메뉴 건너뛰기




Volumn 13, Issue 12, 2017, Pages 1253-1260

Erratum: Continuous directed evolution of aminoacyl-tRNA synthetases (Nature Chemical Biology (2017) 13 (1253-1260) DOI: 10.1038/nchembio.2474);Continuous directed evolution of aminoacyl-tRNA synthetases

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; AMINO ACID TRANSFER RNA LIGASE; TYROSINE TRANSFER RNA LIGASE; PROTEIN;

EID: 85034865436     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio0218-186     Document Type: Erratum
Times cited : (190)

References (46)
  • 1
    • 77953643054 scopus 로고    scopus 로고
    • Adding new chemistries to the genetic code
    • Liu, C.C. & Schultz, P.G. Adding new chemistries to the genetic code. Annu. Rev. Biochem. 79, 413-444 (2010).
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 413-444
    • Liu, C.C.1    Schultz, P.G.2
  • 2
    • 84898629934 scopus 로고    scopus 로고
    • Pyrrolysyl-tRNA synthetase: An ordinary enzyme but an outstanding genetic code expansion tool
    • Wan, W., Tharp, J.M. & Liu, W.R. Pyrrolysyl-tRNA synthetase: an ordinary enzyme but an outstanding genetic code expansion tool. Biochim. Biophys. Acta 1844, 1059-1070 (2014).
    • (2014) Biochim. Biophys. Acta , vol.1844 , pp. 1059-1070
    • Wan, W.1    Tharp, J.M.2    Liu, W.R.3
  • 3
    • 84900420574 scopus 로고    scopus 로고
    • Expanding and reprogramming the genetic code of cells and animals
    • Chin, J.W. Expanding and reprogramming the genetic code of cells and animals. Annu. Rev. Biochem. 83, 379-408 (2014).
    • (2014) Annu. Rev. Biochem. , vol.83 , pp. 379-408
    • Chin, J.W.1
  • 4
    • 84862778261 scopus 로고    scopus 로고
    • N-acetyl lysyl-tRNA synthetases evolved by a CcdB-based selection possess N-acetyl lysine specificity in vitro and in vivo
    • Umehara, T. et al. N-acetyl lysyl-tRNA synthetases evolved by a CcdB-based selection possess N-acetyl lysine specificity in vitro and in vivo. FEBS Lett. 586, 729-733 (2012).
    • (2012) FEBS Lett. , vol.586 , pp. 729-733
    • Umehara, T.1
  • 6
    • 79955534060 scopus 로고    scopus 로고
    • A system for the continuous directed evolution of biomolecules
    • Esvelt, K.M., Carlson, J.C. & Liu, D.R. A system for the continuous directed evolution of biomolecules. Nature 472, 499-503 (2011).
    • (2011) Nature , vol.472 , pp. 499-503
    • Esvelt, K.M.1    Carlson, J.C.2    Liu, D.R.3
  • 7
    • 84874410798 scopus 로고    scopus 로고
    • A population-based experimental model for protein evolution: Effects of mutation rate and selection stringency on evolutionary outcomes
    • Leconte, A.M. et al. A population-based experimental model for protein evolution: effects of mutation rate and selection stringency on evolutionary outcomes. Biochemistry 52, 1490-1499 (2013).
    • (2013) Biochemistry , vol.52 , pp. 1490-1499
    • Leconte, A.M.1
  • 8
    • 84894101033 scopus 로고    scopus 로고
    • Negative selection and stringency modulation in phage-assisted continuous evolution
    • Carlson, J.C., Badran, A.H., Guggiana-Nilo, D.A. & Liu, D.R. Negative selection and stringency modulation in phage-assisted continuous evolution. Nat. Chem. Biol. 10, 216-222 (2014).
    • (2014) Nat. Chem. Biol. , vol.10 , pp. 216-222
    • Carlson, J.C.1    Badran, A.H.2    Guggiana-Nilo, D.A.3    Liu, D.R.4
  • 9
    • 84923266286 scopus 로고    scopus 로고
    • A system for the continuous directed evolution of proteases rapidly reveals drug-resistance mutations
    • Dickinson, B.C., Packer, M.S., Badran, A.H. & Liu, D.R. A system for the continuous directed evolution of proteases rapidly reveals drug-resistance mutations. Nat. Commun. 5, 5352 (2014).
