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Volumn 8, Issue 10, 2009, Pages 1584-1591

The monothiol single-domain glutaredoxin is conserved in the highly reduced mitochondria of giardia intestinalis

Author keywords

[No Author keywords available]

Indexed keywords

GIARDIA INTESTINALIS;

EID: 70349664752     PISSN: 15359778     EISSN: None     Source Type: Journal    
DOI: 10.1128/EC.00181-09     Document Type: Article
Times cited : (19)

References (31)
  • 2
    • 65549160983 scopus 로고    scopus 로고
    • Evolution based on domain combinations: The case of glutaredoxins
    • Alves, R., E. Vilaprinyo, A. Sorribas, and E. Herrero. 2009. Evolution based on domain combinations: the case of glutaredoxins. BMC Evol. Biol. 9:66.
    • (2009) BMC Evol. Biol , vol.9 , pp. 66
    • Alves, R.1    Vilaprinyo, E.2    Sorribas, A.3    Herrero, E.4
  • 4
    • 0027525402 scopus 로고
    • Cysteine is the major low-molecular weight thiol in Giardia duodenalis
    • Brown, D. M., J. A. Upcroft, and P. Upcroft. 1993. Cysteine is the major low-molecular weight thiol in Giardia duodenalis. Mol. Biochem. Parasitol. 61:155-158.
    • (1993) Mol. Biochem. Parasitol , vol.61 , pp. 155-158
    • Brown, D.M.1    Upcroft, J.A.2    Upcroft, P.3
  • 5
    • 34547919212 scopus 로고    scopus 로고
    • Frataxin, a conserved mitochondrial protein, in the hydrogenosome of Trichomonas vaginalis
    • Dolezal, P., A. Daneis, E. Lesuisse, R. Sutak, I. Hrdy, T. M. Embley, and J. Tachezy. 2007. Frataxin, a conserved mitochondrial protein, in the hydrogenosome of Trichomonas vaginalis. Eukaryot. Cell 6:1431-1438.
    • (2007) Eukaryot. Cell , vol.6 , pp. 1431-1438
    • Dolezal, P.1    Daneis, A.2    Lesuisse, E.3    Sutak, R.4    Hrdy, I.5    Embley, T.M.6    Tachezy, J.7
  • 7
    • 33645456207 scopus 로고    scopus 로고
    • Eukaryotic evolution, changes and challenges
    • Embley, T. M., and W. Martin. 2006. Eukaryotic evolution, changes and challenges. Nature 440:623-630.
    • (2006) Nature , vol.440 , pp. 623-630
    • Embley, T.M.1    Martin, W.2
  • 8
    • 33745614344 scopus 로고    scopus 로고
    • Structural insight into poplar glutaredoxin C1 with a bridging iron-sulfur cluster at the active site
    • DOI 10.1021/bi060444t
    • Feng, Y., N. Zhong, N. Rouhier, T. Hase, M. Kusunoki, J. P. Jacquot, C. Jin, and B. Xia. 2006. Structural insight into poplar glutaredoxin Cl with a bridging iron-sulfur cluster at the active site. Biochemistry 45:7998-8008. (Pubitemid 43993221)
    • (2006) Biochemistry , vol.45 , Issue.26 , pp. 7998-8008
    • Feng, Y.1    Zhong, N.2    Rouhier, N.3    Hase, T.4    Kusunoki, M.5    Jacquot, J.-P.6    Jin, C.7    Xia, B.8
  • 10
    • 0002051540 scopus 로고    scopus 로고
    • BioEdit: A user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT
    • Hall, T. A. 1999. BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nucleic Acids Symp. Ser. 41:95-98.
    • (1999) Nucleic Acids Symp. ser , vol.41 , pp. 95-98
    • Hall, T.A.1
  • 11
    • 84895187735 scopus 로고    scopus 로고
    • Reference deleted.
    • Reference deleted.
  • 12
    • 20744446399 scopus 로고    scopus 로고
    • Structure, function, and formation of biological iron-sulfur clusters
    • Johnson, D. C., D. R. Dean, A. D. Smith, and M. K. Johnson. 2005. Structure, function, and formation of biological iron-sulfur clusters. Annu. Rev. Biochem. 74:247-281.
    • (2005) Annu. Rev. Biochem , vol.74 , pp. 247-281
