisinic acid in engineered yeast. Nature 2006, 440, 940–943. [Google Scholar] [CrossRef] [PubMed]
- Gardner, T.S.; Cantor, C.R.; Collins, J.J. Construction of a genetic toggle switch in escherichia coli. Nature 2000, 403, 339–342. [Google Scholar] [CrossRef] [PubMed]
- Elowitz, M.B.; Leibler, S. A synthetic oscillatory network of transcriptional regulators. Nature 2000, 403, 335–338. [Google Scholar] [CrossRef] [PubMed]
- Endy, D. Foundations for engineering biology. Nature 2005, 438, 449–453. [Google Scholar] [CrossRef] [PubMed]
- Schwille, P. Bottom-up synthetic biology: Engineering in a tinkerer’s world. Science 2011, 333, 1252–1254. [Google Scholar] [CrossRef] [PubMed]
- Hammer, K.; Mijakovic, I.; Jensen, P.R. Synthetic promoter libraries—Tuning of gene expression. Trends Biotechnol. 2006, 24, 53–55. [Google Scholar] [CrossRef] [PubMed]
- Cox, R.S., III; Surette, M.G.; Elowitz, M.B. Programming gene expression with combinatorial promoters. Mol. Syst. Biol. 2007, 3. [Google Scholar] [CrossRef]
- Thattai, M.; van Oudenaarden, A. Intrinsic noise in gene regulatory networks. Proc. Natl. Acad. Sci. USA 2001, 98, 8614–8619. [Google Scholar] [CrossRef] [PubMed]
- Elowitz, M.B.; Levine, A.J.; Siggia, E.D.; Swain, P.S. Stochastic gene expression in a single cell. Science 2002, 297, 1183–1186. [Google Scholar] [CrossRef] [PubMed]
- Swain, P.S.; Elowitz, M.B.; Siggia, E.D. Intrinsic and extrinsic contributions to stochasticity in gene expression. Proc. Natl. Acad. Sci. USA 2002, 99, 12795–12800. [Google Scholar] [CrossRef] [PubMed]
- Blake, W.J.; Kaern, M.; Cantor, C.R.; Collins, J.J. Noise in eukaryotic gene expression. Nature 2003, 422, 633–637. [Google Scholar] [CrossRef] [PubMed]
- Milo, R.; Shen-Orr, S.; Itzkovitz, S.; Kashtan, N.; Chklovskii, D.; Alon, U. Network motifs: Simple building blocks of complex networks. Science 2002, 298, 824–827. [Google Scholar] [CrossRef] [PubMed]
- Buchler, N.E.; Gerland, U.; Hwa, T. Nonlinear protein degradation and the function of genetic circuits. Proc. Natl. Acad. Sci. USA 2005, 102, 9559–9564. [Google Scholar] [CrossRef] [PubMed]
- Stricker, J.; Cookson, S.; Bennett, M.R.; Mather, W.H.; Tsimring, L.S.; Hasty, J. A fast, robust and tunable synthetic gene oscillator. Nature 2008, 456, 516–519. [Google Scholar] [CrossRef] [PubMed]
- Smith, R.; Tan, C.; Srimani, J.K.; Pai, A.; Riccione, K.A.; Song, H.; You, L. Programmed allee effect in bacteria causes a tradeoff between population spread and survival. Proc. Natl. Acad. Sci. USA 2014, 111, 1969–1974. [Google Scholar] [CrossRef] [PubMed]
- Hooshangi, S.; Thiberge, S.; Weiss, R. Ultrasensitivity and noise propagation in a synthetic transcriptional cascade. Proc. Natl. Acad. Sci. USA 2005, 102, 3581–3586. [Google Scholar] [CrossRef] [PubMed]
- Tamsir, A.; Tabor, J.J.; Voigt, C.A. Robust multicellular computing using genetically encoded nor gates and chemical “wires”. Nature 2011, 469, 212–215. [Google Scholar] [CrossRef] [PubMed]
- Purcell, O.; Lu, T.K. Synthetic analog and digital circuits for cellular computation and memory. Curr. Opin. Biotechnol. 2014, 29, 146–155. [Google Scholar] [CrossRef] [PubMed]
- Saaem, I.; Ma, S.; Quan, J.; Tian, J. Error correction of microchip synthesized genes using surveyor nuclease. Nucleic Acids Res. 2012, 40. [Google Scholar] [CrossRef] [PubMed]