    • (2014) Nat. Commun. , vol.5 , pp. 5352
    • Dickinson, B.C.1    Packer, M.S.2    Badran, A.H.3    Liu, D.R.4
  • 10
    • 84959102577 scopus 로고    scopus 로고
    • Continuous directed evolution of DNA-binding proteins to improve TALEN specificity
    • Hubbard, B.P. et al. Continuous directed evolution of DNA-binding proteins to improve TALEN specificity. Nat. Methods 12, 939-942 (2015).
    • (2015) Nat. Methods , vol.12 , pp. 939-942
    • Hubbard, B.P.1
  • 11
    • 84969786561 scopus 로고    scopus 로고
    • Continuous evolution of bacillus thuringiensis toxins overcomes insect resistance
    • Badran, A.H. et al. Continuous evolution of Bacillus thuringiensis toxins overcomes insect resistance. Nature 533, 58-63 (2016).
    • (2016) Nature , vol.533 , pp. 58-63
    • Badran, A.H.1
  • 12
    • 0030797114 scopus 로고    scopus 로고
    • The C-terminal domain of TolA is the coreceptor for filamentous phage infection of E. Coli
    • Riechmann, L. & Holliger, P. The C-terminal domain of TolA is the coreceptor for filamentous phage infection of E. coli. Cell 90, 351-360 (1997).
    • (1997) Cell , vol.90 , pp. 351-360
    • Riechmann, L.1    Holliger, P.2
  • 13
    • 0037112082 scopus 로고    scopus 로고
    • Structural basis for the transition from initiation to elongation transcription in T7 RNA polymerase
    • Yin, Y.W. & Steitz, T.A. Structural basis for the transition from initiation to elongation transcription in T7 RNA polymerase. Science 298, 1387-1395 (2002).
    • (2002) Science , vol.298 , pp. 1387-1395
    • Yin, Y.W.1    Steitz, T.A.2
  • 14
    • 33646038596 scopus 로고    scopus 로고
    • The genetic incorporation of a distance probe into proteins in Escherichia coli
    • Tsao, M.L., Summerer, D., Ryu, Y. & Schultz, P.G. The genetic incorporation of a distance probe into proteins in Escherichia coli. J. Am. Chem. Soc. 128, 4572-4573 (2006).
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 4572-4573
    • Tsao, M.L.1    Summerer, D.2    Ryu, Y.3    Schultz, P.G.4
  • 15
    • 49649110168 scopus 로고    scopus 로고
    • Immunochemical termination of self-tolerance
    • Grünewald, J. et al. Immunochemical termination of self-tolerance. Proc. Natl. Acad. Sci. USA 105, 11276-11280 (2008).
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 11276-11280
    • Grünewald, J.1
  • 16
    • 56049106840 scopus 로고    scopus 로고
    • Multistep engineering of pyrrolysyl-tRNA synthetase to genetically encode N -(o-azidobenzyloxycarbonyl) lysine for site-specific protein modification
    • Yanagisawa, T. et al. Multistep engineering of pyrrolysyl-tRNA synthetase to genetically encode N -(o-azidobenzyloxycarbonyl) lysine for site-specific protein modification. Chem. Biol. 15, 1187-1197 (2008).
    • (2008) Chem. Biol. , vol.15 , pp. 1187-1197
    • Yanagisawa, T.1
  • 17
    • 0031911439 scopus 로고    scopus 로고
    • The structural basis of phage display elucidated by the crystal structure of the N-terminal domains of g3p
    • Lubkowski, J., Hennecke, F., Plückthun, A. & Wlodawer, A. The structural basis of phage display elucidated by the crystal structure of the N-terminal domains of g3p. Nat. Struct. Biol. 5, 140-147 (1998).
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 140-147
    • Lubkowski, J.1    Hennecke, F.2    Plückthun, A.3    Wlodawer, A.4
  • 18
    • 0000046526 scopus 로고    scopus 로고
    • Filamentous phage infection: Crystal structure of g3p in complex with its coreceptor, the C-terminal domain of TolA
    • Lubkowski, J., Hennecke, F., Plückthun, A. & Wlodawer, A. Filamentous phage infection: crystal structure of g3p in complex with its coreceptor, the C-terminal domain of TolA. Structure 7, 711-722 (1999).
