메뉴 건너뛰기




Volumn 6, Issue 1, 2017, Pages 39-44

In vitro reconstruction of nonribosomal peptide biosynthesis directly from DNA using cell-free protein synthesis

Author keywords

Biosynthesis; Cell Free Protein Synthesis; Cyclic Dipeptide; Diketopiperazine; Natural Products; Synthetic Biology

Indexed keywords

BACTERIAL DNA; DIPEPTIDE; NONRIBOSOMAL PEPTIDE SYNTHETASE; PIPERAZINEDIONE; CYCLOPEPTIDE; DNA; GRAMICIDIN; PEPTIDE SYNTHASE; PHENYLALANYL-PROLYL DIKETOPIPERAZINE; PIPERAZINE DERIVATIVE;

EID: 85012824047     PISSN: None     EISSN: 21615063     Source Type: Journal    
DOI: 10.1021/acssynbio.6b00160     Document Type: Article
Times cited : (80)

References (38)
  • 3
    • 84934925033 scopus 로고    scopus 로고
    • Reconstitution of metabolic pathways: Insights into nature's chemical logic
    • Lowry, B., Walsh, C. T., and Khosla, C. (2015) Reconstitution of Metabolic Pathways: Insights into Nature's Chemical Logic. Synlett 26, 1008-1025.
    • (2015) Synlett , vol.26 , pp. 1008-1025
    • Lowry, B.1    Walsh, C.T.2    Khosla, C.3
  • 4
    • 33748631825 scopus 로고    scopus 로고
    • Assembly-line enzymology for polyketide and nonribosomal Peptide antibiotics: Logic, machinery, and mechanisms
    • Fischbach, M. A., and Walsh, C. T. (2006) Assembly-line enzymology for polyketide and nonribosomal Peptide antibiotics: logic, machinery, and mechanisms. Chem. Rev. 106, 3468-3496.
    • (2006) Chem. Rev , vol.106 , pp. 3468-3496
    • Fischbach, M.A.1    Walsh, C.T.2
  • 5
    • 84954383343 scopus 로고    scopus 로고
    • Cell-free protein synthesis pros and cons of prokaryotic and eukaryotic systems
    • Zemella, A., Thoring, L., Hoffmeister, C., and Kubick, S. (2015) Cell-Free Protein Synthesis: Pros and Cons of Prokaryotic and Eukaryotic Systems. ChemBioChem 16, 2420-2431.
    • (2015) ChemBioChem , vol.16 , pp. 2420-2431
    • Zemella, A.1    Thoring, L.2    Hoffmeister, C.3    Kubick, S.4
  • 6
    • 84910053480 scopus 로고    scopus 로고
    • Escherichia coli as a cell factory for heterologous production of nonribosomal peptides and polyketides
    • Li, J., and Neubauer, P. (2014) Escherichia coli as a cell factory for heterologous production of nonribosomal peptides and polyketides. New Biotechnol. 31, 579-585.
    • (2014) New Biotechnol , vol.31 , pp. 579-585
    • Li, J.1    Neubauer, P.2
  • 7
    • 84921496822 scopus 로고    scopus 로고
    • Cell-free metabolic engineering: Biomanufacturing beyond the cell
    • Dudley, Q. M., Karim, A. S., and Jewett, M. C. (2015) Cell-free metabolic engineering: biomanufacturing beyond the cell. Biotechnol. J. 10, 69-82.
    • (2015) Biotechnol. J , Issue.10 , pp. 69-82
    • Dudley, Q.M.1    Karim, A.S.2    Jewett, M.C.3
  • 8
    • 79956158054 scopus 로고    scopus 로고
    • Microscale to manufacturing scale-up of cell-free cytokine production-A new approach for shortening protein production development timelines
    • Zawada, J. F., Yin, G., Steiner, A. R., Yang, J., Naresh, A., Roy, S. M., Gold, D. S., Heinsohn, H. G., and Murray, C. J. (2011) Microscale to manufacturing scale-up of cell-free cytokine production-A new approach for shortening protein production development timelines. Biotechnol. Bioeng. 108, 1570-1578.
    • (2011) Biotechnol. Bioeng , vol.108 , pp. 1570-1578
