메뉴 건너뛰기




Volumn 49, Issue 37, 2010, Pages 8033-8042

Distinct extracytoplasmic siderophore binding proteins recognize ferrioxamines and ferricoelichelin in streptomyces coelicolor A3(2)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; BINDING ENERGY; BIOCHEMISTRY; BIOSYNTHESIS; DICHROISM; ESCHERICHIA COLI; GENES; IRON COMPOUNDS;

EID: 77956580393     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi100451k     Document Type: Article
Times cited : (28)

References (29)
  • 1
    • 34548739613 scopus 로고    scopus 로고
    • Siderophore-based iron acquisition and pathogen control
    • Miethke, M. and Marahiel, M. A. (2007) Siderophore-based iron acquisition and pathogen control Microbiol. Mol. Biol. Rev. 71, 413-451
    • (2007) Microbiol. Mol. Biol. Rev. , vol.71 , pp. 413-451
    • Miethke, M.1    Marahiel, M.A.2
  • 2
    • 0942279513 scopus 로고    scopus 로고
    • Bacillus anthracis requires siderophore biosynthesis for growth in macrophages and mouse virulence
    • Cendrowski, S., MacArthur, W., and Hanna, P. (2004) Bacillus anthracis requires siderophore biosynthesis for growth in macrophages and mouse virulence Mol. Microbiol. 51, 407-417
    • (2004) Mol. Microbiol. , vol.51 , pp. 407-417
    • Cendrowski, S.1    MacArthur, W.2    Hanna, P.3
  • 3
    • 34548671159 scopus 로고    scopus 로고
    • Asymmetry in the structure of the ABC transporter - Binding protein complex BtuCD-BtuF
    • DOI 10.1126/science.1145950
    • Hvorup, R. N., Goetz, B. A., Niederer, M., Hollenstein, K., Perozo, E., and Locher, K. P. (2007) Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF Science 317, 1387-1390 (Pubitemid 47417478)
    • (2007) Science , vol.317 , Issue.5843 , pp. 1387-1390
    • Hvorup, R.N.1    Goetz, B.A.2    Niederer, M.3    Hollenstein, K.4    Perozo, E.5    Locher, K.P.6
  • 4
    • 65449162362 scopus 로고    scopus 로고
    • Siderophore-mediated iron acquisition systems in Bacillus cereus: Identification of receptors for anthrax virulence-associated petrobactin
    • Zawadzka, A., Abergel, R. J., Nichiporuk, R., Andersen, U. J., and Raymond, K. N. (2009) Siderophore-mediated iron acquisition systems in Bacillus cereus: Identification of receptors for anthrax virulence-associated petrobactin Biochemistry 48, 3645-3657
    • (2009) Biochemistry , vol.48 , pp. 3645-3657
    • Zawadzka, A.1    Abergel, R.J.2    Nichiporuk, R.3    Andersen, U.J.4    Raymond, K.N.5
  • 6
    • 0346749526 scopus 로고    scopus 로고
    • The role of FhuD2 in iron(III)-hydroxamate transport in Staphylococcus aureus: Demonstration that FhuD2 binds iron(III)-hydroxamates but with minimal conformational change and implication of mutations on transport
    • Sebulsky, M. T., Shilton, B. H., Speziali, C. D., and Heinrichs, D. E. (2003) The role of FhuD2 in iron(III)-hydroxamate transport in Staphylococcus aureus: Demonstration that FhuD2 binds iron(III)-hydroxamates but with minimal conformational change and implication of mutations on transport J. Biol. Chem. 278, 49890-49900
    • (2003) J. Biol. Chem. , vol.278 , pp. 49890-49900
    • Sebulsky, M.T.1    Shilton, B.H.2    Speziali, C.D.3    Heinrichs, D.E.4
  • 8
    • 47749094684 scopus 로고    scopus 로고
    • Mechanistic insights into a novel exporter-importer system of Mycobacterium tuberculosis unravel its role in trafficking of iron
    • Farhana, A., Kumar, S., Rathore, S. S., Ghosh, P. C., Ehtesham, N. Z., Tyagi, A. K., and Hasnain, S. E. (2008) Mechanistic insights into a novel exporter-importer system of Mycobacterium tuberculosis unravel its role in trafficking of iron PLoS One 3, e2087
    • (2008) PLoS One , vol.3 , pp. 2087
    • Farhana, A.1    Kumar, S.2    Rathore, S.S.3    Ghosh, P.C.4    Ehtesham, N.Z.5    Tyagi, A.K.6    Hasnain, S.E.7
  • 9
    • 27544477567 scopus 로고    scopus 로고
    • Discovery of a new peptide natural product by Streptomyces coelicolor genome mining
    • Lautru, S., Deeth, R. J., Bailey, L. M., and Challis, G. L. (2005) Discovery of a new peptide natural product by Streptomyces coelicolor genome mining Nat. Chem. Biol. 1, 265-269
    • (2005) Nat. Chem. Biol. , vol.1 , pp. 265-269
    • Lautru, S.1    Deeth, R.J.2    Bailey, L.M.3    Challis, G.L.4
  • 10
    • 33750963795 scopus 로고    scopus 로고
    • Multiple biosynthetic and uptake systems mediate siderophore-dependent iron acquisition in Streptomyces coelicolor and Streptomyces ambofaciens
    • Barona-Gomez, F., Lautru, S., Francou, F. X., Leblond, P., Pernodet, J. L., and Challis, G. L. (2006) Multiple biosynthetic and uptake systems mediate siderophore-dependent iron acquisition in Streptomyces coelicolor and Streptomyces ambofaciens Microbiology 152, 3355-3366