    • (1999) Structure , vol.7 , pp. 711-722
    • Lubkowski, J.1    Hennecke, F.2    Plückthun, A.3    Wlodawer, A.4
  • 19
    • 0036301383 scopus 로고    scopus 로고
    • Delineating the site of interaction on the pIII protein of filamentous bacteriophage fd with the F-pilus of Escherichia coli
    • Deng, L.W. & Perham, R.N. Delineating the site of interaction on the pIII protein of filamentous bacteriophage fd with the F-pilus of Escherichia coli. J. Mol. Biol. 319, 603-614 (2002).
    • (2002) J. Mol. Biol. , vol.319 , pp. 603-614
    • Deng, L.W.1    Perham, R.N.2
  • 20
    • 0020288417 scopus 로고
    • A prokaryotic membrane anchor sequence: Carboxyl terminus of bacteriophage f1 gene III protein retains it in the membrane
    • Boeke, J.D. & Model, P. A prokaryotic membrane anchor sequence: carboxyl terminus of bacteriophage f1 gene III protein retains it in the membrane. Proc. Natl. Acad. Sci. USA 79, 5200-5204 (1982).
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 5200-5204
    • Boeke, J.D.1    Model, P.2
  • 21
    • 0019967083 scopus 로고
    • Effects of bacteriophage f1 gene III protein on the host cell membrane
    • Boeke, J.D., Model, P. & Zinder, N.D. Effects of bacteriophage f1 gene III protein on the host cell membrane. Mol. Gen. Genet. 186, 185-192 (1982).
    • (1982) Mol. Gen. Genet. , vol.186 , pp. 185-192
    • Boeke, J.D.1    Model, P.2    Zinder, N.D.3
  • 22
    • 0027399020 scopus 로고
    • The filamentous bacteriophage assembly proteins require the bacterial SecA protein for correct localization to the membrane
    • Rapoza, M.P. & Webster, R.E. The filamentous bacteriophage assembly proteins require the bacterial SecA protein for correct localization to the membrane. J. Bacteriol. 175, 1856-1859 (1993).
    • (1993) J. Bacteriol. , vol.175 , pp. 1856-1859
    • Rapoza, M.P.1    Webster, R.E.2
  • 23
    • 84943777049 scopus 로고    scopus 로고
    • Development of potent in vivo mutagenesis plasmids with broad mutational spectra
    • Badran, A.H. & Liu, D.R. Development of potent in vivo mutagenesis plasmids with broad mutational spectra. Nat. Commun. 6, 8425 (2015).
    • (2015) Nat. Commun. , vol.6 , pp. 8425
    • Badran, A.H.1    Liu, D.R.2
  • 24
    • 84912074071 scopus 로고    scopus 로고
    • Polyspecific pyrrolysyl-tRNA synthetases from directed evolution
    • Guo, L.T. et al. Polyspecific pyrrolysyl-tRNA synthetases from directed evolution. Proc. Natl. Acad. Sci. USA 111, 16724-16729 (2014).
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. 16724-16729
    • Guo, L.T.1
  • 25
    • 34547470915 scopus 로고    scopus 로고
    • Structure of pyrrolysyl-tRNA synthetase, an archaeal enzyme for genetic code innovation
    • Kavran, J.M. et al. Structure of pyrrolysyl-tRNA synthetase, an archaeal enzyme for genetic code innovation. Proc. Natl. Acad. Sci. USA 104, 11268-11273 (2007).
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 11268-11273
    • Kavran, J.M.1
  • 26
    • 84858663085 scopus 로고    scopus 로고
    • An asymmetric synthesis of l-pyrrolysine
    • Wong, M.L., Guzei, I.A. & Kiessling, L.L. An asymmetric synthesis of l-pyrrolysine. Org. Lett. 14, 1378-1381 (2012).
    • (2012) Org. Lett. , vol.14 , pp. 1378-1381
    • Wong, M.L.1    Guzei, I.A.2    Kiessling, L.L.3
  • 27
    • 84866548719 scopus 로고    scopus 로고
    • PylSn and the homologous N-terminal domain of pyrrolysyl-tRNA synthetase bind the tRNA that is essential for the genetic encoding of pyrrolysine
    • Jiang, R. & Krzycki, J.A. PylSn and the homologous N-terminal domain of pyrrolysyl-tRNA synthetase bind the tRNA that is essential for the genetic encoding of pyrrolysine. J. Biol. Chem. 287, 32738-32746 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 32738-32746
    • Jiang, R.1    Krzycki, J.A.2
  • 28
    • 34250793331 scopus 로고    scopus 로고
    • The amino-terminal domain of pyrrolysyl-tRNA synthetase is dispensable in vitro but required for in vivo activity
    • Herring, S. et al. The amino-terminal domain of pyrrolysyl-tRNA synthetase is dispensable in vitro but required for in vivo activity. FEBS Lett. 581, 3197-3203 (2007).
