메뉴 건너뛰기




Volumn 181, Issue 5, 1999, Pages 1436-1443

Identification and characterization of SirA, an iron-regulated protein from Staphylococcus aureus

Author keywords

[No Author keywords available]

Indexed keywords

IRON REGULATORY FACTOR;

EID: 0032985815     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.181.5.1436-1443.1999     Document Type: Article
Times cited : (58)

References (33)
  • 1
    • 0027537675 scopus 로고
    • Lipid modification of the 17-kilodalton membrane immunogen of Treponema pallidum determines macrophage activation as well as amphiphilicity
    • Akins, D. R., B. K. Purcell, M. M. Mitra, M. V. Norgard, and J. D. Radolf. 1993. Lipid modification of the 17-kilodalton membrane immunogen of Treponema pallidum determines macrophage activation as well as amphiphilicity. Infect. Immun. 61:1202-1210.
    • (1993) Infect. Immun. , vol.61 , pp. 1202-1210
    • Akins, D.R.1    Purcell, B.K.2    Mitra, M.M.3    Norgard, M.V.4    Radolf, J.D.5
  • 4
    • 0031871386 scopus 로고    scopus 로고
    • Molecular cloning of a 32-kilodalton lipoprotein component of a novel iron-regulated Staphylococcus epidermids ABC transporter
    • Cockayne, A., P. J. Hill, N. B. L. Powell, K. Bishop, C. Sims, and P. Williams. 1998. Molecular cloning of a 32-kilodalton lipoprotein component of a novel iron-regulated Staphylococcus epidermids ABC transporter. Infect. Immun. 66:3767-3774.
    • (1998) Infect. Immun. , vol.66 , pp. 3767-3774
    • Cockayne, A.1    Hill, P.J.2    Powell, N.B.L.3    Bishop, K.4    Sims, C.5    Williams, P.6
  • 5
    • 0030969403 scopus 로고    scopus 로고
    • Siderophore production by Staphylococcus aureus and identification of iron-regulated proteins
    • Courcol, R., D. Trivier, M.-C. Bissinger, G. R. Martin, and M. R. W. Brown. 1997. Siderophore production by Staphylococcus aureus and identification of iron-regulated proteins. Infect. Immun. 65:1944-1948.
    • (1997) Infect. Immun. , vol.65 , pp. 1944-1948
    • Courcol, R.1    Trivier, D.2    Bissinger, M.-C.3    Martin, G.R.4    Brown, M.R.W.5
  • 6
    • 0003208241 scopus 로고    scopus 로고
    • Uptake and metabolism of iron and molybdenum
    • F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), ASM Press, Washington, D.C.
    • Earhart, C. F. 1996. Uptake and metabolism of iron and molybdenum, p. 1075-1090. In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology, vol. 1. ASM Press, Washington, D.C.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology , vol.1 , pp. 1075-1090
    • Earhart, C.F.1
  • 7
    • 0029653518 scopus 로고
    • Whole-genome random sequencing and assembly of Haemophilus influenzae Rd
    • Fleischmann, R. D., et al. 1995. Whole-genome random sequencing and assembly of Haemophilus influenzae Rd. Science 269:469-512.
    • (1995) Science , vol.269 , pp. 469-512
    • Fleischmann, R.D.1
  • 8
    • 0028031926 scopus 로고
    • Isolation and biological characterization of staphyloferrin B, a compound with siderophore activity from staphylococci
    • Haag, H., H.-P. Fiedler, J. Meiwes, H. Drechsel, G. Jung, and H. Zähner. 1994. Isolation and biological characterization of staphyloferrin B, a compound with siderophore activity from staphylococci. FEMS Microbiol. Lett. 115:125-130.
    • (1994) FEMS Microbiol. Lett. , vol.115 , pp. 125-130