- Martin, V.J.; Pitera, D.J.; Withers, S.T.; Newman, J.D.; Keasling, J.D. Engineering a mevalonate pathway in escherichia coli for production of terpenoids. Nat. Biotechnol. 2003, 21, 796–802. [Google Scholar] [CrossRef] [PubMed]
- Cello, J.; Paul, A.V.; Wimmer, E. Chemical synthesis of poliovirus cdna: Generation of infectious virus in the absence of natural template. Science 2002, 297, 1016–1018. [Google Scholar] [CrossRef] [PubMed]
- Gibson, D.G.; Benders, G.A.; Andrews-Pfannkoch, C.; Denisova, E.A.; Baden-Tillson, H.; Zaveri, J.; Stockwell, T.B.; Brownley, A.; Thomas, D.W.; Algire, M.A.; et al. Complete chemical synthesis, assembly, and cloning of a mycoplasma genitalium genome. Science 2008, 319, 1215–1220. [Google Scholar] [CrossRef] [PubMed]
- Salis, H.M.; Mirsky, E.A.; Voigt, C.A. Automated design of synthetic ribosome binding sites to control protein expression. Nat. Biotechnol. 2009, 27, 946–950. [Google Scholar] [CrossRef] [PubMed]
- Moffet, D.A.; Hecht, M.H. De novo proteins from combinatorial libraries. Chem. Rev. 2001, 101, 3191–3203. [Google Scholar] [CrossRef] [PubMed]
- Hecht, M.H.; Das, A.; Go, A.; Bradley, L.H.; Wei, Y. De novo proteins from designed combinatorial libraries. Protein Sci. 2004, 13, 1711–1723. [Google Scholar] [CrossRef] [PubMed]
- Hilvert, D. Design of protein catalysts. Annu. Rev. Biochem. 2013, 82, 447–470. [Google Scholar] [CrossRef] [PubMed]
- King, N.P.; Bale, J.B.; Sheffler, W.; McNamara, D.E.; Gonen, S.; Gonen, T.; Yeates, T.O.; Baker, D. Accurate design of co-assembling multi-component protein nanomaterials. Nature 2014, 510, 103–108. [Google Scholar] [CrossRef] [PubMed]
- Chen, Y.J.; Dalchau, N.; Srinivas, N.; Phillips, A.; Cardelli, L.; Soloveichik, D.; Seelig, G. Programmable chemical controllers made from DNA. Nat. Nanotechnol. 2013, 8, 755–762. [Google Scholar] [CrossRef] [PubMed]
- Grigoryan, G.; Kim, Y.H.; Acharya, R.; Axelrod, K.; Jain, R.M.; Willis, L.; Drndic, M.; Kikkawa, J.M.; DeGrado, W.F. Computational design of virus-like protein assemblies on carbon nanotube surfaces. Science 2011, 332, 1071–1076. [Google Scholar] [CrossRef] [PubMed]
- Appella, D.H. Non-natural nucleic acids for synthetic biology. Curr. Opin. Chem. Biol. 2009, 13, 687–696. [Google Scholar] [CrossRef] [PubMed]
- Hyrup, B.; Nielsen, P.E. Peptide nucleic acids (PNA): Synthesis, properties and potential applications. Bioorg. Med. Chem. 1996, 4, 5–23. [Google Scholar] [CrossRef] [PubMed]
- Hohsaka, T.; Sisido, M. Incorporation of non-natural amino acids into proteins. Curr. Opin. Chem. Biol. 2002, 6, 809–815. [Google Scholar] [CrossRef] [PubMed]
- Link, A.J.; Mock, M.L.; Tirrell, D.A. Non-canonical amino acids in protein engineering. Curr. Opin. Biotechnol. 2003, 14, 603–609. [Google Scholar] [CrossRef] [PubMed]
- Siwy, Z.; Trofin, L.; Kohli, P.; Baker, L.A.; Trautmann, C.; Martin, C.R. Protein biosensors based on biofunctionalized conical gold nanotubes. J. Am. Chem. Soc. 2005, 127, 5000–5001. [Google Scholar] [CrossRef] [PubMed]
- Fan, R.; Karnik, R.; Yue, M.; Li, D.; Majumdar, A.; Yang, P. DNA translocation in inorganic nanotubes. Nano Lett. 2005, 5, 1633–1637. [Google Scholar] [CrossRef] [PubMed]
- Kowalczyk, S.W.; Blosser, T.R.; Dekker, C. Biomimetic nanopores: Learning from and about nature. Trends Biotechnol. 2011, 29, 607–614. [Google Scholar] [CrossRef] [PubMed]
- Keasling, J.D. Synthetic biology and the development of tools for metabolic engineering. Metab. Eng. 2012, 14, 189–195. [Google Scholar] [CrossRef] [PubMed]