    • Zawada, J.F.1    Yin, G.2    Steiner, A.R.3    Yang, J.4    Naresh, A.5    Roy, S.M.6    Gold, D.S.7    Heinsohn, H.G.8    Murray, C.J.9
  • 9
    • 84899918637 scopus 로고    scopus 로고
    • Linear DNA for rapid prototyping of synthetic biological circuits in an Escherichia coli based TX-TL cell-free system
    • Sun, Z. Z., Yeung, E., Hayes, C. A., Noireaux, V., and Murray, R. M. (2014) Linear DNA for rapid prototyping of synthetic biological circuits in an Escherichia coli based TX-TL cell-free system. ACS Synth. Biol. 3, 387-397.
    • (2014) ACS Synth. Biol , Issue.3 , pp. 387-397
    • Sun, Z.Z.1    Yeung, E.2    Hayes, C.A.3    Noireaux, V.4    Murray, R.M.5
  • 10
    • 84864953230 scopus 로고    scopus 로고
    • Cell-free protein synthesis: Applications come of age
    • Carlson, E. D., Gan, R., Hodgman, C. E., and Jewett, M. C. (2012) Cell-free protein synthesis: Applications come of age. Biotechnol. Adv. 30, 1185-1194.
    • (2012) Biotechnol. Adv , vol.30 , pp. 1185-1194
    • Carlson, E.D.1    Gan, R.2    Hodgman, C.E.3    Jewett, M.C.4
  • 11
    • 83255164998 scopus 로고    scopus 로고
    • Cell-free synthetic biology: Thinking outside the cell
    • Hodgman, C. E., and Jewett, M. C. (2012) Cell-free synthetic biology: Thinking outside the cell. Metab. Eng. 14, 261-269.
    • (2012) Metab. Eng , Issue.14 , pp. 261-269
    • Hodgman, C.E.1    Jewett, M.C.2
  • 12
    • 84874201521 scopus 로고    scopus 로고
    • Integrating cell-free biosyntheses of heme prosthetic group and apoenzyme for the synthesis of functional P450 monooxygenase
    • Kwon, Y. C., Oh, I. S., Lee, N., Lee, K. H., Yoon, Y. J., Lee, E. Y., Kim, B. G., and Kim, D. M. (2013) Integrating cell-free biosyntheses of heme prosthetic group and apoenzyme for the synthesis of functional P450 monooxygenase. Biotechnol. Bioeng. 110, 1193-1200.
    • (2013) Biotechnol. Bioeng , Issue.110 , pp. 1193-1200
    • Kwon, Y.C.1    Oh, I.S.2    Lee, N.3    Lee, K.H.4    Yoon, Y.J.5    Lee, E.Y.6    Kim, B.G.7    Kim, D.M.8
  • 16
    • 84966334405 scopus 로고    scopus 로고
    • The all e coli tx-Tl toolbox 2.0: A platform for cell-free synthetic biology
    • Garamella, J., Marshall, R., Rustad, M., and Noireaux, V. (2016) The All E. coli TX-TL Toolbox 2.0: A Platform for Cell-Free Synthetic Biology. ACS Synth. Biol. 5, 344-355.
    • (2016) ACS Synth. Biol , vol.5 , pp. 344-355
    • Garamella, J.1    Marshall, R.2    Rustad, M.3    Noireaux, V.4
  • 17
    • 84941731930 scopus 로고    scopus 로고
    • Characterizing and prototyping genetic networks with cell-free transcription-Translation reactions
    • Takahashi, M. K., Hayes, C. A., Chappell, J., Sun, Z. Z., Murray, R. M., Noireaux, V., and Lucks, J. B. (2015) Characterizing and prototyping genetic networks with cell-free transcription-Translation reactions. Methods 86, 60-72.
    • (2015) Methods , vol.86 , pp. 60-72
    • Takahashi, M.K.1    Hayes, C.A.2    Chappell, J.3    Sun, Z.Z.4    Murray, R.M.5    Noireaux, V.6    Lucks, J.B.7
  • 18
    • 84966298459 scopus 로고    scopus 로고
    • Engineering transcriptional regulator effector specificity using computational design and in vitro rapid prototyping: Developing a vanillin sensor
    • de Los Santos, E. L., Meyerowitz, J. T., Mayo, S. L., and Murray, R. M. (2016) Engineering Transcriptional Regulator Effector Specificity Using Computational Design and In Vitro Rapid Prototyping: Developing a Vanillin Sensor. ACS Synth. Biol. 5, 287-295.
