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Volumn 589, Issue 15, 2015, Pages 1802-1806

The PqqD homologous domain of the radical SAM enzyme ThnB is required for thioether bond formation during thurincin H maturation

Author keywords

Biosynthesis; Natural product; Radical SAM enzyme; Ribosomal peptide; Sactipeptide; 4Fe 4S cluster

Indexed keywords

BACTERIOCIN; ENZYME; PROTEIN PQQD; PROTEIN PRECURSOR; PROTEIN THNB; SULFIDE; THURINCIN H; UNCLASSIFIED DRUG; ADENOSYLMETHIONINE HYDROLASE; HYDROLASE;

EID: 84934434331     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2015.05.032     Document Type: Article
Times cited : (62)

References (27)
  • 2
    • 84881237635 scopus 로고    scopus 로고
    • Radical S-adenosylmethionine enzyme catalyzed thioether bond formation in sactipeptide biosynthesis
    • L. Fluhe, and M.A. Marahiel Radical S-adenosylmethionine enzyme catalyzed thioether bond formation in sactipeptide biosynthesis Curr. Opin. Chem. Biol. 17 2013 605 612
    • (2013) Curr. Opin. Chem. Biol. , vol.17 , pp. 605-612
    • Fluhe, L.1    Marahiel, M.A.2
  • 3
    • 0022413987 scopus 로고
    • Subtilosin A, a new antibiotic peptide produced by Bacillus subtilis 168: isolation, structural analysis, and biogenesis
    • K. Babasaki, T. Takao, Y. Shimonishi, and K. Kurahashi Subtilosin A, a new antibiotic peptide produced by Bacillus subtilis 168: isolation, structural analysis, and biogenesis J. Biochem. 98 1985 585 603
    • (1985) J. Biochem. , vol.98 , pp. 585-603
    • Babasaki, K.1    Takao, T.2    Shimonishi, Y.3    Kurahashi, K.4
  • 4
    • 0037462081 scopus 로고    scopus 로고
    • Structure of subtilosin A, an antimicrobial peptide from Bacillus subtilis with unusual posttranslational modifications linking cysteine sulfurs to alpha-carbons of phenylalanine and threonine
    • K. Kawulka, T. Sprules, R.T. McKay, P. Mercier, C.M. Diaper, P. Zuber, and J.C. Vederas Structure of subtilosin A, an antimicrobial peptide from Bacillus subtilis with unusual posttranslational modifications linking cysteine sulfurs to alpha-carbons of phenylalanine and threonine J. Am. Chem. Soc. 125 2003 4726 4727
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 4726-4727
    • Kawulka, K.1    Sprules, T.2    McKay, R.T.3    Mercier, P.4    Diaper, C.M.5    Zuber, P.6    Vederas, J.C.7
  • 7
    • 79957690316 scopus 로고    scopus 로고
    • The 3D structure of thuricin CD, a two-component bacteriocin with cysteine sulfur to alpha-carbon cross-links
    • C.S. Sit, R.T. McKay, C. Hill, R.P. Ross, and J.C. Vederas The 3D structure of thuricin CD, a two-component bacteriocin with cysteine sulfur to alpha-carbon cross-links J. Am. Chem. Soc. 133 2011 7680 7683
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 7680-7683
    • Sit, C.S.1    Mckay, R.T.2    Hill, C.3    Ross, R.P.4    Vederas, J.C.5
  • 8
    • 80052485163 scopus 로고    scopus 로고
    • The 3D solution structure of thurincin H, a bacteriocin with four sulfur to alpha-carbon crosslinks
    • C.S. Sit, M.J. van Belkum, R.T. McKay, R.W. Worobo, and J.C. Vederas The 3D solution structure of thurincin H, a bacteriocin with four sulfur to alpha-carbon crosslinks Angew. Chem. Int. Ed. Engl. 50 2011 8718 8721
    • (2011) Angew. Chem. Int. Ed. Engl. , vol.50 , pp. 8718-8721
    • Sit, C.S.1    Van Belkum, M.J.2    McKay, R.T.3    Worobo, R.W.4    Vederas, J.C.5
  • 12
    • 70349234326 scopus 로고    scopus 로고
    • Biosynthesis and transcriptional analysis of thurincin H, a tandem repeated bacteriocin genetic locus, produced by Bacillus thuringiensis SF361
    • H. Lee, J.J. Churey, and R.W. Worobo Biosynthesis and transcriptional analysis of thurincin H, a tandem repeated bacteriocin genetic locus, produced by Bacillus thuringiensis SF361 FEMS Microbiol. Lett. 299 2009 205 213
    • (2009) FEMS Microbiol. Lett. , vol.299 , pp. 205-213
    • Lee, H.1    Churey, J.J.2    Worobo, R.W.3
  • 16
    • 84872801335 scopus 로고    scopus 로고
    • Two [4Fe-4S] clusters containing radical SAM enzyme SkfB catalyze thioether bond formation during the maturation of the sporulation killing factor
    • L. Fluhe, O. Burghaus, B.M. Wieckowski, T.W. Giessen, U. Linne, and M.A. Marahiel Two [4Fe-4S] clusters containing radical SAM enzyme SkfB catalyze thioether bond formation during the maturation of the sporulation killing factor J. Am. Chem. Soc. 135 2013 959 962
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 959-962