- Cameron, D.E.; Bashor, C.J.; Collins, J.J. A brief history of synthetic biology. Nat. Rev. Microbiol. 2014, 12, 381–390. [Google Scholar] [CrossRef] [PubMed]
- Ma, S.; Tang, N.; Tian, J. DNA synthesis, assembly and applications in synthetic biology. Curr. Opin. Chem. Biol. 2012, 16, 260–267. [Google Scholar] [CrossRef] [PubMed]
- Kosuri, S.; Church, G.M. Large-scale de novo DNA synthesis: Technologies and applications. Nat. Methods 2014, 11, 499–507. [Google Scholar] [CrossRef] [PubMed]
- Annaluru, N.; Muller, H.; Mitchell, L.A.; Ramalingam, S.; Stracquadanio, G.; Richardson, S.M.; Dymond, J.S.; Kuang, Z.; Scheifele, L.Z.; Cooper, E.M.; et al. Total synthesis of a functional designer eukaryotic chromosome. Science 2014, 344, 55–58. [Google Scholar] [CrossRef] [PubMed]
- Smolke, C.D.; Silver, P.A. Informing biological design by integration of systems and synthetic biology. Cell 2011, 144, 855–859. [Google Scholar] [CrossRef] [PubMed]
- Hillson, N.J.; Rosengarten, R.D.; Keasling, J.D. J5 DNA assembly design automation software. ACS Synth. Biol. 2012, 1, 14–21. [Google Scholar] [CrossRef] [PubMed]
- Rodrigo, G.; Jaramillo, A. Autobiocad: Full biodesign automation of genetic circuits. ACS Synth. Biol. 2013, 2, 230–236. [Google Scholar] [CrossRef] [PubMed]
- Schomburg, I.; Chang, A.; Placzek, S.; Sohngen, C.; Rother, M.; Lang, M.; Munaretto, C.; Ulas, S.; Stelzer, M.; Grote, A.; et al. Brenda in 2013: Integrated reactions, kinetic data, enzyme function data, improved disease classification: New options and contents in brenda. Nucleic Acids Res. 2013, 41, D764–D772. [Google Scholar] [CrossRef] [PubMed]
- McClymont, K.; Soyer, O.S. Metabolic tinker: An online tool for guiding the design of synthetic metabolic pathways. Nucleic Acids Res. 2013, 41. [Google Scholar] [CrossRef] [PubMed]
- Carbonell, P.; Parutto, P.; Herisson, J.; Pandit, S.B.; Faulon, J.L. Xtms: Pathway design in an extended metabolic space. Nucleic Acids Res. 2014, 42, W389–W394. [Google Scholar] [CrossRef] [PubMed]
- Huynh, L.; Tsoukalas, A.; Koppe, M.; Tagkopoulos, I. Sbrome: A scalable optimization and module matching framework for automated biosystems design. ACS Synth. Biol. 2013, 2, 263–273. [Google Scholar] [CrossRef] [PubMed]
- Alves, R.; Antunes, F.; Salvador, A. Tools for kinetic modeling of biochemical networks. Nat. Biotechnol. 2006, 24, 667–672. [Google Scholar] [CrossRef] [PubMed]
- Oberholzer, T.; Albrizio, M.; Luisi, P.L. Polymerase chain reaction in liposomes. Chem. Biol. 1995, 2, 677–682. [Google Scholar] [CrossRef] [PubMed]
- Chakrabarti, A.C.; Breaker, R.R.; Joyce, G.F.; Deamer, D.W. Production of RNA by a polymerase protein encapsulated within phospholipid vesicles. J. Mol. Evol. 1994, 39, 555–559. [Google Scholar] [CrossRef] [PubMed]
- Yu, W.; Sato, K.; Wakabayashi, M.; Nakaishi, T.; Ko-Mitamura, E.P.; Shima, Y.; Urabe, I.; Yomo, T. Synthesis of functional protein in liposome. J. Biosci. Bioeng. 2001, 92, 590–593. [Google Scholar] [CrossRef] [PubMed]
- Bode, J.; Goetze, S.; Heng, H.; Krawetz, S.A.; Benham, C. From DNA structure to gene expression: Mediators of nuclear compartmentalization and dynamics. Chromosome Res. 2003, 11, 435–445. [Google Scholar] [CrossRef] [PubMed]
- Kohwi, Y.; Kohwi-Shigematsu, T. Altered gene expression correlates with DNA structure. Genes Dev. 1991, 5, 2547–2554. [Google Scholar] [CrossRef] [PubMed]
