메뉴 건너뛰기




Volumn 8, Issue 9, 2013, Pages 1998-2008

Engineering unnatural variants of plantazolicin through codon reprogramming

Author keywords

[No Author keywords available]

Indexed keywords

NATURAL PRODUCT; OXAZOLE DERIVATIVE; PEPTIDE DERIVATIVE; PLANTAZOLICIN; THIAZOLE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 84884652959     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb4003392     Document Type: Article
Times cited : (37)

References (50)
  • 1
    • 69549111337 scopus 로고    scopus 로고
    • Antibiotics for emerging pathogens
    • Fischbach, M. A. and Walsh, C. T. (2009) Antibiotics for emerging pathogens Science 325, 1089-1093
    • (2009) Science , vol.325 , pp. 1089-1093
    • Fischbach, M.A.1    Walsh, C.T.2
  • 2
    • 84858308226 scopus 로고    scopus 로고
    • Natural products as sources of new drugs over the 30 years from 1981 to 2010
    • Newman, D. J. and Cragg, G. M. (2012) Natural products as sources of new drugs over the 30 years from 1981 to 2010 J. Nat. Prod. 75, 311-335
    • (2012) J. Nat. Prod. , vol.75 , pp. 311-335
    • Newman, D.J.1    Cragg, G.M.2
  • 3
    • 42949136443 scopus 로고    scopus 로고
    • Genome mining for novel natural product discovery
    • Challis, G. L. (2008) Genome mining for novel natural product discovery J. Med. Chem. 51, 2618-2628
    • (2008) J. Med. Chem. , vol.51 , pp. 2618-2628
    • Challis, G.L.1
  • 4
    • 78650660868 scopus 로고    scopus 로고
    • Molecular recognition between ketosynthase and acyl carrier protein domains of the 6-deoxyerythronolide B synthase
    • Kapur, S., Chen, A. Y., Cane, D. E., and Khosla, C. (2010) Molecular recognition between ketosynthase and acyl carrier protein domains of the 6-deoxyerythronolide B synthase Proc. Natl. Acad. Sci. U.S.A. 107, 22066-22071
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 22066-22071
    • Kapur, S.1    Chen, A.Y.2    Cane, D.E.3    Khosla, C.4
  • 6
    • 80052078373 scopus 로고    scopus 로고
    • Engineering of an 'unnatural' natural product by swapping polyketide synthase domains in Aspergillus nidulans
    • Liu, T., Chiang, Y. M., Somoza, A. D., Oakley, B. R., and Wang, C. C. (2011) Engineering of an 'unnatural' natural product by swapping polyketide synthase domains in Aspergillus nidulans J. Am. Chem. Soc. 133, 13314-13316
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 13314-13316
    • Liu, T.1    Chiang, Y.M.2    Somoza, A.D.3    Oakley, B.R.4    Wang, C.C.5
  • 7
    • 79951841094 scopus 로고    scopus 로고
    • Enzymatic extender unit generation for in vitro polyketide synthase reactions: Structural and functional showcasing of Streptomyces coelicolor MatB
    • Hughes, A. J. and Keatinge-Clay, A. (2011) Enzymatic extender unit generation for in vitro polyketide synthase reactions: structural and functional showcasing of Streptomyces coelicolor MatB Chem. Biol. 18, 165-176
    • (2011) Chem. Biol. , vol.18 , pp. 165-176
    • Hughes, A.J.1    Keatinge-Clay, A.2
  • 9
    • 79955421170 scopus 로고    scopus 로고
    • Bioengineering of a Nisin A-producing Lactococcus lactis to create isogenic strains producing the natural variants Nisin F, Q and Z
    • Piper, C., Hill, C., Cotter, P. D., and Ross, R. P. (2011) Bioengineering of a Nisin A-producing Lactococcus lactis to create isogenic strains producing the natural variants Nisin F, Q and Z Microb. Biotechnol. 4, 375-382
    • (2011) Microb. Biotechnol. , vol.4 , pp. 375-382