    • (2007) FEBS Lett. , vol.581 , pp. 3197-3203
    • Herring, S.1
  • 29
    • 70349765673 scopus 로고    scopus 로고
    • A method for genetically installing site-specific acetylation in recombinant histones defines the effects of H3 K56 acetylation
    • Neumann, H. et al. A method for genetically installing site-specific acetylation in recombinant histones defines the effects of H3 K56 acetylation. Mol. Cell 36, 153-163 (2009).
    • (2009) Mol. Cell , vol.36 , pp. 153-163
    • Neumann, H.1
  • 30
    • 40949099577 scopus 로고    scopus 로고
    • Genetically encoding N - acetyllysine in recombinant proteins
    • Neumann, H., Peak-Chew, S.Y. & Chin, J.W. Genetically encoding N - acetyllysine in recombinant proteins. Nat. Chem. Biol. 4, 232-234 (2008).
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 232-234
    • Neumann, H.1    Peak-Chew, S.Y.2    Chin, J.W.3
  • 31
    • 84959017448 scopus 로고    scopus 로고
    • Efficient reassignment of a frequent serine codon in wild-type Escherichia coli
    • Ho, J.M. et al. Efficient reassignment of a frequent serine codon in wild-type Escherichia coli. ACS Synth. Biol. 5, 163-171 (2016).
    • (2016) ACS Synth. Biol. , vol.5 , pp. 163-171
    • Ho, J.M.1
  • 32
    • 0025341309 scopus 로고
    • Scanning model for translational reinitiation in eubacteria
    • Adhin, M.R. & van Duin, J. Scanning model for translational reinitiation in eubacteria. J. Mol. Biol. 213, 811-818 (1990).
    • (1990) J. Mol. Biol. , vol.213 , pp. 811-818
    • Adhin, M.R.1    Van Duin, J.2
  • 33
    • 0033976678 scopus 로고    scopus 로고
    • Reinitiation of protein synthesis in Escherichia coli can be induced by mRNA cis-elements unrelated to canonical translation initiation signals
    • Andrè, A. et al. Reinitiation of protein synthesis in Escherichia coli can be induced by mRNA cis-elements unrelated to canonical translation initiation signals. FEBS Lett. 468, 73-78 (2000).
    • (2000) FEBS Lett. , vol.468 , pp. 73-78
    • Andrè, A.1
  • 34
    • 48649093851 scopus 로고    scopus 로고
    • New molecular reporters for rapid protein folding assays
    • Cabantous, S., Rogers, Y., Terwilliger, T.C. & Waldo, G.S. New molecular reporters for rapid protein folding assays. PLoS One 3, e2387 (2008).
    • (2008) PLoS One , vol.3 , pp. e2387
    • Cabantous, S.1    Rogers, Y.2    Terwilliger, T.C.3    Waldo, G.S.4
  • 35
    • 61349139930 scopus 로고    scopus 로고
    • Pyrrolysyl-tRNA synthetase-tRNA(Pyl) structure reveals the molecular basis of orthogonality
    • Nozawa, K. et al. Pyrrolysyl-tRNA synthetase-tRNA(Pyl) structure reveals the molecular basis of orthogonality. Nature 457, 1163-1167 (2009).
    • (2009) Nature , vol.457 , pp. 1163-1167
    • Nozawa, K.1
  • 36
    • 5044219778 scopus 로고    scopus 로고
    • The site-specific incorporation of p-iodo-l-phenylalanine into proteins for structure determination
    • Xie, J. et al. The site-specific incorporation of p-iodo-l-phenylalanine into proteins for structure determination. Nat. Biotechnol. 22, 1297-1301 (2004).
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1297-1301
    • Xie, J.1
  • 38
    • 42249114824 scopus 로고    scopus 로고
    • Crystallographic studies on multiple conformational states of active-site loops in pyrrolysyl-tRNA synthetase
    • Yanagisawa, T. et al. Crystallographic studies on multiple conformational states of active-site loops in pyrrolysyl-tRNA synthetase. J. Mol. Biol. 378, 634-652 (2008).
