메뉴 건너뛰기




Volumn 193, Issue 19, 2011, Pages 5374-5385

Novel hemin binding domains in the Corynebacterium diphtheriae HtaA protein interact with hemoglobin and are critical for heme iron utilization by HtaA

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; GLUTATHIONE TRANSFERASE; HEMIN; HEMOGLOBIN; HISTIDINE; HTAA PROTEIN; HTAB PROTEIN; IRON BINDING PROTEIN; TYROSINE; UNCLASSIFIED DRUG;

EID: 80053600205     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.05508-11     Document Type: Article
Times cited : (33)

References (48)
  • 1
    • 65249145115 scopus 로고    scopus 로고
    • HtaA is an iron-regulated hemin binding protein involved in the utilization of heme iron in Corynebacterium diphtheriae
    • Allen, C. E., and M. P. Schmitt. 2009. HtaA is an iron-regulated hemin binding protein involved in the utilization of heme iron in Corynebacterium diphtheriae. J. Bacteriol. 191:2638-2648.
    • (2009) J. Bacteriol. , vol.191 , pp. 2638-2648
    • Allen, C.E.1    Schmitt, M.P.2
  • 3
    • 17144469585 scopus 로고    scopus 로고
    • posting date. NEAT: a domain duplicated in genes near the components of a putative Fe3+ siderophore transporter from Gram-positive bacteria
    • 15 August research0047-research0047.5. doi:10.1186/gb-2002-3-9-research0047
    • Andrade, M. A., F. D. Ciccarelli, C. Perez-Iratxeta, and P. Bork. 15 August 2002, posting date. NEAT: a domain duplicated in genes near the components of a putative Fe3+ siderophore transporter from Gram-positive bacteria. Genome Biol. 3:research0047-research0047.5. doi:10.1186/gb-2002-3-9-research0047.
    • (2002) Genome Biol , vol.3
    • Andrade, M.A.1    Ciccarelli, F.D.2    Perez-Iratxeta, C.3    Bork, P.4
  • 4
    • 78649921851 scopus 로고    scopus 로고
    • Overcoming the heme paradox: heme toxicity and tolerance in bacterial pathogens
    • Anzaldi, L. L., and E. P. Skaar. 2010. Overcoming the heme paradox: heme toxicity and tolerance in bacterial pathogens. Infect. Immun. 78:4977-4989.
    • (2010) Infect. Immun. , vol.78 , pp. 4977-4989
    • Anzaldi, L.L.1    Skaar, E.P.2
  • 5
    • 0019763671 scopus 로고
    • Preparation and properties of apohemoglobin and reconstituted hemoglobins
    • Ascoli, F., M. R. Fanelli, and E. Antonini. 1981. Preparation and properties of apohemoglobin and reconstituted hemoglobins. Methods Enzymol. 76: 72-87.
    • (1981) Methods Enzymol , vol.76 , pp. 72-87
    • Ascoli, F.1    Fanelli, M.R.2    Antonini, E.3
  • 6
    • 0037371345 scopus 로고    scopus 로고
    • Identification and characterization of a Streptococcus pyogenes operon involved in binding of hemoproteins and acquisition of iron
    • Bates, C. S., G. E. Montanez, C. R. Woods, R. M. Vincent, and Z. Eichenbaum. 2003. Identification and characterization of a Streptococcus pyogenes operon involved in binding of hemoproteins and acquisition of iron. Infect. Immun. 71:1042-1055.
    • (2003) Infect. Immun. , vol.71 , pp. 1042-1055
    • Bates, C.S.1    Montanez, G.E.2    Woods, C.R.3    Vincent, R.M.4    Eichenbaum, Z.5
  • 7
    • 16544393485 scopus 로고    scopus 로고
    • Bacterial iron transport related to virulence
    • Braun, V. 2005. Bacterial iron transport related to virulence. Contrib. Microbiol. 12:210-233.
    • (2005) Contrib. Microbiol. , vol.12 , pp. 210-233
    • Braun, V.1
  • 8
    • 0036754957 scopus 로고    scopus 로고
    • Iron acquisition by gram-positive bacterial pathogens
    • Brown, J. S., and D. W. Holden. 2002. Iron acquisition by gram-positive bacterial pathogens. Microbes Infect. 4:1149-1156.
    • (2002) Microbes Infect , vol.4 , pp. 1149-1156
    • Brown, J.S.1    Holden, D.W.2
  • 9
    • 10744229660 scopus 로고    scopus 로고
    • The complete genome sequence and analysis of Corynebacterium diphtheriae NCTC13129
    • Cerdeño-Tárraga, A. M., et al. 2003. The complete genome sequence and analysis of Corynebacterium diphtheriae NCTC13129. Nucleic Acids Res. 31:6516-6523.