    • Piper, C.1    Hill, C.2    Cotter, P.D.3    Ross, R.P.4
  • 10
    • 84874929048 scopus 로고    scopus 로고
    • Saturation mutagenesis of lysine 12 leads to the identification of derivatives of nisin a with enhanced antimicrobial activity
    • Molloy, E. M., Field, D., Connor, P. M., Cotter, P. D., Hill, C., and Ross, R. P. (2013) Saturation mutagenesis of lysine 12 leads to the identification of derivatives of nisin a with enhanced antimicrobial activity PloS One 8, e58530
    • (2013) PloS One , vol.8 , pp. 58530
    • Molloy, E.M.1    Field, D.2    Connor, P.M.3    Cotter, P.D.4    Hill, C.5    Ross, R.P.6
  • 11
    • 84870182562 scopus 로고    scopus 로고
    • 'Bac' to the future: Bioengineering lantibiotics for designer purposes
    • Molloy, E. M., Ross, R. P., and Hill, C. (2012) 'Bac' to the future: bioengineering lantibiotics for designer purposes Biochem. Soc. Trans. 40, 1492-1497
    • (2012) Biochem. Soc. Trans. , vol.40 , pp. 1492-1497
    • Molloy, E.M.1    Ross, R.P.2    Hill, C.3
  • 12
    • 33749999203 scopus 로고    scopus 로고
    • Complete alanine scanning of the two-component lantibiotic lacticin 3147: Generating a blueprint for rational drug design
    • Cotter, P. D., Deegan, L. H., Lawton, E. M., Draper, L. A., O'Connor, P. M., Hill, C., and Ross, R. P. (2006) Complete alanine scanning of the two-component lantibiotic lacticin 3147: generating a blueprint for rational drug design Mol. Microbiol. 62, 735-747
    • (2006) Mol. Microbiol. , vol.62 , pp. 735-747
    • Cotter, P.D.1    Deegan, L.H.2    Lawton, E.M.3    Draper, L.A.4    O'Connor, P.M.5    Hill, C.6    Ross, R.P.7
  • 13
    • 84882289135 scopus 로고    scopus 로고
    • Saturation mutagenesis of selected residues of the alpha-peptide of the lantibiotic lacticin 3147 yields a derivative with enhanced antimicrobial activity
    • 10.1111/1751-7915.12041
    • Field, D., Molloy, E. M., Iancu, C., Draper, L. A., O' Connor, P. M., Cotter, P. D., Hill, C., and Ross, R. P. (2013) Saturation mutagenesis of selected residues of the alpha-peptide of the lantibiotic lacticin 3147 yields a derivative with enhanced antimicrobial activity Microb. Biotechnol 10.1111/1751-7915.12041
    • (2013) Microb. Biotechnol
    • Field, D.1    Molloy, E.M.2    Iancu, C.3    Draper, L.A.4    Connor P M, O.'.5    Cotter, P.D.6    Hill, C.7    Ross, R.P.8
  • 15
    • 79251579302 scopus 로고    scopus 로고
    • Heterologous expression, biosynthesis, and mutagenesis of type II lantibiotics from Bacillus licheniformis in Escherichia coli
    • Caetano, T., Krawczyk, J. M., Mosker, E., Sussmuth, R. D., and Mendo, S. (2011) Heterologous expression, biosynthesis, and mutagenesis of type II lantibiotics from Bacillus licheniformis in Escherichia coli Chem. Biol. 18, 90-100
    • (2011) Chem. Biol. , vol.18 , pp. 90-100
    • Caetano, T.1    Krawczyk, J.M.2    Mosker, E.3    Sussmuth, R.D.4    Mendo, S.5
  • 17
    • 77952836412 scopus 로고    scopus 로고
    • Manipulation of thiocillin variants by prepeptide gene replacement: Structure, conformation, and activity of heterocycle substitution mutants
    • Bowers, A. A., Acker, M. G., Koglin, A., and Walsh, C. T. (2010) Manipulation of thiocillin variants by prepeptide gene replacement: structure, conformation, and activity of heterocycle substitution mutants J. Am. Chem. Soc. 132, 7519-7527
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 7519-7527