    • (2008) J. Mol. Biol. , vol.378 , pp. 634-652
    • Yanagisawa, T.1
  • 39
    • 68949161807 scopus 로고    scopus 로고
    • Programming cells by multiplex genome engineering and accelerated evolution
    • Wang, H.H. et al. Programming cells by multiplex genome engineering and accelerated evolution. Nature 460, 894-898 (2009).
    • (2009) Nature , vol.460 , pp. 894-898
    • Wang, H.H.1
  • 40
    • 84949796862 scopus 로고    scopus 로고
    • Evolution of translation machinery in recoded bacteria enables multi-site incorporation of nonstandard amino acids
    • Amiram, M. et al. Evolution of translation machinery in recoded bacteria enables multi-site incorporation of nonstandard amino acids. Nat. Biotechnol. 33, 1272-1279 (2015).
    • (2015) Nat. Biotechnol. , vol.33 , pp. 1272-1279
    • Amiram, M.1
  • 41
    • 84885791219 scopus 로고    scopus 로고
    • Genomically recoded organisms expand biological functions
    • Lajoie, M.J. et al. Genomically recoded organisms expand biological functions. Science 342, 357-360 (2013).
    • (2013) Science , vol.342 , pp. 357-360
    • Lajoie, M.J.1
  • 42
    • 84908626417 scopus 로고    scopus 로고
    • Efficient multisite unnatural amino acid incorporation in mammalian cells via optimized pyrrolysyl tRNA synthetase/tRNA expression and engineered eRF1
    • Schmied, W.H., Elsässer, S.J., Uttamapinant, C. & Chin, J.W. Efficient multisite unnatural amino acid incorporation in mammalian cells via optimized pyrrolysyl tRNA synthetase/tRNA expression and engineered eRF1. J. Am. Chem. Soc. 136, 15577-15583 (2014).
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 15577-15583
    • Schmied, W.H.1    Elsässer, S.J.2    Uttamapinant, C.3    Chin, J.W.4
  • 43
    • 84964322244 scopus 로고    scopus 로고
    • Rationally evolving tRNAPyl for efficient incorporation of noncanonical amino acids
    • Fan, C., Xiong, H., Reynolds, N.M. & Söll, D. Rationally evolving tRNAPyl for efficient incorporation of noncanonical amino acids. Nucleic Acids Res. 43, e156 (2015).
    • (2015) Nucleic Acids Res. , vol.43 , pp. e156
    • Fan, C.1    Xiong, H.2    Reynolds, N.M.3    Söll, D.4
  • 44
    • 73149104141 scopus 로고    scopus 로고
    • An enhanced system for unnatural amino acid mutagenesis in E. Coli
    • Young, T.S., Ahmad, I., Yin, J.A. & Schultz, P.G. An enhanced system for unnatural amino acid mutagenesis in E. coli. J. Mol. Biol. 395, 361-374 (2010).
    • (2010) J. Mol. Biol. , vol.395 , pp. 361-374
    • Young, T.S.1    Ahmad, I.2    Yin, J.A.3    Schultz, P.G.4
  • 45
    • 70449597245 scopus 로고    scopus 로고
    • Evolution of amber suppressor tRNAs for efficient bacterial production of proteins containing nonnatural amino acids
    • Guo, J., Melançon, C.E. III, Lee, H.S., Groff, D. & Schultz, P.G. Evolution of amber suppressor tRNAs for efficient bacterial production of proteins containing nonnatural amino acids. Angew. Chem. Int. Edn. Engl. 48, 9148-9151 (2009).
    • (2009) Angew. Chem. Int. Edn. Engl. , vol.48 , pp. 9148-9151
    • Guo, J.1    Melançon, C.E.2    Lee, H.S.3    Groff, D.4    Schultz, P.G.5
  • 46
    • 85006483995 scopus 로고    scopus 로고
    • Nitrilase-activatable noncanonical amino acid precursors for cell-selective metabolic labeling of proteomes
    • Li, Z. et al. Nitrilase-activatable noncanonical amino acid precursors for cell-selective metabolic labeling of proteomes. ACS Chem. Biol. 11, 3273-3277 (2016)
    • (2016) ACS Chem. Biol. , vol.11 , pp. 3273-3277
    • Li, Z.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.