- Aldaye, F.A.; Senapedis, W.T.; Silver, P.A.; Way, J.C. A structurally tunable DNA-based extracellular matrix. J. Am. Chem. Soc. 2010, 132, 14727–14729. [Google Scholar] [CrossRef] [PubMed]
- Wang, W.; Li, G.W.; Chen, C.; Xie, X.S.; Zhuang, X. Chromosome organization by a nucleoid-associated protein in live bacteria. Science 2011, 333, 1445–1449. [Google Scholar] [CrossRef] [PubMed]
- Higgins, C.F.; Dorman, C.J.; Stirling, D.A.; Waddell, L.; Booth, I.R.; May, G.; Bremer, E. A physiological role for DNA supercoiling in the osmotic regulation of gene expression in s. Typhimurium and E. Coli. Cell 1988, 52, 569–584. [Google Scholar] [CrossRef] [PubMed]
- Chen, H.; Li, B.; Workman, J.L. A histone-binding protein, nucleoplasmin, stimulates transcription factor binding to nucleosomes and factor-induced nucleosome disassembly. EMBO J. 1994, 13, 380–390. [Google Scholar] [PubMed]
- Kuo, M.H.; Allis, C.D. Roles of histone acetyltransferases and deacetylases in gene regulation. BioEssays 1998, 20, 615–626. [Google Scholar] [CrossRef] [PubMed]
- Zimmerman, S.B.; Trach, S.O. Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of escherichia coli. J. Mol. Biol. 1991, 222, 599–620. [Google Scholar] [CrossRef] [PubMed]
- Dix, J.A.; Verkman, A.S. Crowding effects on diffusion in solutions and cells. Annu. Rev. Biophys. 2008, 37, 247–263. [Google Scholar] [CrossRef] [PubMed]
- Spitzer, J.; Poolman, B. The role of biomacromolecular crowding, ionic strength, and physicochemical gradients in the complexities of life's emergence. Microbiol. Mol. Biol. Rev. 2009, 73, 371–388. [Google Scholar] [CrossRef] [PubMed]
- McGuffee, S.R.; Elcock, A.H. Diffusion, crowding & protein stability in a dynamic molecular model of the bacterial cytoplasm. PLOS Comput. Biol. 2010, 6. [Google Scholar] [CrossRef]
- Mika, J.T.; Poolman, B. Macromolecule diffusion and confinement in prokaryotic cells. Curr. Opin. Biotechnol. 2011, 22, 117–126. [Google Scholar] [CrossRef] [PubMed]
- Morelli, M.J.; Allen, R.J.; Wolde, P.R. Effects of macromolecular crowding on genetic networks. Biophys. J. 2011, 101, 2882–2891. [Google Scholar] [CrossRef] [PubMed]
- Klumpp, S.; Scott, M.; Pedersen, S.; Hwa, T. Molecular crowding limits translation and cell growth. Proc. Natl. Acad. Sci. USA 2013, 110, 16754–16759. [Google Scholar] [CrossRef] [PubMed]
- Minton, A.P. Implications of macromolecular crowding for protein assembly. Curr. Opin. Struct. Biol. 2000, 10, 34–39. [Google Scholar] [CrossRef] [PubMed]
- Zhou, H.X.; Rivas, G.; Minton, A.P. Macromolecular crowding and confinement: Biochemical, biophysical, and potential physiological consequences. Annu. Rev. Biophys. 2008, 37, 375–397. [Google Scholar] [CrossRef] [PubMed]
- Miyoshi, D.; Sugimoto, N. Molecular crowding effects on structure and stability of DNA. Biochimie 2008, 90, 1040–1051. [Google Scholar] [CrossRef] [PubMed]
- Cheung, M.S.; Klimov, D.; Thirumalai, D. Molecular crowding enhances native state stability and refolding rates of globular proteins. Proc. Natl. Acad. Sci. USA 2005, 102, 4753–4758. [Google Scholar] [CrossRef] [PubMed]
- Stagg, L.; Zhang, S.Q.; Cheung, M.S.; Wittung-Stafshede, P. Molecular crowding enhances native structure and stability of alpha/beta protein flavodoxin. Proc. Natl. Acad. Sci. USA 2007, 104, 18976–18981. [Google Scholar] [CrossRef] [PubMed]
- Guthold, M.; Zhu, X.; Rivetti, C.; Yang, G.; Thomson, N.H.; Kasas, S.; Hansma, H.G.; Smith, B.; Hansma, P.K.; Bustamante, C. Direct observation of one-dimensional diffusion and transcription by escherichia coli RNA polymerase. Biophys. J. 1999, 77, 2284–2294. [Google Scholar] [CrossRef] [PubMed]