    • Bowers, A.A.1    Acker, M.G.2    Koglin, A.3    Walsh, C.T.4
  • 18
    • 84863477081 scopus 로고    scopus 로고
    • Generation of thiocillin ring size variants by prepeptide gene replacement and in vivo processing by Bacillus cereus
    • Bowers, A. A., Acker, M. G., Young, T. S., and Walsh, C. T. (2012) Generation of thiocillin ring size variants by prepeptide gene replacement and in vivo processing by Bacillus cereus J. Am. Chem. Soc. 134, 10313-10316
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 10313-10316
    • Bowers, A.A.1    Acker, M.G.2    Young, T.S.3    Walsh, C.T.4
  • 19
    • 78650115990 scopus 로고    scopus 로고
    • Heterologous production of thiostrepton A and biosynthetic engineering of thiostrepton analogs
    • Li, C., Zhang, F., and Kelly, W. L. (2011) Heterologous production of thiostrepton A and biosynthetic engineering of thiostrepton analogs Mol. Biosyst. 7, 82-90
    • (2011) Mol. Biosyst. , vol.7 , pp. 82-90
    • Li, C.1    Zhang, F.2    Kelly, W.L.3
  • 20
    • 83455261993 scopus 로고    scopus 로고
    • Mutagenesis of the thiostrepton precursor peptide at Thr7 impacts both biosynthesis and function
    • Li, C., Zhang, F., and Kelly, W. L. (2012) Mutagenesis of the thiostrepton precursor peptide at Thr7 impacts both biosynthesis and function Chem. Commun. 48, 558-560
    • (2012) Chem. Commun. , vol.48 , pp. 558-560
    • Li, C.1    Zhang, F.2    Kelly, W.L.3
  • 21
    • 84871562064 scopus 로고    scopus 로고
    • Codon randomization for rapid exploration of chemical space in thiopeptide antibiotic variants
    • Young, T. S., Dorrestein, P. C., and Walsh, C. T. (2012) Codon randomization for rapid exploration of chemical space in thiopeptide antibiotic variants Chem. Biol. 19, 1600-1610
    • (2012) Chem. Biol. , vol.19 , pp. 1600-1610
    • Young, T.S.1    Dorrestein, P.C.2    Walsh, C.T.3
  • 23
    • 79953852240 scopus 로고    scopus 로고
    • Sequence diversity in the lasso peptide framework: Discovery of functional microcin J25 variants with multiple amino acid substitutions
    • Pan, S. J. and Link, A. J. (2011) Sequence diversity in the lasso peptide framework: discovery of functional microcin J25 variants with multiple amino acid substitutions J. Am. Chem. Soc. 133, 5016-5023
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 5016-5023
    • Pan, S.J.1    Link, A.J.2
  • 25
    • 84861308350 scopus 로고    scopus 로고
    • YcaO domains use ATP to activate amide backbones during peptide cyclodehydrations
    • Dunbar, K. L., Melby, J. O., and Mitchell, D. A. (2012) YcaO domains use ATP to activate amide backbones during peptide cyclodehydrations Nat. Chem. Biol. 8, 569-575
    • (2012) Nat. Chem. Biol. , vol.8 , pp. 569-575
    • Dunbar, K.L.1    Melby, J.O.2    Mitchell, D.A.3
  • 27
    • 84858656036 scopus 로고    scopus 로고
    • Structure determination and interception of biosynthetic intermediates for the plantazolicin class of highly discriminating antibiotics
    • Molohon, K. J., Melby, J. O., Lee, J., Evans, B. S., Dunbar, K. L., Bumpus, S. B., Kelleher, N. L., and Mitchell, D. A. (2011) Structure determination and interception of biosynthetic intermediates for the plantazolicin class of highly discriminating antibiotics ACS Chem. Biol. 6, 1307-1313
    • (2011) ACS Chem. Biol. , vol.6 , pp. 1307-1313
    • Molohon, K.J.1    Melby, J.O.2    Lee, J.3    Evans, B.S.4    Dunbar, K.L.5    Bumpus, S.B.6    Kelleher, N.L.7    Mitchell, D.A.8