    • (2003) Nucleic Acids Res , vol.31 , pp. 6516-6523
    • Cerdeño-Tárraga, A.M.1
  • 10
    • 1542407100 scopus 로고    scopus 로고
    • IsdA of Staphylococcus aureus is a broad spectrum iron-regulated adhesin
    • Clarke, S. R., M. D. Wiltshire, and S. J. Foster. 2004. IsdA of Staphylococcus aureus is a broad spectrum iron-regulated adhesin. Mol. Microbiol. 51:1509-1519.
    • (2004) Mol. Microbiol. , vol.51 , pp. 1509-1519
    • Clarke, S.R.1    Wiltshire, M.D.2    Foster, S.J.3
  • 11
    • 0034878448 scopus 로고    scopus 로고
    • Understanding the mode of action of diphtheria toxin: a perspective on progress during the 20th century
    • Collier, R. J. 2001. Understanding the mode of action of diphtheria toxin: a perspective on progress during the 20th century. Toxicon 39:1793-1803.
    • (2001) Toxicon , vol.39 , pp. 1793-1803
    • Collier, R.J.1
  • 13
    • 0034128270 scopus 로고    scopus 로고
    • Corynebacterium diphtheriae genes required for acquisition of iron from hemin and hemoglobin are homologous to ABC hemin transporters
    • Drazek, E. S., C. A. Hammack, and M. P. Schmitt. 2000. Corynebacterium diphtheriae genes required for acquisition of iron from hemin and hemoglobin are homologous to ABC hemin transporters. Mol. Microbiol. 36:68-84.
    • (2000) Mol. Microbiol. , vol.36 , pp. 68-84
    • Drazek, E.S.1    Hammack, C.A.2    Schmitt, M.P.3
  • 14
    • 70450246905 scopus 로고    scopus 로고
    • Heme transfer to the bacterial cell envelope occurs via a secreted hemophore in the gram-positive pathogen Bacillus anthracis
    • Fabian, M., E. Solomaha, J. S. Olson, and A. W. Maresso. 2009. Heme transfer to the bacterial cell envelope occurs via a secreted hemophore in the gram-positive pathogen Bacillus anthracis. J. Biol. Chem. 284:32138-32146.
    • (2009) J. Biol. Chem. , vol.284 , pp. 32138-32146
    • Fabian, M.1    Solomaha, E.2    Olson, J.S.3    Maresso, A.W.4
  • 15
    • 55849096919 scopus 로고    scopus 로고
    • Shr is a broad-spectrum surface receptor that contributes to adherence and virulence in group A streptococcus
    • Fisher, M., et al. 2008. Shr is a broad-spectrum surface receptor that contributes to adherence and virulence in group A streptococcus. Infect. Immun. 76:5006-5015.
    • (2008) Infect. Immun. , vol.76 , pp. 5006-5015
    • Fisher, M.1
  • 17
    • 0027417443 scopus 로고
    • Cloning and characterization of the Vibrio cholerae genes encoding the utilization of iron from haemin and haemoglobin
    • Henderson, D. P., and S. M. Payne. 1993. Cloning and characterization of the Vibrio cholerae genes encoding the utilization of iron from haemin and haemoglobin. Mol. Microbiol. 7:461-469.
    • (1993) Mol. Microbiol. , vol.7 , pp. 461-469
    • Henderson, D.P.1    Payne, S.M.2
  • 18
    • 0344825084 scopus 로고    scopus 로고
    • Analysis of the Corynebacterium diphtheriae DtxR regulon: identification of a putative siderophore synthesis and transport system that is similar to the Yersinia high-pathogenicity islandencoded yersiniabactin synthesis and uptake system
    • Kunkle, C. A., and M. P. Schmitt. 2003. Analysis of the Corynebacterium diphtheriae DtxR regulon: identification of a putative siderophore synthesis and transport system that is similar to the Yersinia high-pathogenicity islandencoded yersiniabactin synthesis and uptake system. J. Bacteriol. 185:6826-6840.
    • (2003) J. Bacteriol. , vol.185 , pp. 6826-6840
    • Kunkle, C.A.1    Schmitt, M.P.2
  • 19
    • 11844281592 scopus 로고    scopus 로고
    • Analysis of a DtxR-regulated iron transport and siderophore biosynthesis gene cluster in Corynebacterium diphtheriae
    • Kunkle, C. A., and M. P. Schmitt. 2005. Analysis of a DtxR-regulated iron transport and siderophore biosynthesis gene cluster in Corynebacterium diphtheriae. J. Bacteriol. 187:422-433.