    • Haag, H.1    Fiedler, H.-P.2    Meiwes, J.3    Drechsel, H.4    Jung, G.5    Zähner, H.6
  • 9
    • 0023443062 scopus 로고
    • Selection procedure for deregulated iron transport mutants (fur) in Escherichia coli K12: Fur not only affects iron metabolism
    • Hantke, K. 1987. Selection procedure for deregulated iron transport mutants (fur) in Escherichia coli K12: fur not only affects iron metabolism. Mol. Gen. Genet. 210:135-139.
    • (1987) Mol. Gen. Genet. , vol.210 , pp. 135-139
    • Hantke, K.1
  • 10
    • 0030199715 scopus 로고    scopus 로고
    • Identification and analysis of a gene encoding a Fur-like protein of Staphylococcus epidermidis
    • Heidrich, C., K. Hantke, G. Bierbaum, and H.-G. Sahl. 1996. Identification and analysis of a gene encoding a Fur-like protein of Staphylococcus epidermidis. FEMS Microbiol. Lett. 140:253-259.
    • (1996) FEMS Microbiol. Lett. , vol.140 , pp. 253-259
    • Heidrich, C.1    Hantke, K.2    Bierbaum, G.3    Sahl, H.-G.4
  • 11
    • 0030045982 scopus 로고    scopus 로고
    • Characterization of the sar locus and its interaction with agr in Staphylococcus aureus
    • Heinrichs, J. H., M. G, Bayer, and A. L. Cheung. 1996. Characterization of the sar locus and its interaction with agr in Staphylococcus aureus. J. Bacteriol. 178:418-423.
    • (1996) J. Bacteriol. , vol.178 , pp. 418-423
    • Heinrichs, J.H.1    Bayer, M.G.2    Cheung, A.L.3
  • 13
    • 0002014616 scopus 로고
    • agr: A polycistronic locus regulating exoprotein synthesis in Staphylococcus aureus
    • R. P. Novick (ed.), VCH Publishers, New York, N.Y.
    • Kornblum, J., B. Kreiswirth, S. J. Projan, and R. P. Novick. 1990. agr: a polycistronic locus regulating exoprotein synthesis in Staphylococcus aureus, p. 373-402. In R. P. Novick (ed.), Molecular biology of the staphylococci. VCH Publishers, New York, N.Y.
    • (1990) Molecular Biology of the Staphylococci , pp. 373-402
    • Kornblum, J.1    Kreiswirth, B.2    Projan, S.J.3    Novick, R.P.4
  • 14
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 0028284677 scopus 로고
    • Staphylococcal iron requirements, siderophore production, and iron-regulated protein expression
    • Lindsay, J. A., and T. V. Riley. 1994. Staphylococcal iron requirements, siderophore production, and iron-regulated protein expression. Infect. Immun. 62:2309-2314.
    • (1994) Infect. Immun. , vol.62 , pp. 2309-2314
    • Lindsay, J.A.1    Riley, T.V.2
  • 16
    • 0028826326 scopus 로고
    • Differential expression of two siderophore-dependent iron-acquisition pathways in Erwinia chrysanthemi 3937: Characterization of a novel ferrisiderophore permease of the ABC transporter family
    • Mahé, B., C. Masclaux, L. Rauscher, C. Enard, and D. Expert. 1995. Differential expression of two siderophore-dependent iron-acquisition pathways in Erwinia chrysanthemi 3937: characterization of a novel ferrisiderophore permease of the ABC transporter family. Mol. Microbiol. 18:33-43.
    • (1995) Mol. Microbiol. , vol.18 , pp. 33-43
    • Mahé, B.1    Masclaux, C.2    Rauscher, L.3    Enard, C.4    Expert, D.5
  • 17
    • 0025707185 scopus 로고
    • Isolation and characterization of staphyloferrin A, a compound with siderophore activity from Staphylococcus hyicus DSM 20459
    • Meiwes, J., H. P. Fiedler, H. Haag, H. Zähner, Konetschny, A. Rapp, and G. Jung. 1990. Isolation and characterization of staphyloferrin A, a compound with siderophore activity from Staphylococcus hyicus DSM 20459. FEMS Microbiol. Lett. 55:201-205.