    • Fluhe, L.1    Burghaus, O.2    Wieckowski, B.M.3    Giessen, T.W.4    Linne, U.5    Marahiel, M.A.6
  • 17
    • 79958173211 scopus 로고    scopus 로고
    • Biological systems discovery in silico: radical S-adenosylmethionine protein families and their target peptides for posttranslational modification
    • D.H. Haft, and M.K. Basu Biological systems discovery in silico: radical S-adenosylmethionine protein families and their target peptides for posttranslational modification J. Bacteriol. 193 2011 2745 2755
    • (2011) J. Bacteriol. , vol.193 , pp. 2745-2755
    • Haft, D.H.1    Basu, M.K.2
  • 18
    • 84858693177 scopus 로고    scopus 로고
    • Distribution and properties of the genes encoding the biosynthesis of the bacterial cofactor, pyrroloquinoline quinone
    • Y.Q. Shen, F. Bonnot, E.M. Imsand, J.M. RoseFigura, K. Sjolander, and J.P. Klinman Distribution and properties of the genes encoding the biosynthesis of the bacterial cofactor, pyrroloquinoline quinone Biochemistry 51 2012 2265 2275
    • (2012) Biochemistry , vol.51 , pp. 2265-2275
    • Shen, Y.Q.1    Bonnot, F.2    Imsand, E.M.3    Rosefigura, J.M.4    Sjolander, K.5    Klinman, J.P.6
  • 19
    • 77956457511 scopus 로고    scopus 로고
    • Interaction of PqqE and PqqD in the pyrroloquinoline quinone (PQQ) biosynthetic pathway links PqqD to the radical SAM superfamily
    • S.R. Wecksler, S. Stoll, A.T. Iavarone, E.M. Imsand, H. Tran, R.D. Britt, and J.P. Klinman Interaction of PqqE and PqqD in the pyrroloquinoline quinone (PQQ) biosynthetic pathway links PqqD to the radical SAM superfamily Chem. Commun. 46 2010 7031 7033
    • (2010) Chem. Commun. , vol.46 , pp. 7031-7033
    • Wecksler, S.R.1    Stoll, S.2    Iavarone, A.T.3    Imsand, E.M.4    Tran, H.5    Britt, R.D.6    Klinman, J.P.7
  • 20
    • 0035902555 scopus 로고    scopus 로고
    • Spectroscopic changes during a single turnover of biotin synthase: destruction of a [2Fe-2S] cluster accompanies sulfur insertion
    • N.B. Ugulava, C.J. Sacanell, and J.T. Jarrett Spectroscopic changes during a single turnover of biotin synthase: destruction of a [2Fe-2S] cluster accompanies sulfur insertion Biochemistry 40 2001 8352 8358
    • (2001) Biochemistry , vol.40 , pp. 8352-8358
    • Ugulava, N.B.1    Sacanell, C.J.2    Jarrett, J.T.3
  • 21
    • 84866036753 scopus 로고    scopus 로고
    • Biotin synthase: insights into radical-mediated carbon-sulfur bond formation
    • C.J. Fugate, and J.T. Jarrett Biotin synthase: insights into radical-mediated carbon-sulfur bond formation Biochim. Biophys. Acta 1824 2012 1213 1222
    • (2012) Biochim. Biophys. Acta , vol.1824 , pp. 1213-1222
    • Fugate, C.J.1    Jarrett, J.T.2
  • 22
    • 16544395270 scopus 로고    scopus 로고
    • Site-directed, Ligase-Independent Mutagenesis (SLIM): a single-tube methodology approaching 100% efficiency in 4 h
    • J. Chiu, P.E. March, R. Lee, and D. Tillett Site-directed, Ligase-Independent Mutagenesis (SLIM): a single-tube methodology approaching 100% efficiency in 4 h Nucleic Acids Res. 32 2004 e174
    • (2004) Nucleic Acids Res. , vol.32 , pp. e174
    • Chiu, J.1    March, P.E.2    Lee, R.3    Tillett, D.4
  • 23
    • 42249087464 scopus 로고    scopus 로고
    • Site-directed, Ligase-Independent Mutagenesis (SLIM) for highly efficient mutagenesis of plasmids greater than 8 kb
    • J. Chiu, D. Tillett, I.W. Dawes, and P.E. March Site-directed, Ligase-Independent Mutagenesis (SLIM) for highly efficient mutagenesis of plasmids greater than 8 kb J. Microbiol. Methods 73 2008 195 198
    • (2008) J. Microbiol. Methods , vol.73 , pp. 195-198
    • Chiu, J.1    Tillett, D.2    Dawes, I.W.3    March, P.E.4
  • 24
    • 0024357799 scopus 로고
    • A simple method for site-directed mutagenesis using the polymerase chain reaction
    • A. Hemsley, N. Arnheim, M.D. Toney, G. Cortopassi, and D.J. Galas A simple method for site-directed mutagenesis using the polymerase chain reaction Nucleic Acids Res. 17 1989 6545 6551
    • (1989) Nucleic Acids Res. , vol.17 , pp. 6545-6551
    • Hemsley, A.1    Arnheim, N.2    Toney, M.D.3    Cortopassi, G.4    Galas, D.J.5
  • 25
    • 3242887157 scopus 로고    scopus 로고
    • CD-Search: protein domain annotations on the fly
    • A. Marchler-Bauer, and S.H. Bryant CD-Search: protein domain annotations on the fly Nucleic Acids Res. 32 2004 W327 W331
    • (2004) Nucleic Acids Res. , vol.32 , pp. W327-W331
    • Marchler-Bauer, A.1    Bryant, S.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.