    • (2005) J. Bacteriol. , vol.187 , pp. 422-433
    • Kunkle, C.A.1    Schmitt, M.P.2
  • 20
    • 34247624144 scopus 로고    scopus 로고
    • Comparative analysis of hmuO function and expression in Corynebacterium species
    • Kunkle, C. A., and M. P. Schmitt. 2007. Comparative analysis of hmuO function and expression in Corynebacterium species. J. Bacteriol. 189:3650-3654.
    • (2007) J. Bacteriol. , vol.189 , pp. 3650-3654
    • Kunkle, C.A.1    Schmitt, M.P.2
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0036070707 scopus 로고    scopus 로고
    • Identification and characterization of a novel hemeassociated cell surface protein made by Streptococcus pyogenes
    • Lei, B., et al. 2002. Identification and characterization of a novel hemeassociated cell surface protein made by Streptococcus pyogenes. Infect. Immun. 70:4494-4500.
    • (2002) Infect. Immun. , vol.70 , pp. 4494-4500
    • Lei, B.1
  • 23
    • 0028170732 scopus 로고
    • Iron acquisition from heme and hemoglobin by a Serratia marcescens extracellular protein
    • Létoffé, S., J. M. Ghigo, and C. Wandersman. 1994. Iron acquisition from heme and hemoglobin by a Serratia marcescens extracellular protein. Proc. Natl. Acad. Sci. U. S. A. 91:9876-9880.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 9876-9880
    • Létoffé, S.1    Ghigo, J.M.2    Wandersman, C.3
  • 24
    • 23344441114 scopus 로고    scopus 로고
    • Heme transfer from streptococcal cell surface protein Shp to HtsA of transporter HtsABC
    • Liu, M., and B. Lei. 2005. Heme transfer from streptococcal cell surface protein Shp to HtsA of transporter HtsABC. Infect. Immun. 73:5086-5092.
    • (2005) Infect. Immun. , vol.73 , pp. 5086-5092
    • Liu, M.1    Lei, B.2
  • 25
    • 40549098798 scopus 로고    scopus 로고
    • Direct hemin transfer from IsdA to IsdC in the ironregulated surface determinant (Isd) heme acquisition system of Staphylococcus aureus
    • Liu, M., et al. 2008. Direct hemin transfer from IsdA to IsdC in the ironregulated surface determinant (Isd) heme acquisition system of Staphylococcus aureus. J. Biol. Chem. 283:6668-6676.
    • (2008) J. Biol. Chem. , vol.283 , pp. 6668-6676
    • Liu, M.1
  • 26
    • 50849124753 scopus 로고    scopus 로고
    • Bacillus anthracis secretes proteins that mediate heme acquisition from hemoglobin
    • Maresso, A. W., G. Garufi, and O. Schneewind. 2008. Bacillus anthracis secretes proteins that mediate heme acquisition from hemoglobin. PLoS Pathog. 4:e1000132.
    • (2008) PLoS Pathog , vol.4
    • Maresso, A.W.1    Garufi, G.2    Schneewind, O.3
  • 27
    • 0037423231 scopus 로고    scopus 로고
    • Passage of heme-iron across the envelope of Staphylococcus aureus
    • Mazmanian, S. K., et al. 2003. Passage of heme-iron across the envelope of Staphylococcus aureus. Science 299:906-909.
    • (2003) Science , vol.299 , pp. 906-909
    • Mazmanian, S.K.1
  • 28
    • 34848869068 scopus 로고    scopus 로고
    • Passively released heme from hemoglobin and myoglobin is a potential source of nutrient iron for Bordetella bronchiseptica
    • Mocny, J. C., J. S. Olson, and T. D. Connell. 2007. Passively released heme from hemoglobin and myoglobin is a potential source of nutrient iron for Bordetella bronchiseptica. Infect. Immun. 75:4857-4866.
    • (2007) Infect. Immun. , vol.75 , pp. 4857-4866
    • Mocny, J.C.1    Olson, J.S.2    Connell, T.D.3
  • 30
    • 77958592013 scopus 로고    scopus 로고
    • Shr of group A streptococcus is a new type of composite NEAT protein involved in sequestering haem from methemoglobin
    • Ouattara, M., et al. 2010. Shr of group A streptococcus is a new type of composite NEAT protein involved in sequestering haem from methemoglobin. Mol. Microbiol. 78:739-756.
