메뉴 건너뛰기




Volumn 582, Issue 9, 2008, Pages 1351-1354

Lipoprotein MtsA of MtsABC in Streptococcus pyogenes primarily binds ferrous ion with bicarbonate as a synergistic anion

Author keywords

Bicarbonate; Ferrous ion; Metal binding; MtsA; Streptococcus pyogenes

Indexed keywords

BICARBONATE; BINDING PROTEIN; CUPRIC ION; FERRIC ION; FERROUS ION; MANGANESE; PROTEIN MTSA; TRANSFERRIN; UNCLASSIFIED DRUG; ZINC ION;

EID: 41449096957     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2008.03.020     Document Type: Article
Times cited : (30)

References (24)
  • 1
    • 0033759220 scopus 로고    scopus 로고
    • Iron metabolism in pathogenic bacteria
    • Ratledge C., and Dover L.G. Iron metabolism in pathogenic bacteria. Annu. Rev. Microbiol. 54 (2000) 881-941
    • (2000) Annu. Rev. Microbiol. , vol.54 , pp. 881-941
    • Ratledge, C.1    Dover, L.G.2
  • 2
    • 0033939735 scopus 로고    scopus 로고
    • Pathogenesis of group A streptococcal infections
    • Cunningham M.W. Pathogenesis of group A streptococcal infections. Clin. Microbiol. Rev. 13 (2000) 470-511
    • (2000) Clin. Microbiol. Rev. , vol.13 , pp. 470-511
    • Cunningham, M.W.1
  • 3
    • 0032746814 scopus 로고    scopus 로고
    • Identification and characterization of a Streptococcus pyogenes ABC transporter with multiple specificity for metal cations
    • Janulczyk R., Pallon J., and Bjorck L. Identification and characterization of a Streptococcus pyogenes ABC transporter with multiple specificity for metal cations. Mol. Microbiol. 34 (1999) 596-606
    • (1999) Mol. Microbiol. , vol.34 , pp. 596-606
    • Janulczyk, R.1    Pallon, J.2    Bjorck, L.3
  • 4
    • 0037407638 scopus 로고    scopus 로고
    • MtsABC is important for manganese and iron transport, oxidative stress resistance, and virulence of Streptococcus pyogenes
    • Janulczyk R., Ricci S., and Bjorck L. MtsABC is important for manganese and iron transport, oxidative stress resistance, and virulence of Streptococcus pyogenes. Infect. Immun. 71 (2003) 2656-2664
    • (2003) Infect. Immun. , vol.71 , pp. 2656-2664
    • Janulczyk, R.1    Ricci, S.2    Bjorck, L.3
  • 5
    • 0028987131 scopus 로고
    • Lipoproteins of Gram-positive bacteria
    • Sutcliffe I.C., and Russell R.R. Lipoproteins of Gram-positive bacteria. J. Bacteriol. 177 (1995) 1123-1128
    • (1995) J. Bacteriol. , vol.177 , pp. 1123-1128
    • Sutcliffe, I.C.1    Russell, R.R.2
  • 6
    • 0141668997 scopus 로고    scopus 로고
    • Identification and characterization of HtsA, a second heme-binding protein made by Streptococcus pyogenes
    • Lei B., Liu M., Voyich J.M., Prater C.I., Kala S.V., DeLeo F.R., and Musser J.M. Identification and characterization of HtsA, a second heme-binding protein made by Streptococcus pyogenes. Infect. Immun. 71 (2003) 5962-5969
    • (2003) Infect. Immun. , vol.71 , pp. 5962-5969
    • Lei, B.1    Liu, M.2    Voyich, J.M.3    Prater, C.I.4    Kala, S.V.5    DeLeo, F.R.6    Musser, J.M.7
  • 8
    • 34547404155 scopus 로고    scopus 로고
    • A proteomic approach for the identification of bismuth-binding proteins in Helicobacter pylori
    • Ge R., et al. A proteomic approach for the identification of bismuth-binding proteins in Helicobacter pylori. J. Biol. Inorg. Chem. 12 (2007) 831-842
    • (2007) J. Biol. Inorg. Chem. , vol.12 , pp. 831-842
    • Ge, R.1
  • 9
    • 0037541161 scopus 로고    scopus 로고
    • Serum biomarkers of hepatitis B virus infected liver inflammation: a proteomic study
    • He Q.Y., Lau G.K., Zhou Y., Yuen S.T., Lin M.C., Kung H.F., and Chiu J.F. Serum biomarkers of hepatitis B virus infected liver inflammation: a proteomic study. Proteomics 3 (2003) 666-674
    • (2003) Proteomics , vol.3 , pp. 666-674
    • He, Q.Y.1    Lau, G.K.2    Zhou, Y.3    Yuen, S.T.4    Lin, M.C.5    Kung, H.F.6    Chiu, J.F.7
  • 10
    • 33748372299 scopus 로고    scopus 로고
    • Thermodynamic and kinetic aspects of metal binding to the histidine-rich protein, Hpn
    • Ge R., Zhang Y., Sun X., Watt R.M., He Q.Y., Huang J.D., Wilcox D.E., and Sun H. Thermodynamic and kinetic aspects of metal binding to the histidine-rich protein, Hpn. J. Am. Chem. Soc. 128 (2006) 11330-11331
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 11330-11331
    • Ge, R.1    Zhang, Y.2    Sun, X.3    Watt, R.M.4    He, Q.Y.5    Huang, J.D.6    Wilcox, D.E.7    Sun, H.8
  • 11
    • 0035818422 scopus 로고    scopus 로고
    • Interactions of bismuth with human lactoferrin and recognition of the Bi(III)-lactoferrin complex by intestinal cells
