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Volumn 50, Issue 39, 2011, Pages 8362-8373

Leader peptide-directed processing of labyrinthopeptin A2 precursor peptide by the modifying enzyme LabKC

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; CLASS I; EXTRACELLULAR; HELICAL STRUCTURES; HYDROPHOBIC PATCH; IN-VITRO; LANTHIONINES; LANTIBIOTICS; LINEAR PEPTIDES; N-TERMINALS; PEPTIDE ANTIBIOTICS; PEPTIDE PROCESSING; PEPTIDE RECOGNITION; PHOSPHATE GROUP; POST-TRANSLATIONAL MODIFICATIONS; POST-TRANSLATIONAL PROCESSING; RIBOSOMAL PEPTIDES; SECONDARY STRUCTURES; SELF-IMMUNITY; SIDE-CHAINS;

EID: 80053432405     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi200526q     Document Type: Article
Times cited : (53)

References (46)
  • 1
    • 35848941716 scopus 로고    scopus 로고
    • Lantibiotics: Peptides of diverse structure and function
    • DOI 10.1146/annurev.micro.61.080706.093501
    • Willey, J. M. and van der Donk, W. A. (2007) Lantibiotics: Peptides of diverse structure and function Annu. Rev. Microbiol. 61, 477-501 (Pubitemid 350058218)
    • (2007) Annual Review of Microbiology , vol.61 , pp. 477-501
    • Willey, J.M.1    Van Der Donk, W.A.2
  • 2
    • 0023912839 scopus 로고
    • Prepeptide sequence of epidermin, a ribosomally synthesized antibiotic with four sulphide-rings
    • Schnell, N., Entian, K.-D., Schneider, U., Götz, F., Zähner, H., Kellner, R., and Jung, G. (1988) Prepeptide sequence of epidermin, a ribosomally synthesized antibiotic with four sulphide-rings Nature 333, 276-278
    • (1988) Nature , vol.333 , pp. 276-278
    • Schnell, N.1    Entian, K.-D.2    Schneider, U.3    Götz, F.4    Zähner, H.5    Kellner, R.6    Jung, G.7
  • 4
    • 33748797399 scopus 로고    scopus 로고
    • Enzyme-catalyzed sulfide ring formation in lantibiotics
    • DOI 10.1002/anie.200601850
    • Jung, G. (2006) Enzyme-catalyzed sulfide ring formation in lantibiotics Angew. Chem., Int. Ed. 45, 5919-5921 (Pubitemid 44408672)
    • (2006) Angewandte Chemie - International Edition , vol.45 , Issue.36 , pp. 5919-5921
    • Jung, G.1
  • 6
    • 14844340728 scopus 로고    scopus 로고
    • Biosynthesis and mode of action of lantibiotics
    • Chatterjee, C., Paul, M., Xie, L., and van der Donk, W. A. (2005) Biosynthesis and mode of action of lantibiotics Chem. Rev. 105, 633-684
    • (2005) Chem. Rev. , vol.105 , pp. 633-684
    • Chatterjee, C.1    Paul, M.2    Xie, L.3    Van Der Donk, W.A.4
  • 10
    • 0037337317 scopus 로고    scopus 로고
    • Structure of Mycobacterium tuberculosis PknB supports a universal activation mechanism for Ser/Thr protein kinases
    • DOI 10.1038/nsb897
    • Young, T. A., Delagoutte, B., Endrizzi, J. A., Falick, A. M., and Alber, T. (2003) Structure of Mycobacterium tuberculosis PknB supports a universal activation mechanism for Ser/Thr protein kinases Nat. Struct. Biol. 10, 168-174 (Pubitemid 36297985)
    • (2003) Nature Structural Biology , vol.10 , Issue.3 , pp. 168-174
    • Young, T.A.1    Delagoutte, B.2    Endrizzi, J.A.3    Falick, A.M.4    Alber, T.5
  • 12
    • 33644854595 scopus 로고    scopus 로고
    • Structure and mechanism of the lantibiotic cyclase involved in nisin biosynthesis
    • DOI 10.1126/science.1121422
    • Li, B., Yu, J. P. J., Brunzelle, J. S., Moll, G. N., van der Donk, W. A., and Nair, S. K. (2006) Structure and mechanism of the lantibiotic cyclase involved in nisin biosynthesis Science 311, 1464-1467 (Pubitemid 43376701)
    • (2006) Science , vol.311 , Issue.5766 , pp. 1464-1467
    • Li, B.1    Yu, J.P.J.2    Brunzelle, J.S.3    Moll, G.N.4    Van Der Donk, W.A.5    Nair, S.K.6
  • 13
    • 36749011295 scopus 로고    scopus 로고