  • 28
    • 34250666615 scopus 로고    scopus 로고
    • Tryptophan-dependent production of indole-3-acetic acid (IAA) affects level of plant growth promotion by Bacillus amyloliquefaciens FZB42
    • Idris, E. E., Iglesias, D. J., Talon, M., and Borriss, R. (2007) Tryptophan-dependent production of indole-3-acetic acid (IAA) affects level of plant growth promotion by Bacillus amyloliquefaciens FZB42 Mol. Plant-Microbe Interact. 20, 619-626
    • (2007) Mol. Plant-Microbe Interact. , vol.20 , pp. 619-626
    • Idris, E.E.1    Iglesias, D.J.2    Talon, M.3    Borriss, R.4
  • 29
    • 49449119076 scopus 로고    scopus 로고
    • Cloning, expression, and biochemical characterization of Streptomyces rubellomurinus genes required for biosynthesis of antimalarial compound FR900098
    • Eliot, A. C., Griffin, B. M., Thomas, P. M., Johannes, T. W., Kelleher, N. L., Zhao, H., and Metcalf, W. W. (2008) Cloning, expression, and biochemical characterization of Streptomyces rubellomurinus genes required for biosynthesis of antimalarial compound FR900098 Chem. Biol. 15, 765-770
    • (2008) Chem. Biol. , vol.15 , pp. 765-770
    • Eliot, A.C.1    Griffin, B.M.2    Thomas, P.M.3    Johannes, T.W.4    Kelleher, N.L.5    Zhao, H.6    Metcalf, W.W.7
  • 30
    • 0021050913 scopus 로고
    • Double cos site vectors: Simplified cosmid cloning
    • Bates, P. F. and Swift, R. A. (1983) Double cos site vectors: simplified cosmid cloning Gene 26, 137-146
    • (1983) Gene , vol.26 , pp. 137-146
    • Bates, P.F.1    Swift, R.A.2
  • 31
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter
    • Guzman, L. M., Belin, D., Carson, M. J., and Beckwith, J. (1995) Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter J. Bacteriol. 177, 4121-4130
    • (1995) J. Bacteriol. , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 32
    • 0028017482 scopus 로고
    • Production, purification, and cleavage of tandem repeats of recombinant peptides
    • Kuliopulos, A. and Walsh, C. T. (1994) Production, purification, and cleavage of tandem repeats of recombinant peptides J. Am. Chem. Soc. 116, 4599-4607
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 4599-4607
    • Kuliopulos, A.1    Walsh, C.T.2
  • 33
    • 0035996712 scopus 로고    scopus 로고
    • Processive degradation of nascent polypeptides, triggered by tandem AGA codons, limits the accumulation of recombinant tobacco etch virus protease in Escherichia coli BL21(DE3)
    • Kapust, R. B., Routzahn, K. M., and Waugh, D. S. (2002) Processive degradation of nascent polypeptides, triggered by tandem AGA codons, limits the accumulation of recombinant tobacco etch virus protease in Escherichia coli BL21(DE3) Protein Expression Purif. 24, 61-70
    • (2002) Protein Expression Purif. , vol.24 , pp. 61-70
    • Kapust, R.B.1    Routzahn, K.M.2    Waugh, D.S.3
  • 34
    • 65649123071 scopus 로고    scopus 로고
    • Expression of Epstein-Barr virus EBNA1 protein in Escherichia coli: Purification under nondenaturing conditions and use in DNA-binding studies
    • Bouallag, N., Gaillard, C., Marechal, V., and Strauss, F. (2009) Expression of Epstein-Barr virus EBNA1 protein in Escherichia coli: purification under nondenaturing conditions and use in DNA-binding studies Protein Expression Purif. 67, 35-40
    • (2009) Protein Expression Purif. , vol.67 , pp. 35-40
    • Bouallag, N.1    Gaillard, C.2    Marechal, V.3    Strauss, F.4