    • (2006) Microbiology , vol.152 , pp. 3355-3366
    • Barona-Gomez, F.1    Lautru, S.2    Francou, F.X.3    Leblond, P.4    Pernodet, J.L.5    Challis, G.L.6
  • 11
    • 11444260150 scopus 로고    scopus 로고
    • Identification of a cluster of genes that directs desferrioxamine biosynthesis in Streptomyces coelicolor M145
    • Barona-Gomez, F., Wong, U., Giannakopulos, A. E., Derrick, P. J., and Challis, G. L. (2004) Identification of a cluster of genes that directs desferrioxamine biosynthesis in Streptomyces coelicolor M145 J. Am. Chem. Soc. 126, 16282-16283
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 16282-16283
    • Barona-Gomez, F.1    Wong, U.2    Giannakopulos, A.E.3    Derrick, P.J.4    Challis, G.L.5
  • 12
    • 21044449406 scopus 로고    scopus 로고
    • A widely distributed bacterial pathway independent of nonribosomal peptide synthetases for siderophore biosynthesis
    • Challis, G. L. (2005) A widely distributed bacterial pathway independent of nonribosomal peptide synthetases for siderophore biosynthesis ChemBioChem 4, 601-611
    • (2005) ChemBioChem , vol.4 , pp. 601-611
    • Challis, G.L.1
  • 13
    • 34548688717 scopus 로고    scopus 로고
    • A new family of ATP-dependent oligomerization-macrocyclization biocatalysts
    • Kadi, N., Oves-Costales, D., Barona-Gomez, F., and Challis, G. L. (2007) A new family of ATP-dependent oligomerization-macrocyclization biocatalysts Nat. Chem. Biol. 3, 652-656
    • (2007) Nat. Chem. Biol. , vol.3 , pp. 652-656
    • Kadi, N.1    Oves-Costales, D.2    Barona-Gomez, F.3    Challis, G.L.4
  • 14
    • 33846847791 scopus 로고    scopus 로고
    • Transcriptional regulation of the desferrioxamine gene cluster of Streptomyces coelicolor is mediated by binding of DmdR1 to an iron box in the promoter of the desA gene
    • Tunca, S., Barreiro, C., Sola-Landa, A., Coque, J. J. R., and Martin, J. F. (2007) Transcriptional regulation of the desferrioxamine gene cluster of Streptomyces coelicolor is mediated by binding of DmdR1 to an iron box in the promoter of the desA gene FEBS J. 274, 1110-1122
    • (2007) FEBS J. , vol.274 , pp. 1110-1122
    • Tunca, S.1    Barreiro, C.2    Sola-Landa, A.3    Coque, J.J.R.4    Martin, J.F.5
  • 15
    • 23844511517 scopus 로고    scopus 로고
    • Effects of growth phase and the developmentally significant bldA-specified tRNA on the membrane-associated proteome of Streptomyces coelicolor
    • Kim, D.-W., Chater, K. F., Lee, K.-J., and Hesketh, A. (2005) Effects of growth phase and the developmentally significant bldA-specified tRNA on the membrane-associated proteome of Streptomyces coelicolor Microbiology 151, 2707-2720
    • (2005) Microbiology , vol.151 , pp. 2707-2720
    • Kim, D.-W.1    Chater, K.F.2    Lee, K.-J.3    Hesketh, A.4
  • 16
    • 58149295961 scopus 로고    scopus 로고
    • Lipoprotein biogenesis in Gram-positive bacteria: Knowing when to hold em, knowing when to fold em
    • Hutchings, M. I., Palmer, T., Harrington, D. J., and Sutcliffe, I. C. (2009) Lipoprotein biogenesis in Gram-positive bacteria: Knowing when to hold em, knowing when to fold em Trends Microbiol. 17, 13-21
    • (2009) Trends Microbiol. , vol.17 , pp. 13-21
    • Hutchings, M.I.1    Palmer, T.2    Harrington, D.J.3    Sutcliffe, I.C.4
  • 18
    • 33747074333 scopus 로고    scopus 로고
    • Identification of genes involved in siderophore transport in Streptomyces coelicolor A3(2)
    • Bunet, R., Brock, A., Rexer, H.-U., and Takano, E. (2006) Identification of genes involved in siderophore transport in Streptomyces coelicolor A3(2) FEMS Microbiol. Lett. 262, 57-64
    • (2006) FEMS Microbiol. Lett. , vol.262 , pp. 57-64
    • Bunet, R.1    Brock, A.2    Rexer, H.-U.3    Takano, E.4
  • 20
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 21
    • 0035711194 scopus 로고    scopus 로고
    • Tobacco etch virus protease: Mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency
    • Kapust, R. B., Tözsér, J., Fox, J. D., Anderson, D. E., Cherry, S., Copeland, T. D., and Waugh, D. S. (2001) Tobacco etch virus protease: Mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency Protein Eng. 14, 993-1000
    • (2001) Protein Eng. , vol.14 , pp. 993-1000
    • Kapust, R.B.1    Tözsér, J.2    Fox, J.D.3    Anderson, D.E.4    Cherry, S.5    Copeland, T.D.6    Waugh, D.S.7
  • 22
    • 84923587128 scopus 로고    scopus 로고
    • Origin. 6.0 Professional, Microcal Software Inc
    • Origin. 6.0 Professional, Microcal Software Inc.