    • Structural Insights into the Enzymatic Mechanism of the Pathogenic MAPK Phosphothreonine Lyase
    • DOI 10.1016/j.molcel.2007.11.011, PII S1097276507007782
    • Zhu, Y., Li, H., Long, C., Hu, L., Xu, H., Hao, X., Liu, L., Chen, S., Wang, D. C., and Shao, F. (2007) Structural insights into the enzymatic mechanism of the pathogenic MAPK phosphothreonine lyase Mol. Cell 28, 899-913 (Pubitemid 350217059)
    • (2007) Molecular Cell , vol.28 , Issue.5 , pp. 899-913
    • Zhu, Y.1    Li, H.2    Long, C.3    Hu, L.4    Xu, H.5    Liu, L.6    Chen, S.7    Wang, D.-C.8    Shao, F.9
  • 15
    • 33847154642 scopus 로고    scopus 로고
    • The phosphothreonine lyase activity of a bacterial type III effector family
    • DOI 10.1126/science.1138960
    • Li, H., Xu, H., Zhou, Y., Zhang, J., Long, C., Li, S., Chen, S., Zhou, J.-M., and Shao, F. (2007) The phosphothreonine lyase activity of a bacterial type III effector family Science 315, 1000-1003 (Pubitemid 46281190)
    • (2007) Science , vol.315 , Issue.5814 , pp. 1000-1003
    • Li, H.1    Xu, H.2    Zhou, Y.3    Zhang, J.4    Long, C.5    Li, S.6    Chen, S.7    Zhou, J.-M.8    Shao, F.9
  • 16
    • 77950563372 scopus 로고    scopus 로고
    • Discovery of unique lanthionine synthetases reveals new mechanistic and evolutionary insights
    • Goto, Y., Li, B., Claesen, J., Shi, Y., Bibb, M. J., and van der Donk, W. A. (2010) Discovery of unique lanthionine synthetases reveals new mechanistic and evolutionary insights PLoS Biol. 8 (3) e1000339
    • (2010) PLoS Biol. , vol.8 , Issue.3 , pp. 1000339
    • Goto, Y.1    Li, B.2    Claesen, J.3    Shi, Y.4    Bibb, M.J.5    Van Der Donk, W.A.6
  • 17
    • 79952097307 scopus 로고    scopus 로고
    • Mechanistic studies of Ser/Thr dehydration catalyzed by a member of the LanL lanthionine synthetase family
    • Goto, Y., Ökesli, A., and van der Donk, W. A. (2011) Mechanistic studies of Ser/Thr dehydration catalyzed by a member of the LanL lanthionine synthetase family Biochemistry 50, 891-898
    • (2011) Biochemistry , vol.50 , pp. 891-898
    • Goto, Y.1    Ökesli, A.2    Van Der Donk, W.A.3
  • 18
    • 77953528770 scopus 로고    scopus 로고
    • In vitro biosynthesis of the prepeptide of type-III lantibiotic labyrinthopeptin A2 including formation of a C-C bond as a post-translational modification
    • Müller, W. M., Schmiederer, T., Ensle, P., and Süssmuth, R. D. (2010) In vitro biosynthesis of the prepeptide of type-III lantibiotic labyrinthopeptin A2 including formation of a C-C bond as a post-translational modification Angew. Chem., Int. Ed. 49, 2436-2440
    • (2010) Angew. Chem., Int. Ed. , vol.49 , pp. 2436-2440
    • Müller, W.M.1    Schmiederer, T.2    Ensle, P.3    Süssmuth, R.D.4
  • 19
    • 0942268866 scopus 로고    scopus 로고
    • Lacticin 481: In Vitro Reconstitution of Lantibiotic Synthetase Activity
    • DOI 10.1126/science.1092600
    • Xie, L., Miller, L. M., Chatterjee, C., Averin, O., Kelleher, N. L., and van der Donk, W. A. (2004) Lacticin 481: In vitro reconstitution of lantibiotic synthetase activity Science 303, 679-681 (Pubitemid 38141635)
    • (2004) Science , vol.303 , Issue.5658 , pp. 679-681
    • Xie, L.1    Miller, L.M.2    Chatterjee, C.3    Averin, O.4    Kelleher, N.L.5    Van Der Donk, W.A.6
  • 21
    • 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
  • 22
    • 2542432896 scopus 로고    scopus 로고
    • NisT, the transporter of the lantibiotic nisin, can transport fully modified, dehydrated, and unmodified prenisin and fusions of the leader peptide with non-lantibiotic peptides
    • DOI 10.1074/jbc.M312789200