  • 35
    • 0032126996 scopus 로고    scopus 로고
    • Kinetics and regioselectivity of peptide-to-heterocycle conversions by microcin B17 synthetase
    • Belshaw, P. J., Roy, R. S., Kelleher, N. L., and Walsh, C. T. (1998) Kinetics and regioselectivity of peptide-to-heterocycle conversions by microcin B17 synthetase Chem. Biol. 5, 373-384
    • (1998) Chem. Biol. , vol.5 , pp. 373-384
    • Belshaw, P.J.1    Roy, R.S.2    Kelleher, N.L.3    Walsh, C.T.4
  • 36
    • 0033598801 scopus 로고    scopus 로고
    • Posttranslational heterocyclization of cysteine and serine residues in the antibiotic microcin B17: Distributivity and directionality
    • Kelleher, N. L., Hendrickson, C. L., and Walsh, C. T. (1999) Posttranslational heterocyclization of cysteine and serine residues in the antibiotic microcin B17: distributivity and directionality Biochemistry 38, 15623-15630
    • (1999) Biochemistry , vol.38 , pp. 15623-15630
    • Kelleher, N.L.1    Hendrickson, C.L.2    Walsh, C.T.3
  • 37
    • 84858665499 scopus 로고    scopus 로고
    • Selectivity, directionality, and promiscuity in peptide processing from a Bacillus sp. Al Hakam cyclodehydratase
    • Melby, J. O., Dunbar, K. L., Trinh, N. Q., and Mitchell, D. A. (2012) Selectivity, directionality, and promiscuity in peptide processing from a Bacillus sp. Al Hakam cyclodehydratase J. Am. Chem. Soc. 134, 5309-5316
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 5309-5316
    • Melby, J.O.1    Dunbar, K.L.2    Trinh, N.Q.3    Mitchell, D.A.4
  • 38
    • 67649730080 scopus 로고    scopus 로고
    • Structural and functional dissection of the heterocyclic peptide cytotoxin streptolysin S
    • Mitchell, D. A., Lee, S. W., Pence, M. A., Markley, A. L., Limm, J. D., Nizet, V., and Dixon, J. E. (2009) Structural and functional dissection of the heterocyclic peptide cytotoxin streptolysin S J. Biol. Chem. 284, 13004-13012
    • (2009) J. Biol. Chem. , vol.284 , pp. 13004-13012
    • Mitchell, D.A.1    Lee, S.W.2    Pence, M.A.3    Markley, A.L.4    Limm, J.D.5    Nizet, V.6    Dixon, J.E.7
  • 39
    • 0001265178 scopus 로고    scopus 로고
    • Mutational analysis of posttranslational heterocycle biosynthesis in the gyrase inhibitor microcin B17: Distance dependence from propeptide and tolerance for substitution in a GSCG cyclizable sequence
    • Sinha Roy, R., Belshaw, P. J., and Walsh, C. T. (1998) Mutational analysis of posttranslational heterocycle biosynthesis in the gyrase inhibitor microcin B17: distance dependence from propeptide and tolerance for substitution in a GSCG cyclizable sequence Biochemistry 37, 4125-4136
    • (1998) Biochemistry , vol.37 , pp. 4125-4136
    • Sinha Roy, R.1    Belshaw, P.J.2    Walsh, C.T.3
  • 40
    • 0033229860 scopus 로고    scopus 로고
    • Expressed protein ligation to probe regiospecificity of heterocyclization in the peptide antibiotic microcin B17
    • Roy, R. S., Allen, O., and Walsh, C. T. (1999) Expressed protein ligation to probe regiospecificity of heterocyclization in the peptide antibiotic microcin B17 Chem. Biol. 6, 789-799
    • (1999) Chem. Biol. , vol.6 , pp. 789-799
    • Roy, R.S.1    Allen, O.2    Walsh, C.T.3
  • 41
    • 69349105507 scopus 로고    scopus 로고
    • Distributive and directional behavior of lantibiotic synthetases revealed by high-resolution tandem mass spectrometry