- Richter, K.; Nessling, M.; Lichter, P. Macromolecular crowding and its potential impact on nuclear function. Biochim. Biophys. Acta 2008, 1783, 2100–2107. [Google Scholar] [CrossRef] [PubMed]
- Bancaud, A.; Huet, S.; Daigle, N.; Mozziconacci, J.; Beaudouin, J.; Ellenberg, J. Molecular crowding affects diffusion and binding of nuclear proteins in heterochromatin and reveals the fractal organization of chromatin. EMBO J. 2009, 28, 3785–3798. [Google Scholar] [CrossRef] [PubMed]
- Macnab, R.M. Microbiology. Action at a distance—Bacterial flagellar assembly. Science 2000, 290, 2086–2087. [Google Scholar] [CrossRef] [PubMed]
- Takai, K.; Sawasaki, T.; Endo, Y. Practical cell-free protein synthesis system using purified wheat embryos. Nat. Protoc. 2010, 5, 227–238. [Google Scholar] [CrossRef] [PubMed]
- Pelham, H.R.; Jackson, R.J. An efficient mRNA-dependent translation system from reticulocyte lysates. Eur. J. Biochem. 1976, 67, 247–256. [Google Scholar] [CrossRef] [PubMed]
- Ge, X.; Luo, D.; Xu, J. Cell-free protein expression under macromolecular crowding conditions. PLOS ONE 2011, 6. [Google Scholar] [CrossRef] [PubMed]
- Sokolova, E.; Spruijt, E.; Hansen, M.M.; Dubuc, E.; Groen, J.; Chokkalingam, V.; Piruska, A.; Heus, H.A.; Huck, W.T. Enhanced transcription rates in membrane-free protocells formed by coacervation of cell lysate. Proc. Natl. Acad. Sci. USA 2013, 110, 11692–11697. [Google Scholar] [CrossRef] [PubMed]
- Fujiwara, K.; Nomura, S.M. Condensation of an additive-free cell extract to mimic the conditions of live cells. PLOS ONE 2013, 8. [Google Scholar] [CrossRef] [PubMed]
- Martini, L.; Mansy, S.S. Cell-like systems with riboswitch controlled gene expression. Chem. Commun. 2011, 47, 10734–10736. [Google Scholar] [CrossRef]
- Berclaz, N.; Müller, M.; Walde, P.; Luisi, P.L. Growth and transformation of vesicles studied by ferritin labeling and cryotransmission electron microscopy. J. Phys. Chem. B 2000, 105, 1056–1064. [Google Scholar] [CrossRef]
- Budin, I.; Szostak, J.W. Physical effects underlying the transition from primitive to modern cell membranes. Proc. Natl. Acad. Sci. USA 2011, 108, 5249–5254. [Google Scholar] [CrossRef] [PubMed]
- Maeda, Y.T.; Nakadai, T.; Shin, J.; Uryu, K.; Noireaux, V.; Libchaber, A. Assembly of mreb filaments on liposome membranes: A synthetic biology approach. ACS Synth. Biol. 2012, 1, 53–59. [Google Scholar] [CrossRef] [PubMed]
- Osawa, M.; Anderson, D.E.; Erickson, H.P. Reconstitution of contractile ftsz rings in liposomes. Science 2008, 320, 792–794. [Google Scholar] [CrossRef] [PubMed]
- Shin, J.; Jardine, P.; Noireaux, V. Genome replication, synthesis, and assembly of the bacteriophage t7 in a single cell-free reaction. ACS Synth. Biol. 2012, 1, 408–413. [Google Scholar] [CrossRef] [PubMed]
- Kobayashi, T.; Nakamura, Y.; Mikami, S.; Masutani, M.; Machida, K.; Imataka, H. Synthesis of encephalomyocarditis virus in a cell-free system: From DNA to RNA virus in one tube. Biotechnol. Lett. 2012, 34, 67–73. [Google Scholar] [CrossRef] [PubMed]
- Gorter, E.; Grendel, F. On bimolecular layers of lipoids on the chromocytes of the blood. J. Exp. Med. 1925, 41, 439–443. [Google Scholar] [CrossRef] [PubMed]
- Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, A.R.; Sutton, G.; Kelley, J.M.; et al. The minimal gene complement of mycoplasma genitalium. Science 1995, 270, 397–403. [Google Scholar] [CrossRef] [PubMed]
- Demir, E.; Babur, O.; Dogrusoz, U.; Gursoy, A.; Nisanci, G.; Cetin-Atalay, R.; Ozturk, M. Patika: An integrated visual environment for collaborative construction and analysis of cellular pathways. Bioinformatics 2002, 18, 996–1003. [Google Scholar] [CrossRef] [PubMed]
- Krishnamurthy, L.; Nadeau, J.; Ozsoyoglu, G.; Ozsoyoglu, M.; Schaeffer, G.; Tasan, M.; Xu, W. Pathways database system: An integrated system for biological pathways. Bioinformatics 2003, 19, 930–937. [Google Scholar] [CrossRef] [PubMed]
- Demir, E.; Babur, O.; Dogrusoz, U.; Gursoy, A.; Ayaz, A.; Gulesir, G.; Nisanci, G.; Cetin-Atalay, R. An ontology for collaborative construction and analysis of cellular pathways. Bioinformatics 2004, 20, 349–356. [Google Scholar] [CrossRef] [PubMed]
- Holford, M.; Li, N.; Nadkarni, P.; Zhao, H. Vitapad: Visualization tools for the analysis of pathway data. Bioinformatics 2005, 21, 1596–1602. [Google Scholar] [CrossRef] [PubMed]
- Busso, D.; Delagoutte-Busso, B.; Moras, D. Construction of a set gateway-based destination vectors for high-throughput cloning and expression screening in escherichia coli. Anal. Biochem. 2005, 343, 313–321. [Google Scholar] [CrossRef] [PubMed]
- Richmond, K.E.; Li, M.H.; Rodesch, M.J.; Patel, M.; Lowe, A.M.; Kim, C.; Chu, L.L.; Venkataramaian, N.; Flickinger, S.F.; Kaysen, J.; et al. Amplification and assembly of chip-eluted DNA (aaced): A method for high-throughput gene synthesis. Nucleic Acids Res. 2004, 32, 5011–5018. [Google Scholar] [CrossRef] [PubMed]
- Tian, J.; Ma, K.; Saaem, I. Advancing high-throughput gene synthesis technology. Mol. Biosyst. 2009, 5, 714–722. [Google Scholar] [CrossRef] [PubMed]
- Gibson, D.G.; Young, L.; Chuang, R.Y.; Venter, J.C.; Hutchison, C.A., III; Smith, H.O. Enzymatic assembly of DNA molecules up to several hundred kilobases. Nat. Methods 2009, 6, 343–345. [Google Scholar] [CrossRef] [PubMed]
- Trinh, C.T.; Wlaschin, A.; Srienc, F. Elementary mode analysis: A useful metabolic pathway analysis tool for characterizing cellular metabolism. Appl. Microbiol. Biotechnol. 2009, 81, 813–826. [Google Scholar] [CrossRef] [PubMed]
- Stemmer, W.P. DNA shuffling by random fragmentation and reassembly: In vitro recombination for molecular evolution. Proc. Natl. Acad. Sci. USA 1994, 91, 10747–10751. [Google Scholar] [CrossRef] [PubMed]
- Neylon, C. Chemical and biochemical strategies for the randomization of protein encoding DNA sequences: Library construction methods for directed evolution. Nucleic Acids Res. 2004, 32, 1448–1459. [Google Scholar] [CrossRef] [PubMed]
- Matosevic, S.; Paegel, B.M. Stepwise synthesis of giant unilamellar vesicles on a microfluidic assembly line. J. Am. Chem. Soc. 2011, 133, 2798–2800. [Google Scholar] [CrossRef] [PubMed]
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Ding, Y.; Wu, F.; Tan, C. Synthetic Biology: A Bridge between Artificial and Natural Cells. Life 2014, 4, 1092-1116. https://doi.org/10.3390/life4041092
Ding Y, Wu F, Tan C. Synthetic Biology: A Bridge between Artificial and Natural Cells. Life. 2014; 4(4):1092-1116. https://doi.org/10.3390/life4041092
Chicago/Turabian StyleDing, Yunfeng, Fan Wu, and Cheemeng Tan. 2014. "Synthetic Biology: A Bridge between Artificial and Natural Cells" Life 4, no. 4: 1092-1116. https://doi.org/10.3390/life4041092