    • Kuipers, A., De Boef, E., Rink, R., Fekken, S., Kluskens, L. D., Driessen, A. J., Leenhouts, K., Kuipers, O. P., and Moll, G. N. (2004) NisT, the transporter of the lantibiotic nisin, can transport fully modified, dehydrated and unmodified prenisin and fusions of the leader peptide with non-lantibiotic peptides J. Biol. Chem. 279, 22176-22182 (Pubitemid 38679411)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.21 , pp. 22176-22182
    • Kuipers, A.1    De Boef, E.2    Rink, R.3    Fekken, S.4    Kluskens, L.D.5    Driessen, A.J.M.6    Leenhouts, K.7    Kuipers, O.P.8    Moll, G.N.9
  • 23
    • 34548245086 scopus 로고    scopus 로고
    • The leader peptide is not required for post-translational modification by lacticin 481 synthetase
    • DOI 10.1021/ja072967+
    • Levengood, M. R., Patton, G. C., and van der Donk, W. A. (2007) The leader peptide is not required for post-translational modification by Lacticin 481 synthetase J. Am. Chem. Soc. 129, 10314-10315 (Pubitemid 47330231)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.34 , pp. 10314-10315
    • Levengood, M.R.1    Patton, G.C.2    Van Der Donk, W.A.3
  • 24
    • 47249108199 scopus 로고    scopus 로고
    • The importance of the leader sequence for directing lanthionine formation in lacticin 481
    • DOI 10.1021/bi800277d
    • Patton, G. C., Paul, M., Cooper, L. E., Chatterjee, C., and van der Donk, W. A. (2008) The importance of the leader sequence for directing lanthionine formation in Lacticin 481 Biochemistry 47, 7342-7351 (Pubitemid 351991013)
    • (2008) Biochemistry , vol.47 , Issue.28 , pp. 7342-7351
    • Patton, G.C.1    Paul, M.2    Cooper, L.E.3    Chatterjee, C.4    Van Der Donk, W.A.5
  • 25
    • 0028017962 scopus 로고
    • Influence of amino acid substitutions in the nisin leader peptide on biosynthesis and secretion of nisin by Lactococcus lactis
    • van der Meer, J. R., Rollema, H. S., Siezen, R. J., Beerthuyzen, M. M., Kuipers, O. P., and de Vos, W. M. (1994) Influence of amino acid substitutions in the nisin leader peptide on biosynthesis and secretion of nisin by Lactococcus lactis J. Biol. Chem. 269, 3555-3562 (Pubitemid 24237680)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.5 , pp. 3555-3562
    • Van Der Meer, J.R.1    Rollema, H.S.2    Siezen, R.J.3    Beerthuyzen, M.M.4    Kuipers, O.P.5    De Vos, W.M.6
  • 26
    • 0030845959 scopus 로고    scopus 로고
    • Use of alkaline phosphatase as a reporter polypeptide to study the role of the subtilin leader segment and the SpaT transporter in the posttranslational modifications and secretion of subtilin in Bacillus subtilis 168
    • Izaguirre, G. and Hansen, J. N. (1997) Use of alkaline phosphatase as a reporter polypeptide to study the role of the subtilin leader segment and the SpaT transporter in the posttranslational modifications and secretion of subtilin in Bacillus subtilis 168 Appl. Environ. Microbiol. 63, 3965-3971 (Pubitemid 27411355)
    • (1997) Applied and Environmental Microbiology , vol.63 , Issue.10 , pp. 3965-3971
    • Izaguirre, G.1    Hansen, J.N.2
  • 27
    • 25444499680 scopus 로고    scopus 로고
    • Post-translational modification of therapeutic peptides by NisB, the dehydratase of the lantibiotic nisin
    • DOI 10.1021/bi050805p
    • Kluskens, L. D., Kuipers, A., Rink, R., de Boef, E., Fekken, S., Driessen, A. J., Kuipers, O. P., and Moll, G. N. (2005) Posttranslational modification of therapeutic peptides by NisB, the dehydratase of the lantibiotic Nisin Biochemistry 44, 12827-12834 (Pubitemid 41377322)
    • (2005) Biochemistry , vol.44 , Issue.38 , pp. 12827-12834
    • Kluskens, L.D.1    Kuipers, A.2    Rink, R.3    De Boef, E.4    Fekken, S.5    Driessen, A.J.M.6    Kuipers, O.P.7    Moll, G.N.8
  • 28