    • (2016) ACS Synth. Biol , Issue.5 , pp. 287-295
    • De Los Santos, E.L.1    Meyerowitz, J.T.2    Mayo, S.L.3    Murray, R.M.4
  • 19
    • 84957434998 scopus 로고    scopus 로고
    • Cell-free protein synthesis of a cytotoxic cancer therapeutic: Onconase production and a just-Addwater cell-free system
    • Salehi, A. S., Smith, M. T., Bennett, A. M., Williams, J. B., Pitt, W. G., and Bundy, B. C. (2016) Cell-free protein synthesis of a cytotoxic cancer therapeutic: Onconase production and a just-Addwater cell-free system. Biotechnol. J. 11, 274-281.
    • (2016) Biotechnol. J , Issue.11 , pp. 274-281
    • Salehi, A.S.1    Smith, M.T.2    Bennett, A.M.3    Williams, J.B.4    Pitt, W.G.5    Bundy, B.C.6
  • 21
    • 84876382897 scopus 로고    scopus 로고
    • Validation of an entirely in vitro approach for rapid prototyping of DNA regulatory elements for synthetic biology
    • Chappell, J., Jensen, K., and Freemont, P. S. (2013) Validation of an entirely in vitro approach for rapid prototyping of DNA regulatory elements for synthetic biology. Nucleic Acids Res. 41, 3471-3481.
    • (2013) Nucleic Acids Res , vol.41 , pp. 3471-3481
    • Chappell, J.1    Jensen, K.2    Freemont, P.S.3
  • 22
    • 0025898498 scopus 로고
    • Characterization and location of the L-proline activating fragment from the multifunctional gramicidin S synthetase 2
    • Kurotsu, T., Hori, K., Kanda, M., and Saito, Y. (1991) Characterization and location of the L-proline activating fragment from the multifunctional gramicidin S synthetase 2. J. Biochem 109, 763-769.
    • (1991) J. Biochem , vol.109 , pp. 763-769
    • Kurotsu, T.1    Hori, K.2    Kanda, M.3    Saito, Y.4
  • 23
    • 0028830908 scopus 로고
    • Bioactive cyclic dipeptides
    • Prasad, C. (1995) Bioactive cyclic dipeptides. Peptides 16, 151-164.
    • (1995) Peptides , vol.16 , pp. 151-164
    • Prasad, C.1
  • 25
    • 84865007362 scopus 로고    scopus 로고
    • The nonribosomal synthesis of diketopiperazines in tRNA-dependent cyclodipeptide synthase pathways
    • Belin, P., Moutiez, M., Lautru, S., Seguin, J., Pernodet, J. L., and Gondry, M. (2012) The nonribosomal synthesis of diketopiperazines in tRNA-dependent cyclodipeptide synthase pathways. Nat. Prod. Rep. 29, 961-979.
    • (2012) Nat. Prod. Rep , vol.29 , pp. 961-979
    • Belin, P.1    Moutiez, M.2    Lautru, S.3    Seguin, J.4    Pernodet, J.L.5    Gondry, M.6
  • 26
    • 2942560272 scopus 로고    scopus 로고
    • Vivo production of artificial nonribosomal peptide products in the heterologous host Escherichia coli
    • Gruenewald, S., Mootz, H. D., Stehmeier, P., and Stachelhaus, T. (2004) In vivo production of artificial nonribosomal peptide products in the heterologous host Escherichia coli. Appl. Environ. Microbiol. 70, 3282-3291.
    • (2004) Appl. Environ. Microbiol , vol.70 , pp. 3282-3291
    • Gruenewald, S.1    Mootz, H.D.2    Stehmeier, P.3    Stachelhaus, T.4
  • 27
    • 84879209549 scopus 로고    scopus 로고
    • Quorum-sensing inhibitory compounds from extremophilic microorganisms isolated from a hypersaline cyanobacterial mat
    • Abed, R. M., Dobretsov, S., Al-Fori, M., Gunasekera, S. P., Sudesh, K., and Paul, V. J. (2013) Quorum-sensing inhibitory compounds from extremophilic microorganisms isolated from a hypersaline cyanobacterial mat. J. Ind. Microbiol. Biotechnol. 40, 759-772.