    • Johnson, D.C.1    Dean, D.R.2    Smith, A.D.3    Johnson, M.K.4
  • 13
    • 0020651210 scopus 로고
    • Axenic culture of Giardia lamblia in TYI-S-33 medium supplemented with bile
    • Keister, D. B. 1983. Axenic culture of Giardia lamblia in TYI-S-33 medium supplemented with bile. Trans. R. Soc. Trop. Med. Hyg. 77:487-488.
    • (1983) Trans. R. Soc. Trop. Med. Hyg , vol.77 , pp. 487-488
    • Keister, D.B.1
  • 14
    • 0033565665 scopus 로고    scopus 로고
    • The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins
    • DOI 10.1093/emboj/18.14.3981
    • Kispal, G., P. Csere, C. Prohl, and R. Lill. 1999. The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins. EMBO J. 18:3981-3989. (Pubitemid 29335851)
    • (1999) EMBO Journal , vol.18 , Issue.14 , pp. 3981-3989
    • Kispal, G.1    Csere, P.2    Prohl, C.3    Lill, R.4
  • 15
    • 47249094614 scopus 로고    scopus 로고
    • Maturation of iron-sulfur proteins in eukaryotes: Mechanisms, connected processes, and diseases
    • Lill, R., and U. Muhlenhoff. 2008. Maturation of iron-sulfur proteins in eukaryotes: mechanisms, connected processes, and diseases. Annu. Rev. Biochem. 77:669-700.
    • (2008) Annu. Rev. Biochem , vol.77 , pp. 669-700
    • Lill, R.1    Muhlenhoff, U.2
  • 18
    • 0141737067 scopus 로고    scopus 로고
    • Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p
    • DOI 10.1093/emboj/cdg446
    • Mühlenhoff, U., J. Gerber, N. Richhardt, and R. Lill. 2003. Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p. EMBO J. 22:4815-4825. (Pubitemid 37162917)
    • (2003) EMBO Journal , vol.22 , Issue.18 , pp. 4815-4825
    • Muhlenhoff, U.1    Gerber, J.2    Richhardt, N.3    Lill, R.4
  • 19
    • 2242453224 scopus 로고    scopus 로고
    • Characterization of iron-sulfur protein assembly in isolated mitochondria-a requirement for ATP, NADH, and reduced iron
    • Mühlenhoff, U., N. Richhardt, J. Gerber, and R. Lill. 2002. Characterization of iron-sulfur protein assembly in isolated mitochondria-a requirement for ATP, NADH, and reduced iron. J. Biol. Chem. 277:29810-29816.
    • (2002) J. Biol. Chem , vol.277 , pp. 29810-29816
    • Mühlenhoff, U.1    Richhardt, N.2    Gerber, J.3    Lill, R.4
  • 20
    • 37349036175 scopus 로고    scopus 로고
    • CGFS-type monothiol glutaredoxins from the cyanobacterium Synechocystis PCC6803 and other evolutionary distant model organisms possess a glutathione-ligated [2Fe-2S] cluster
    • Picciocchi, A., C. Saguez, A. Boussac, C. Cassier-Chauvat, and F. Chauvat. 2007. CGFS-type monothiol glutaredoxins from the cyanobacterium Synechocystis PCC6803 and other evolutionary distant model organisms possess a glutathione-ligated [2Fe-2S] cluster. Biochemistry 46:15018-15026.
    • (2007) Biochemistry , vol.46 , pp. 15018-15026
    • Picciocchi, A.1    Saguez, C.2    Boussac, A.3    Cassier-Chauvat, C.4    Chauvat, F.5
  • 21
    • 33745618402 scopus 로고    scopus 로고
    • Evolution of the Isd11-IscS complex reveals a single alpha- proteobacterial endosymbiosis for all eukaryotes
    • Richards, T. A., and M. van der Giezen. 2006. Evolution of the Isd11-IscS complex reveals a single alpha-proteobacterial endosymbiosis for all eukaryotes. Mol. Biol. Evol. 23:1341-1344.
    • (2006) Mol. Biol. Evol , vol.23 , pp. 1341-1344
    • Richards, T.A.1    Van Der Giezen, M.2
  • 22
    • 0036226063 scopus 로고    scopus 로고
    • Grx5 is a mitochondrial glutaredoxin required for the activity of iron/ sulfur enzymes