    • 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 (Pubitemid 26423562)
    • (1997) Molecular Microbiology , vol.23 , Issue.1 , pp. 161-168
    • Madison, L.L.1    Vivas, E.I.2    Li, Y.-M.3    Walsh, C.T.4    Kolter, R.5
  • 29
    • 0030951761 scopus 로고    scopus 로고
    • Effect of leader peptide mutations on biosynthesis of the lantibiotic Pep5
    • DOI 10.1016/S0378-1097(97)00084-0, PII S0378109797000840
    • Neis, S., Bierbaum, G., Josten, M., Pag, U., Kempter, C., Jung, G., and Sahl, H. G. (1997) Effect of leader peptide mutations on biosynthesis of the lantibiotic Pep5 FEMS Microbiol. Lett. 149, 249-255 (Pubitemid 27163353)
    • (1997) FEMS Microbiology Letters , vol.149 , Issue.2 , pp. 249-255
    • Neis, S.1    Bierbaum, G.2    Josten, M.3    Pag, U.4    Kempter, C.5    Jung, G.6    Sahl, H.-G.7
  • 31
    • 33645064834 scopus 로고    scopus 로고
    • Morphogenetic surfactants and their role in the formation of aerial hyphae in Streptomyces coelicolor
    • Willey, J., Willems, M. A., Kodani, S., and Nodwell, J. R. (2006) Morphogenetic surfactants and their role in the formation of aerial hyphae in Streptomyces coelicolor Mol. Microbiol. 59, 731-742
    • (2006) Mol. Microbiol. , vol.59 , pp. 731-742
    • Willey, J.1    Willems, M.A.2    Kodani, S.3    Nodwell, J.R.4
  • 32
    • 0027465542 scopus 로고
    • A gene cluster involved in aerial mycelium formation in Streptomyces griseus encodes proteins similar to the response regulators of two-component regulatory systems and membrane translocators
    • Ueda, K., Miyake, K., Horinouchi, S., and Beppu, T. (1993) A gene cluster involved in aerial mycelium formation in Streptomyces griseus encodes proteins similar to the response regulator and membrane translocator J. Bacteriol. 175, 2006-2016 (Pubitemid 23097509)
    • (1993) Journal of Bacteriology , vol.175 , Issue.7 , pp. 2006-2016
    • Ueda, K.1    Miyake, K.2    Horinouchi, S.3    Beppu, T.4
  • 35
    • 34147183821 scopus 로고    scopus 로고
    • Complete genome sequence of the erythromycin-producing bacterium Saccharopolyspora erythraea NRRL23338
    • DOI 10.1038/nbt1297, PII NBT1297
    • Oliynyk, M., Samborskyy, M., Lester, J. B., Mironenko, T., Scott, N., Dickens, S., Haydock, S. F., and Leadlay, P. F. (2007) Complete genome sequence of the erythromycin-producing bacterium Saccharopolyspora erythraea Nat. Biotechnol. 4, 447-453 (Pubitemid 46572853)
    • (2007) Nature Biotechnology , vol.25 , Issue.4 , pp. 447-453
    • Oliynyk, M.1    Samborskyy, M.2    Lester, J.B.3    Mironenko, T.4    Scott, N.5    Dickens, S.6    Haydock, S.F.7    Leadlay, P.F.8
  • 36
    • 3242885293 scopus 로고    scopus 로고
    • The PredictProtein server
    • Web Server Issue
    • Rost, B., Yachdav, G., and Liu, J. (2004) The PredictProtein server Nucleic Acids Res. 32 (Web Server issue) W321-W326
    • (2004) Nucleic Acids Res. , vol.32
    • Rost, B.1    Yachdav, G.2    Liu, J.3
  • 37
    • 48449106792 scopus 로고    scopus 로고
    • The JPRED 3 secondary structure prediction server
    • Cole, C., Barber, J. D., and Barton, G. J. (2008) The JPRED 3 secondary structure prediction server Nucleic Acids Res. 35 (Suppl. 2) W197-W201
    • (2008) Nucleic Acids Res. , vol.35 , Issue.SUPPL. 2
    • Cole, C.1    Barber, J.D.2    Barton, G.J.3
  • 38
    • 0025222978 scopus 로고
    • A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids
    • ONeil, K. T. and DeGrado, W. F. (1990) A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids Science 250, 646-651
    • (1990) Science , vol.250 , pp. 646-651
    • Oneil, K.T.1    Degrado, W.F.2
  • 39
    • 0009165149 scopus 로고
    • (Jung, G. and Sahl, H.-G. Eds.) ESCOM, Leiden, The Netherlands.