  • 23
    • 34548149278 scopus 로고    scopus 로고
    • Hydrophobic ligand binding properties of the human lipocalin apolipoprotein M
    • Ahnström, J., Faber, K., Axler, O., and Dahlbäck, B. (2007) Hydrophobic ligand binding properties of the human lipocalin apolipoprotein M J. Lipid. Res. 48, 1754-1762
    • (2007) J. Lipid. Res. , vol.48 , pp. 1754-1762
    • Ahnström, J.1    Faber, K.2    Axler, O.3    Dahlbäck, B.4
  • 24
    • 0003483442 scopus 로고
    • Iron carriers and iron proteins: Siderophore-mediated iron transport
    • Loehr T.M. (, Ed.) VCH Inc., New York
    • Matzanke, B. F., Müller-Matzanke, G., and Raymond, K. N. (1989) Iron carriers and iron proteins: Siderophore-mediated iron transport, in Iron Carriers and Iron Proteins (Loehr, T. M., Ed.) VCH Inc., New York.
    • (1989) Iron Carriers and Iron Proteins
    • Matzanke, B.F.1    Müller-Matzanke, G.2    Raymond, K.N.3
  • 26
    • 0037134502 scopus 로고    scopus 로고
    • X-ray crystallographic structures of the Escherichia coli periplasmic protein FhuD bound to hydroxamate-type siderophores and the antibiotic albomycin
    • Clarke, T. E., Braun, V., Winkelmann, G., Tari, L. W., and Vogel, H. J. (2002) X-ray crystallographic structures of the Escherichia coli periplasmic protein FhuD bound to hydroxamate-type siderophores and the antibiotic albomycin J. Biol. Chem. 277, 13966-13972
    • (2002) J. Biol. Chem. , vol.277 , pp. 13966-13972
    • Clarke, T.E.1    Braun, V.2    Winkelmann, G.3    Tari, L.W.4    Vogel, H.J.5
  • 27
    • 0345492332 scopus 로고    scopus 로고
    • Synergy and contingency as driving forces for the evolution of multiple secondary metabolite production in Streptomyces species
    • Challis, G. L. and Hopwood, D. A. (2003) Synergy and contingency as driving forces for the evolution of multiple secondary metabolite production in Streptomyces species Proc. Natl. Acad. Sci. U.S.A. 25, 14555-14561
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.25 , pp. 14555-14561
    • Challis, G.L.1    Hopwood, D.A.2
  • 28
    • 66149116873 scopus 로고    scopus 로고
    • Trapping open and closed forms of FitE-A group III periplasmic binding protein
    • Shi, R., Proteau, A., Wagner, J., Cui, Q., Purisima, E. O., Matte, A., and Cygler, M. (2009) Trapping open and closed forms of FitE-A group III periplasmic binding protein Proteins 75, 598-605
    • (2009) Proteins , vol.75 , pp. 598-605
    • Shi, R.1    Proteau, A.2    Wagner, J.3    Cui, Q.4    Purisima, E.O.5    Matte, A.6    Cygler, M.7
  • 29
    • 0037424465 scopus 로고    scopus 로고
    • Crystal structures of the BtuF periplasmic-binding protein for vitamin B12 suggest a functionally important reduction in protein mobility upon ligand binding
    • Karpowich, N. K., Huang, H. H., Smith, P. C., and Hunt, J. F. (2003) Crystal structures of the BtuF periplasmic-binding protein for vitamin B12 suggest a functionally important reduction in protein mobility upon ligand binding J. Biol. Chem. 278, 8429-8434
    • (2003) J. Biol. Chem. , vol.278 , pp. 8429-8434
    • Karpowich, N.K.1    Huang, H.H.2    Smith, P.C.3    Hunt, J.F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.