    • (1990) FEMS Microbiol. Lett. , vol.55 , pp. 201-205
    • Meiwes, J.1    Fiedler, H.P.2    Haag, H.3    Zähner, H.4    Konetschny5    Rapp, A.6    Jung, G.7
  • 18
    • 0028133393 scopus 로고
    • Staphylococci express a receptor for human transferrin: Identification of a 42-kilodalton cell wall transferrin-binding protein
    • Modun, B., D. Kendall, and P. Williams. 1994. Staphylococci express a receptor for human transferrin: identification of a 42-kilodalton cell wall transferrin-binding protein. Infect. Immun. 62:3850-3858.
    • (1994) Infect. Immun. , vol.62 , pp. 3850-3858
    • Modun, B.1    Kendall, D.2    Williams, P.3
  • 19
    • 0025837196 scopus 로고
    • Genetic systems in staphylococci
    • Novick, R. P. 1991. Genetic systems in staphylococci. Methods Enzymol. 204: 587-636.
    • (1991) Methods Enzymol. , vol.204 , pp. 587-636
    • Novick, R.P.1
  • 20
    • 0014127769 scopus 로고
    • Properties of a cryptic high-frequency transducing phage in Staphylococcus aureus
    • Novick, R. P. 1967. Properties of a cryptic high-frequency transducing phage in Staphylococcus aureus. Virology 33:155-166.
    • (1967) Virology , vol.33 , pp. 155-166
    • Novick, R.P.1
  • 21
    • 0025178972 scopus 로고
    • Lipid modification of the 15 kilodalton major membrane immunogen of Treponema pallidum
    • Purcell, B. K., M. A. Swancutt, and J. D. Radolf. 1990. Lipid modification of the 15 kilodalton major membrane immunogen of Treponema pallidum. Mol. Microbiol. 4:1371-1379.
    • (1990) Mol. Microbiol. , vol.4 , pp. 1371-1379
    • Purcell, B.K.1    Swancutt, M.A.2    Radolf, J.D.3
  • 22
    • 0002079266 scopus 로고
    • Transport mechanisms
    • A. L. Sonenshein, J. A. Hoch, and R. Losick (ed.), American Society for Microbiology, Washington, D.C.
    • Saier, M. H., Jr., M. J. Fagan, C. Hoischen, and J. Reizer. 1993. Transport mechanisms, p. 133-156. In A. L. Sonenshein, J. A. Hoch, and R. Losick (ed.), Bacillus subtilis and other gram-positive bacteria. American Society for Microbiology, Washington, D.C.
    • (1993) Bacillus Subtilis and Other Gram-positive Bacteria , pp. 133-156
    • Saier M.H., Jr.1    Fagan, M.J.2    Hoischen, C.3    Reizer, J.4
  • 24
    • 0027468111 scopus 로고
    • Iron-hydroxamate uptake systems in Bacillus subtilis: Identification of a lipoprotein as part of binding protein-dependent transport system
    • Schneider, R., and K. Hantke. 1993. Iron-hydroxamate uptake systems in Bacillus subtilis: identification of a lipoprotein as part of binding protein-dependent transport system. Mol. Microbiol. 8:111-121.
    • (1993) Mol. Microbiol. , vol.8 , pp. 111-121
    • Schneider, R.1    Hantke, K.2
  • 25
    • 0023127806 scopus 로고
    • Universal chemical assay for the detection and determination of siderophores
    • Schwyn, B., and J. B. Neilands. 1987. Universal chemical assay for the detection and determination of siderophores. Anal. Biochem. 160:47-55.
    • (1987) Anal. Biochem. , vol.160 , pp. 47-55
    • Schwyn, B.1    Neilands, J.B.2
  • 26
    • 0028327173 scopus 로고
    • Fur regulon in gram-negative bacteria. Identification and characterization of new iron-regulated Escherichia coli genes by a fur titration assay