    • Zhang L., Szeto K.Y., Wong W.B., Loh T.T., Sadler P.J., and Sun H. Interactions of bismuth with human lactoferrin and recognition of the Bi(III)-lactoferrin complex by intestinal cells. Biochemistry 40 (2001) 13281-13287
    • (2001) Biochemistry , vol.40 , pp. 13281-13287
    • Zhang, L.1    Szeto, K.Y.2    Wong, W.B.3    Loh, T.T.4    Sadler, P.J.5    Sun, H.6
  • 12
    • 4344645436 scopus 로고    scopus 로고
    • a value of iron-binding ligand Tyr188 and its implication in iron release and anion binding of human transferrin
    • a value of iron-binding ligand Tyr188 and its implication in iron release and anion binding of human transferrin. FEBS Lett. 573 (2004) 181-185
    • (2004) FEBS Lett. , vol.573 , pp. 181-185
    • Sun, X.1    Sun, H.2    Ge, R.3    Richter, M.4    Woodworth, R.C.5    Mason, A.B.6    He, Q.Y.7
  • 13
    • 0001790974 scopus 로고    scopus 로고
    • The iron-uptake systems of pathogenic bacteria, fungi and potozoa
    • Bullen J.J., and Griffiths E. (Eds), John Wiley & Sons, NY
    • Griffiths E., and Williams P. The iron-uptake systems of pathogenic bacteria, fungi and potozoa. In: Bullen J.J., and Griffiths E. (Eds). Iron and Infection: Molecular, Physiological and Clinical Aspects (1999), John Wiley & Sons, NY 87-212
    • (1999) Iron and Infection: Molecular, Physiological and Clinical Aspects , pp. 87-212
    • Griffiths, E.1    Williams, P.2
  • 14
    • 0036754957 scopus 로고    scopus 로고
    • Iron acquisition by Gram-positive bacterial pathogens
    • Brown J.S., and Holden D.W. Iron acquisition by Gram-positive bacterial pathogens. Microbes Infect. 4 (2002) 1149-1156
    • (2002) Microbes Infect. , vol.4 , pp. 1149-1156
    • Brown, J.S.1    Holden, D.W.2
  • 15
    • 27744530244 scopus 로고    scopus 로고
    • ABC transporter FtsABCD of Streptococcus pyogenes mediates uptake of ferric ferrichrome
    • Hanks T.S., Liu M., McClure M.J., and Lei B. ABC transporter FtsABCD of Streptococcus pyogenes mediates uptake of ferric ferrichrome. BMC Microbiol. 5 (2005) 62
    • (2005) BMC Microbiol. , vol.5 , pp. 62
    • Hanks, T.S.1    Liu, M.2    McClure, M.J.3    Lei, B.4
  • 17
    • 0015808508 scopus 로고
    • Exchangeability of bicarbonate specifically bound to transferrin
    • Aisen P., Leibman A., Pinkowitz R.A., and Pollack S. Exchangeability of bicarbonate specifically bound to transferrin. Biochemistry 12 (1973) 3679-3684
    • (1973) Biochemistry , vol.12 , pp. 3679-3684
    • Aisen, P.1    Leibman, A.2    Pinkowitz, R.A.3    Pollack, S.4
  • 20
    • 0002526768 scopus 로고
    • The molecular mechanism of the bicarbonate effect at the plastoquinone reductase site of photosynthesis
    • Blubaugh D., and Govindjee. The molecular mechanism of the bicarbonate effect at the plastoquinone reductase site of photosynthesis. Photosynth. Res. 19 (1988) 85-128
    • (1988) Photosynth. Res. , vol.19 , pp. 85-128
    • Blubaugh, D.1    Govindjee2
  • 21
    • 0016591336 scopus 로고
    • 3+ to transferrin in the absence of synergistic anions
    • 3+ to transferrin in the absence of synergistic anions. J. Biol. Chem. 250 (1975) 2177-2181
    • (1975) J. Biol. Chem. , vol.250 , pp. 2177-2181
    • Bates, G.W.1    Schlabach, M.R.2
  • 22
    • 0016669917 scopus 로고
    • 3+ by transferrin. Implications for the interlocking sites hypothesis
    • 3+ by transferrin. Implications for the interlocking sites hypothesis. J. Biol. Chem. 250 (1975) 2182-2188
    • (1975) J. Biol. Chem. , vol.250 , pp. 2182-2188
    • Schlabach, M.R.1    Bates, G.W.2
  • 23
    • 1642550025 scopus 로고    scopus 로고
    • Iron chemistry
    • Templeton D.M. (Ed), Marcel Dekker, NY
    • Harris W.R. Iron chemistry. In: Templeton D.M. (Ed). Molecular and Cellular Iron Transport (2002), Marcel Dekker, NY 1-35
    • (2002) Molecular and Cellular Iron Transport , pp. 1-35
    • Harris, W.R.1
  • 24
    • 33748056473 scopus 로고    scopus 로고
    • Differential regulation of iron- and manganese-specific MtsABC and heme-specific HtsABC transporters by the metalloregulator MtsR of group A Streptococcus
    • Hanks T.S., Liu M., McClure M.J., Fukumura M., Duffy A., and Lei B. Differential regulation of iron- and manganese-specific MtsABC and heme-specific HtsABC transporters by the metalloregulator MtsR of group A Streptococcus. Infect. Immun. 74 (2006) 5132-5139
    • (2006) Infect. Immun. , vol.74 , pp. 5132-5139
    • Hanks, T.S.1    Liu, M.2    McClure, M.J.3    Fukumura, M.4    Duffy, A.5    Lei, B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.