    • (2010) Mol. Microbiol. , vol.78 , pp. 739-756
    • Ouattara, M.1
  • 31
    • 59449109486 scopus 로고    scopus 로고
    • Functionally distinct NEAT (NEAr Transporter) domains within the Staphylococcus aureus IsdH/HarA protein extract heme from methemoglobin
    • Pilpa, R. M., et al. 2009. Functionally distinct NEAT (NEAr Transporter) domains within the Staphylococcus aureus IsdH/HarA protein extract heme from methemoglobin. J. Biol. Chem. 284:1166-1176.
    • (2009) J. Biol. Chem. , vol.284 , pp. 1166-1176
    • Pilpa, R.M.1
  • 32
    • 0029859097 scopus 로고    scopus 로고
    • Molecular epidemiology of diphtheria in Russia, 1985-1994
    • Popovic, T., et al. 1996. Molecular epidemiology of diphtheria in Russia, 1985-1994. J. Infect. Dis. 174:1064-1072.
    • (1996) J. Infect. Dis. , vol.174 , pp. 1064-1072
    • Popovic, T.1
  • 33
    • 0031034090 scopus 로고    scopus 로고
    • Utilization of host iron sources by Corynebacterium diphtheriae: identification of a gene whose product is homologous to eukaryotic heme oxygenase and is required for acquisition of iron from heme and hemoglobin
    • Schmitt, M. P. 1997. Utilization of host iron sources by Corynebacterium diphtheriae: identification of a gene whose product is homologous to eukaryotic heme oxygenase and is required for acquisition of iron from heme and hemoglobin. J. Bacteriol. 179:838-845.
    • (1997) J. Bacteriol. , vol.179 , pp. 838-845
    • Schmitt, M.P.1
  • 34
    • 0030732290 scopus 로고    scopus 로고
    • Transcription of the Corynebacterium diphtheriae hmuO gene is regulated by iron and heme
    • Schmitt, M. P. 1997. Transcription of the Corynebacterium diphtheriae hmuO gene is regulated by iron and heme. Infect. Immun. 65:4634-4641.
    • (1997) Infect. Immun. , vol.65 , pp. 4634-4641
    • Schmitt, M.P.1
  • 35
    • 27744535908 scopus 로고    scopus 로고
    • Jorge H. Crosa, Alexandra R. Mey, and Shelley M. Payne (ed.), ASM Press, Washington, DC Iron transport in bacteria
    • Schmitt, M. P. 2004. Corynebacterium diphtheriae, p. 344-359. In Jorge H. Crosa, Alexandra R. Mey, and Shelley M. Payne (ed.), Iron transport in bacteria. ASM Press, Washington, DC.
    • (2004) Corynebacterium diphtheriae , pp. 344-359
    • Schmitt, M.P.1
  • 36
    • 0035139975 scopus 로고    scopus 로고
    • Construction and consequences of directed mutations affecting the hemin receptor in pathogenic Corynebacterium species
    • Schmitt, M. P., and E. S. Drazek. 2001. Construction and consequences of directed mutations affecting the hemin receptor in pathogenic Corynebacterium species. J. Bacteriol. 183:1476-1481.
    • (2001) J. Bacteriol. , vol.183 , pp. 1476-1481
    • Schmitt, M.P.1    Drazek, E.S.2
  • 37
    • 0345791519 scopus 로고    scopus 로고
    • IsdG and IsdI, hemedegrading enzymes in the cytoplasm of Staphylococcus aureus
    • Skaar, E. P., A. H. Gaspar, and O. Schneewind. 2004. IsdG and IsdI, hemedegrading enzymes in the cytoplasm of Staphylococcus aureus. J. Biol. Chem. 279:436-443.
    • (2004) J. Biol. Chem. , vol.279 , pp. 436-443
    • Skaar, E.P.1    Gaspar, A.H.2    Schneewind, O.3
  • 38
    • 0028086537 scopus 로고
    • Transport of hemin across the cytoplasmic membrane through a hemin-specific periplasmic binding-proteindependent transport system in Yersinia enterocolitica
    • Stojiljkovic, I., and K. Hantke. 1994. Transport of hemin across the cytoplasmic membrane through a hemin-specific periplasmic binding-proteindependent transport system in Yersinia enterocolitica. Mol. Microbiol. 13: 719-732.
    • (1994) Mol. Microbiol. , vol.13 , pp. 719-732
    • Stojiljkovic, I.1    Hantke, K.2
  • 39
    • 0036263269 scopus 로고    scopus 로고
    • Processing of heme and hemecontaining proteins by bacteria
    • Stojiljkovic, I., and D. Perkins-Balding. 2002. Processing of heme and hemecontaining proteins by bacteria. DNA Cell Biol. 21:281-295.