    • Stojiljkovic, I., A. J. Bäumler, and K. Hantke. 1994. Fur regulon in gram-negative bacteria. Identification and characterization of new iron-regulated Escherichia coli genes by a fur titration assay. J. Mol. Biol. 236:531-545.
    • (1994) J. Mol. Biol. , vol.236 , pp. 531-545
    • Stojiljkovic, I.1    Bäumler, A.J.2    Hantke, K.3
  • 27
    • 0027254484 scopus 로고
    • Protective immunity elicited by recombinant Bacille Calmette-Guerin (BCG) expressing outer surface protein A (OspA) lipoprotein: A candidate Lyme disease vaccine
    • Stover, C. K., G. P. Bansal, M. S. Hanson, J. E. Burlein, S. R. Palaszynski, J. F. Young, S. Koenig, D. B. Young, A. Sadziene, and A. G. Barbour. 1993. Protective immunity elicited by recombinant Bacille Calmette-Guerin (BCG) expressing outer surface protein A (OspA) lipoprotein: a candidate Lyme disease vaccine. J. Exp. Med. 178:197-209.
    • (1993) J. Exp. Med. , vol.178 , pp. 197-209
    • Stover, C.K.1    Bansal, G.P.2    Hanson, M.S.3    Burlein, J.E.4    Palaszynski, S.R.5    Young, J.F.6    Koenig, S.7    Young, D.B.8    Sadziene, A.9    Barbour, A.G.10
  • 28
    • 0028987131 scopus 로고
    • Lipoproteins of gram-positive bacteria
    • Sutcliffe, I. C., and R. R. B. Russell. 1995. Lipoproteins of gram-positive bacteria. J. Bacteriol. 177:1123-1128.
    • (1995) J. Bacteriol. , vol.177 , pp. 1123-1128
    • Sutcliffe, I.C.1    Russell, R.R.B.2
  • 29
    • 0027256676 scopus 로고
    • Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria
    • Tam, R., and M. H. Saier, Jr. 1993. Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria. Microbiol. Rev. 57:320-346.
    • (1993) Microbiol. Rev. , vol.57 , pp. 320-346
    • Tam, R.1    Saier M.H., Jr.2
  • 30
    • 0030222101 scopus 로고    scopus 로고
    • Iron depletion and virulence in Staphylococcus aureus
    • Trivier, D., and R. J. Courcol. 1996. Iron depletion and virulence in Staphylococcus aureus. FEMS Microbiol. Lett. 141:117-127.
    • (1996) FEMS Microbiol. Lett. , vol.141 , pp. 117-127
    • Trivier, D.1    Courcol, R.J.2
  • 31
    • 0020442864 scopus 로고
    • The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers
    • Vieria, J., and J. Messing. 1982. The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers. Gene 19:259.
    • (1982) Gene , vol.19 , pp. 259
    • Vieria, J.1    Messing, J.2
  • 32
    • 0024393453 scopus 로고
    • The structure of signal peptides from bacterial lipoproteins
    • von Heijne, G. 1989. The structure of signal peptides from bacterial lipoproteins. Protein Eng. 2:531-534.
    • (1989) Protein Eng. , vol.2 , pp. 531-534
    • Von Heijne, G.1
  • 33
    • 84949189494 scopus 로고
    • Folding and purification of insoluble (inclusion body) proteins from Escherichia coli
    • J. E. Coligan, B. M. Dunn, H. L. Ploegh, D. W. Speicher, and P. T. Wingfield (ed.), John Wiley & Sons, Inc., New York, N.Y.
    • Wingfield, P. T., I. Palmer, and S. Liang. 1995. Folding and purification of insoluble (inclusion body) proteins from Escherichia coli. p. 6.5.1-6.5.27. In J. E. Coligan, B. M. Dunn, H. L. Ploegh, D. W. Speicher, and P. T. Wingfield (ed.), Current protocols in protein science, vol. 1. John Wiley & Sons, Inc., New York, N.Y.
    • (1995) Current Protocols in Protein Science , vol.1 , pp. 651-6527
    • Wingfield, P.T.1    Palmer, I.2    Liang, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.