    • Rodriguez-Manzaneque, M. T., J. Tamarit, G. Belli, J. Ros, and E. Herrero. 2002. Grx5 is a mitochondrial glutaredoxin required for the activity of iron/ sulfur enzymes. Mol. Biol. Cell 13:1109-1121.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1109-1121
    • Rodriguez-Manzaneque, M.T.1    Tamarit, J.2    Belli, G.3    Ros, J.4    Herrero, E.5
  • 23
    • 0041386108 scopus 로고    scopus 로고
    • MrBayes 3: Bayesian phylogenetic inference under mixed models
    • Ronquist, F., and J. P. Huelsenbeck. 2003. MrBayes 3: Bayesian phylogenetic inference under mixed models. Bioinformatics 19:1572-1574.
    • (2003) Bioinformatics , vol.19 , pp. 1572-1574
    • Ronquist, F.1    Huelsenbeck, J.P.2
  • 25
    • 0032054894 scopus 로고    scopus 로고
    • Stable DNA transfection of the primitive protozoan pathogen Giardia lamblia
    • Sun, C. H., C. F. Chou, and J. H. Tai. 1998. Stable DNA transfection of the primitive protozoan pathogen Giardia lamblia. MoI. Biochem. Parasitol. 92:123-132.
    • (1998) MoI. Biochem. Parasitol , vol.92 , pp. 123-132
    • Sun, C.H.1    Chou, C.F.2    Tai, J.H.3
  • 26
    • 36549035976 scopus 로고    scopus 로고
    • Iron-sulfur proteins and iron-sulfur cluster assembly in organisms with hydrogenosomes and mitosomes
    • W. Martin and M. Müller (ed.), Springer-Verlag, Berlin, Germany
    • Tachezy, J., and P. Dolezal. 2007. Iron-sulfur proteins and iron-sulfur cluster assembly in organisms with hydrogenosomes and mitosomes, p. 105-133. In W. Martin and M. Müller (ed.), Origin of mitochondria and hydrogenosomes. Springer-Verlag, Berlin, Germany.
    • (2007) Origin of Mitochondria and Hydrogenosomes , pp. 105-133
    • Tachezy, J.1    Dolezal, P.2
  • 27
    • 77349127520 scopus 로고    scopus 로고
    • Mitosomes in parasitic protists
    • J. Tachezy (ed.), Springer-Verlag, Berlin, Germany
    • Tachezy, J., and O. Smid. 2008. Mitosomes in parasitic protists, p. 202-230. In J. Tachezy (ed.), Microbial monographs. Springer-Verlag, Berlin, Germany.
    • (2008) Microbial Monographs , pp. 202-230
    • Tachezy, J.1    Smid, O.2
  • 28
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL-X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson, J. D., T. J. Gibson, F. Plewniak, F. Jeanmougin, and D. G. Higgins. 1997. The CLUSTAL-X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25:4876-4882.
    • (1997) Nucleic Acids Res , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 30
    • 65849420352 scopus 로고    scopus 로고
    • Hydrogenosomes and mitosomes: Conservation and evolution of functions
    • van der Giezen, M. 2009. Hydrogenosomes and mitosomes: conservation and evolution of functions. J. Eukaryot. Microbiol. 56:221-231.
    • (2009) J. Eukaryot. Microbiol , vol.56 , pp. 221-231
    • Van Der Giezen, M.1
  • 31
    • 14744301484 scopus 로고    scopus 로고
    • Functional link between ribosome formation and biogenesis of iron-sulfur proteins
    • DOI 10.1038/sj.emboj.7600540
    • Yarunin, A., V. G. Panse, E. Petfalski, C. Dez, D. Tollervey, and E. C. Hurt. 2005. Functional link between ribosome formation and biogenesis of ironsulfur proteins. EMBO J. 24:580-588. (Pubitemid 40343259)
    • (2005) EMBO Journal , vol.24 , Issue.3 , pp. 580-588
    • Yarunin, A.1    Panse, V.G.2    Petfalski, E.3    Dez, C.4    Tollervey, D.5    Hurt, E.C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.