    • Lee, M. V., Ihnken, L. A., You, Y. O., McClerren, A. L., van der Donk, W. A., and Kelleher, N. L. (2009) Distributive and directional behavior of lantibiotic synthetases revealed by high-resolution tandem mass spectrometry J. Am. Chem. Soc. 131, 12258-12264
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 12258-12264
    • Lee, M.V.1    Ihnken, L.A.2    You, Y.O.3    McClerren, A.L.4    Van Der Donk, W.A.5    Kelleher, N.L.6
  • 42
    • 0011349767 scopus 로고
    • Hydrolysis of 2-methyl-delta-oxazoline - An intramolecular O-N-acetyl transfer reaction
    • Martin, R. B. and Parcell, A. (1961) Hydrolysis of 2-methyl-delta- oxazoline-an intramolecular O-N-acetyl transfer reaction J. Am. Chem. Soc. 83, 4835-4838
    • (1961) J. Am. Chem. Soc. , vol.83 , pp. 4835-4838
    • Martin, R.B.1    Parcell, A.2
  • 43
    • 0006329127 scopus 로고
    • Thiazoline + oxazoline hydrolyses + sulfur-nitrogen + oxygen-nitrogen acyl transfer reactions
    • Martin, R. B., Hedrick, R. I., and Parcell, A. (1964) Thiazoline + oxazoline hydrolyses + sulfur-nitrogen + oxygen-nitrogen acyl transfer reactions J. Org. Chem. 29, 3197-3206
    • (1964) J. Org. Chem. , vol.29 , pp. 3197-3206
    • Martin, R.B.1    Hedrick, R.I.2    Parcell, A.3
  • 44
    • 84878951786 scopus 로고    scopus 로고
    • Insights into the mechanism of peptide cyclodehydrations achieved through the chemoenzymatic generation of amide derivatives
    • Dunbar, K. L. and Mitchell, D. A. (2013) Insights into the mechanism of peptide cyclodehydrations achieved through the chemoenzymatic generation of amide derivatives J. Am. Chem. Soc. 135, 8692-8701
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 8692-8701
    • Dunbar, K.L.1    Mitchell, D.A.2
  • 45
    • 0032054255 scopus 로고    scopus 로고
    • Role of the microcin B17 propeptide in substrate recognition: Solution structure and mutational analysis of McbA1-26
    • Roy, R. S., Kim, S., Baleja, J. D., and Walsh, C. T. (1998) Role of the microcin B17 propeptide in substrate recognition: solution structure and mutational analysis of McbA1-26 Chem. Biol. 5, 217-228
    • (1998) Chem. Biol. , vol.5 , pp. 217-228
    • Roy, R.S.1    Kim, S.2    Baleja, J.D.3    Walsh, C.T.4
  • 46
    • 0031023072 scopus 로고    scopus 로고
    • The leader peptide is essential for the post-translational modification of the DNA-gyrase inhibitor microcin B17
    • Madison, L. L., Vivas, E. I., Li, Y. M., Walsh, C. T., and Kolter, R. (1997) The leader peptide is essential for the post-translational modification of the DNA-gyrase inhibitor microcin B17 Mol. Microbiol. 23, 161-168
    • (1997) Mol. Microbiol. , vol.23 , pp. 161-168
    • Madison, L.L.1    Vivas, E.I.2    Li, Y.M.3    Walsh, C.T.4    Kolter, R.5
  • 47
    • 74049115080 scopus 로고    scopus 로고
    • Follow the leader: The use of leader peptides to guide natural product biosynthesis
    • Oman, T. J. and van der Donk, W. A. (2010) Follow the leader: the use of leader peptides to guide natural product biosynthesis Nat. Chem. Biol. 6, 9-18
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 9-18
    • Oman, T.J.1    Van Der Donk, W.A.2
  • 50
    • 0036134395 scopus 로고    scopus 로고
    • Site-directed mutagenesis by polymerase chain reaction
    • Jeltsch, A. and Lanio, T. (2002) Site-directed mutagenesis by polymerase chain reaction Methods Mol. Biol. 182, 85-94
    • (2002) Methods Mol. Biol. , vol.182 , pp. 85-94
    • Jeltsch, A.1    Lanio, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.