    • (2013) J. Ind. Microbiol. Biotechnol , vol.40 , pp. 759-772
    • Abed, R.M.1    Dobretsov, S.2    Al-Fori, M.3    Gunasekera, S.P.4    Sudesh, K.5    Paul, V.J.6
  • 29
    • 53949093950 scopus 로고    scopus 로고
    • An integrated cell-free metabolic platform for protein production and synthetic biology
    • Jewett, M. C., Calhoun, K. A., Voloshin, A., Wuu, J. J., and Swartz, J. R. (2008) An integrated cell-free metabolic platform for protein production and synthetic biology. Mol. Syst. Biol. 4, 220.
    • (2008) Mol. Syst. Biol , vol.4 , pp. 220
    • Jewett, M.C.1    Calhoun, K.A.2    Voloshin, A.3    Wuu, J.J.4    Swartz, J.R.5
  • 30
    • 1542720448 scopus 로고    scopus 로고
    • Mimicking the Escherichia coli cytoplasmic environment activates long-lived and efficient cell-free protein synthesis
    • Jewett, M. C., and Swartz, J. R. (2004) Mimicking the Escherichia coli cytoplasmic environment activates long-lived and efficient cell-free protein synthesis. Biotechnol. Bioeng. 86, 19-26.
    • (2004) Biotechnol. Bioeng , vol.86 , pp. 19-26
    • Jewett, M.C.1    Swartz, J.R.2
  • 31
    • 65549131891 scopus 로고    scopus 로고
    • Mapping the limits of substrate specificity of the adenylation domain of TycA
    • Villiers, B. R., and Hollfelder, F. (2009) Mapping the limits of substrate specificity of the adenylation domain of TycA. ChemBioChem 10, 671-682.
    • (2009) ChemBioChem , vol.10 , pp. 671-682
    • Villiers, B.R.1    Hollfelder, F.2
  • 32
    • 0036161991 scopus 로고    scopus 로고
    • Mutational analysis of the C-domain in nonribosomal peptide synthesis
    • Bergendahl, V., Linne, U., and Marahiel, M. A. (2002) Mutational analysis of the C-domain in nonribosomal peptide synthesis. Eur. J. Biochem. 269, 620-629.
    • (2002) Eur. J. Biochem , vol.269 , pp. 620-629
    • Bergendahl, V.1    Linne, U.2    Marahiel, M.A.3
  • 33
    • 84923876698 scopus 로고    scopus 로고
    • High-Throughput preparation methods of crude extract for robust cell-free protein synthesis
    • Kwon, Y. C., and Jewett, M. C. (2015) High-Throughput preparation methods of crude extract for robust cell-free protein synthesis. Sci. Rep. 5, 8663.
    • (2015) Sci. Rep , Issue.5 , pp. 8663
    • Kwon, Y.C.1    Jewett, M.C.2
  • 35
    • 25144485731 scopus 로고    scopus 로고
    • Parallel interrogation of covalent intermediates in the biosynthesis of gramicidin S using high-resolution mass spectrometry
    • Miller, L. M., Mazur, M. T., McLoughlin, S. M., and Kelleher, N. L. (2005) Parallel interrogation of covalent intermediates in the biosynthesis of gramicidin S using high-resolution mass spectrometry. Protein Sci. 14, 2702-2712.
    • (2005) Protein Sci , Issue.14 , pp. 2702-2712
    • Miller, L.M.1    Mazur, M.T.2    McLoughlin, S.M.3    Kelleher, N.L.4
  • 36
    • 0034673983 scopus 로고    scopus 로고
    • Mutational analysis of the epimerization domain in the initiation module PheATE of gramicidin S synthetase
    • Stachelhaus, T., and Walsh, C. T. (2000) Mutational analysis of the epimerization domain in the initiation module PheATE of gramicidin S synthetase. Biochemistry 39, 5775-5787.
    • (2000) Biochemistry , vol.39 , pp. 5775-5787
    • Stachelhaus, T.1    Walsh, C.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.