    • (2002) DNA Cell Biol , vol.21 , pp. 281-295
    • Stojiljkovic, I.1    Perkins-Balding, D.2
  • 40
    • 0024469837 scopus 로고
    • A 101- kilodalton heme-binding protein associated with Congo Red binding and virulence of Shigella flexneri and enteroinvasive Escherichia coli strains
    • Stugard, C. E., P. A. Daskaleros, and S. M. Payne. 1989. A 101-kilodalton heme-binding protein associated with Congo Red binding and virulence of Shigella flexneri and enteroinvasive Escherichia coli strains. Infect. Immun. 57:3534-3539.
    • (1989) Infect. Immun. , vol.57 , pp. 3534-3539
    • Stugard, C.E.1    Daskaleros, P.A.2    Payne, S.M.3
  • 41
    • 0025696065 scopus 로고
    • Coordinate regulation of siderophore and diphtheria toxin production by iron in Corynebacterium diphtheriae
    • Tai, S.-P., A. E. Krafft, P. Nootheti, and R. K. Holmes. 1990. Coordinate regulation of siderophore and diphtheria toxin production by iron in Corynebacterium diphtheriae. Microb. Pathog. 9:267-273.
    • (1990) Microb. Pathog. , vol.9 , pp. 267-273
    • Tai, S.-P.1    Krafft, A.E.2    Nootheti, P.3    Holmes, R.K.4
  • 42
    • 77954358807 scopus 로고    scopus 로고
    • A Bacillus anthracis S-layer homology protein that binds heme and mediates heme delivery to IsdC
    • Tarlovsky, Y., et al. 2010. A Bacillus anthracis S-layer homology protein that binds heme and mediates heme delivery to IsdC. J. Bacteriol. 192:3503-3511.
    • (2010) J. Bacteriol. , vol.192 , pp. 3503-3511
    • Tarlovsky, Y.1
  • 43
    • 33845428586 scopus 로고    scopus 로고
    • Staphylococcus aureus IsdB is a hemoglobin receptor required for heme iron utilization
    • Torres, V. J., G. Pishchany, M. Humayun, O. Schneewind, and E. P. Skaar. 2006. Staphylococcus aureus IsdB is a hemoglobin receptor required for heme iron utilization. J. Bacteriol. 188:8421-8429.
    • (2006) J. Bacteriol. , vol.188 , pp. 8421-8429
    • Torres, V.J.1    Pishchany, G.2    Humayun, M.3    Schneewind, O.4    Skaar, E.P.5
  • 44
    • 33846476692 scopus 로고    scopus 로고
    • Methemoglobin-it's not just blue: a concise review
    • Umbreit, J. 2007. Methemoglobin-it's not just blue: a concise review. Am. J. Hematol. 82:134-144.
    • (2007) Am. J. Hematol. , vol.82 , pp. 134-144
    • Umbreit, J.1
  • 45
    • 0031984521 scopus 로고    scopus 로고
    • Expression and characterization of a heme oxygenase (HmuO) from Corynebacterium diphtheriae
    • Wilks, A., and M. P. Schmitt. 1998. Expression and characterization of a heme oxygenase (HmuO) from Corynebacterium diphtheriae. J. Biol. Chem. 273:837-841.
    • (1998) J. Biol. Chem. , vol.273 , pp. 837-841
    • Wilks, A.1    Schmitt, M.P.2
  • 46
    • 0036670736 scopus 로고    scopus 로고
    • Microbial siderophore-mediated transport
    • Winkelmann, G. 2002. Microbial siderophore-mediated transport. Biochem. Soc. Trans. 30:691-696.
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 691-696
    • Winkelmann, G.1
  • 47
    • 40549124374 scopus 로고    scopus 로고
    • The surface protein Shr of Streptococcus pyogenes binds heme and transfers it to the streptococcal heme-binding protein Shp
    • Zhu, H., M. Liu, and B. Lei. 2008. The surface protein Shr of Streptococcus pyogenes binds heme and transfers it to the streptococcal heme-binding protein Shp. BMC Microbiol. 8:15.
    • (2008) BMC Microbiol , vol.8 , pp. 15
    • Zhu, H.1    Liu, M.2    Lei, B.3
  • 48
    • 49649090027 scopus 로고    scopus 로고
    • Pathway for heme uptake from human methemoglobin by the iron-regulated surface determinants (Isd) system of Staphylococcus aureus
    • Zhu, et al. 2008. Pathway for heme uptake from human methemoglobin by the iron-regulated surface determinants (Isd) system of Staphylococcus aureus. J. Biol. Chem. 283:18450-18460.
    • (2008) J. Biol. Chem. , vol.283 , pp. 18450-18460
    • Zhu1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.