    • Beck-Sickinger, A. G. and Jung, G. (1991) in Nisin and novel lantibiotics (Jung, G. and Sahl, H.-G., Eds.) pp 218-230, ESCOM, Leiden, The Netherlands.
    • (1991) Nisin and Novel Lantibiotics , pp. 218-230
    • Beck-Sickinger, A.G.1    Jung, G.2
  • 40
    • 0032054255 scopus 로고    scopus 로고
    • 1-26
    • 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 Chem. Biol. 5, 217-228 (Pubitemid 28203052)
    • (1998) Chemistry and Biology , vol.5 , Issue.4 , pp. 217-228
    • Roy, R.S.1    Kim, S.2    Baleja, J.D.3    Walsh, C.T.4
  • 41
    • 67650569231 scopus 로고    scopus 로고
    • Mapping and identification of the region and secondary structure required for the maturation of the nukacin ISK-1 prepeptide
    • Nagao, J., Morinaga, Y., Islam, M. R., Asaduzzaman, S. M., Aso, Y., Nakamayama, J., and Sonomoto, K. (2009) Mapping and identification of the region and secondary structure required for the maturation of the nukacin ISK-1 prepeptide Peptides 30, 1412-1420
    • (2009) Peptides , vol.30 , pp. 1412-1420
    • Nagao, J.1    Morinaga, Y.2    Islam, M.R.3    Asaduzzaman, S.M.4    Aso, Y.5    Nakamayama, J.6    Sonomoto, K.7
  • 42
    • 0035916407 scopus 로고    scopus 로고
    • Effect of amino acid substitutions in conserved residues in the leader peptide on biosynthesis of the lantibiotic mutacin II
    • DOI 10.1016/S0378-1097(00)00565-6, PII S0378109700005656
    • Chen, P., Qi, F., Novak, J., Krull, R. E., and Caufield, P. W. (2001) Effect of amino acid substitutions in conserved residues in the leader peptide on biosynthesis of the lantibiotic mutcinII FEMS Microbiol. Lett. 195, 139-144 (Pubitemid 32155368)
    • (2001) FEMS Microbiology Letters , vol.195 , Issue.2 , pp. 139-144
    • Chen, P.1    Qi, F.2    Novak, J.3    Krull, R.E.4    Caufield, P.W.5
  • 43
    • 0029923954 scopus 로고    scopus 로고
    • From peptide precursors to oxazole and thiazole-containing peptide antibiotics: Microcin B17 synthase
    • DOI 10.1126/science.274.5290.1188
    • Li, Y. M., Milne, J. C., Madison, L. L., Kolter, R., and Walsh, C. T. (1996) From peptide precursors to oxazole and thiazole-containing peptide antibiotics: Microcin B17 synthase Science 274, 1188-1193 (Pubitemid 26389284)
    • (1996) Science , vol.274 , Issue.5290 , pp. 1188-1193
    • Li, Y.-M.1    Milne, J.C.2    Madison, L.L.3    Kolter, R.4    Walsh, C.T.5
  • 44
    • 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
    • DOI 10.1021/bi9728250
    • Roy, R. S., 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 (Pubitemid 28166434)
    • (1998) Biochemistry , vol.37 , Issue.12 , pp. 4125-4136
    • Roy, R.S.1    Belshaw, P.J.2    Walsh, C.T.3
  • 45
    • 33749658643 scopus 로고    scopus 로고
    • Engineering Dehydro Amino Acids and Thioethers into Peptides Using Lacticin 481 Synthetase
    • DOI 10.1016/j.chembiol.2006.08.015, PII S1074552106003395
    • Chatterjee, C., Patton, G. C., Cooper, L., Paul, M., and van der Donk, W. A. (2006) Engineering dehydro amino acids and thioethers into peptides using lacticin 481 synthetase Chem. Biol. 13, 1109-1117 (Pubitemid 44557075)
    • (2006) Chemistry and Biology , vol.13 , Issue.10 , pp. 1109-1117
    • Chatterjee, C.1    Patton, G.C.2    Cooper, L.3    Paul, M.4    Van Der Donk, W.A.5
  • 46
    • 79551491572 scopus 로고    scopus 로고
    • Requirements of the engineered leader peptide of nisin for inducing modification, export, and cleavage
    • Plat, A., Kluskens, L. D., Kuipers, A., Rink, R., and Moll, G. N. (2011) Requirements of the engineered leader peptide of nisin for inducing modification, export, and cleavage Appl. Environ. Microbiol. 77, 604-611
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 604-611
    • Plat, A.1    Kluskens, L.D.2    Kuipers, A.3    Rink, R.4    Moll, G.N.5


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