메뉴 건너뛰기




Volumn 41, Issue 13-14, 2011, Pages 1421-1434

The Trichomonas vaginalis hydrogenosome proteome is highly reduced relative to mitochondria, yet complex compared with mitosomes

Author keywords

Hydrogenosome; Mitochondria; Mitosome; Organelle evolution; Parasite; Trichomonas

Indexed keywords

ADENOSINE TRIPHOSPHATE; CELL PROTEIN; CHAPERONIN; GUANOSINE TRIPHOSPHATASE; HYDROGEN; HYDROGENOSOMAL PROTEIN; IRON SULFUR PROTEIN; OXYGEN; PROTEIN; PROTEOME; QUERCETIN; RIBOSOME PROTEIN; UNCLASSIFIED DRUG;

EID: 82355191521     PISSN: 00207519     EISSN: 18790135     Source Type: Journal    
DOI: 10.1016/j.ijpara.2011.10.001     Document Type: Article
Times cited : (89)

References (115)
  • 1
    • 57649136751 scopus 로고    scopus 로고
    • Cysteine synthase (CysM) of Mycobacterium tuberculosis is an O-phosphoserine sulfhydrylase: evidence for an alternative cysteine biosynthesis pathway in mycobacteria
    • Agren D., Schnell R., Oehlmann W., Singh M., Schneider G. Cysteine synthase (CysM) of Mycobacterium tuberculosis is an O-phosphoserine sulfhydrylase: evidence for an alternative cysteine biosynthesis pathway in mycobacteria. J Biol Chem 2008, 283:31567-31574.
    • (2008) J Biol Chem , vol.283 , pp. 31567-31574
    • Agren, D.1    Schnell, R.2    Oehlmann, W.3    Singh, M.4    Schneider, G.5
  • 2
    • 1942490139 scopus 로고    scopus 로고
    • An intestinal parasitic protist, Entamoeba histolytica, possesses a non-redundant nitrogen fixation-like system for iron-sulfur cluster assembly under anaerobic conditions
    • Ali V., Shigeta Y., Tokumoto U., Takahashi Y., Nozaki T. An intestinal parasitic protist, Entamoeba histolytica, possesses a non-redundant nitrogen fixation-like system for iron-sulfur cluster assembly under anaerobic conditions. J Biol Chem 2004, 279:16863-16874.
    • (2004) J Biol Chem , vol.279 , pp. 16863-16874
    • Ali, V.1    Shigeta, Y.2    Tokumoto, U.3    Takahashi, Y.4    Nozaki, T.5
  • 5
    • 33745618670 scopus 로고    scopus 로고
    • Evolution of four gene families with patchy phylogenetic distributions: influx of genes into protist genomes
    • Andersson J.O., Hirt R.P., Foster P.G., Roger A.J. Evolution of four gene families with patchy phylogenetic distributions: influx of genes into protist genomes. BMC Evol Biol 2006, 6:27.
    • (2006) BMC Evol Biol , vol.6 , pp. 27
    • Andersson, J.O.1    Hirt, R.P.2    Foster, P.G.3    Roger, A.J.4
  • 6
    • 33745601933 scopus 로고    scopus 로고
    • The relationship between mitochondrial shape and function and the cytoskeleton
    • Anesti V., Scorrano L. The relationship between mitochondrial shape and function and the cytoskeleton. Biochim Biophys Acta (BBA) - Bioenerg 2006, 1757:692-699.
    • (2006) Biochim Biophys Acta (BBA) - Bioenerg , vol.1757 , pp. 692-699
    • Anesti, V.1    Scorrano, L.2
  • 7
    • 67349094900 scopus 로고    scopus 로고
    • Hydrogenosomes under microscopy
    • Benchimol M. Hydrogenosomes under microscopy. Tissue Cell 2009, 41:151-168.
    • (2009) Tissue Cell , vol.41 , pp. 151-168
    • Benchimol, M.1
  • 11
    • 0031010331 scopus 로고    scopus 로고
    • Targeting and translocation of proteins into the hydrogenosome of the protist Trichomonas: similarities with mitochondrial protein import
    • Bradley P.J., Lahti C.J., Plumper E., Johnson P.J. Targeting and translocation of proteins into the hydrogenosome of the protist Trichomonas: similarities with mitochondrial protein import. EMBO J 1997, 16:3484-3493.
    • (1997) EMBO J , vol.16 , pp. 3484-3493
    • Bradley, P.J.1    Lahti, C.J.2    Plumper, E.3    Johnson, P.J.4
  • 14
    • 0029881944 scopus 로고    scopus 로고
    • Identification and characterization of [Fe]-hydrogenases in the hydrogenosome of Trichomonas vaginalis
    • Bui E.T., Johnson P.J. Identification and characterization of [Fe]-hydrogenases in the hydrogenosome of Trichomonas vaginalis. Mol Biochem Parasitol 1996, 76:305-310.
    • (1996) Mol Biochem Parasitol , vol.76 , pp. 305-310
    • Bui, E.T.1    Johnson, P.J.2
  • 15
    • 0029817685 scopus 로고    scopus 로고
    • A common evolutionary origin for mitochondria and hydrogenosomes
    • Bui E.T., Bradley P.J., Johnson P.J. A common evolutionary origin for mitochondria and hydrogenosomes. Proc Nat Acad Sci USA 1996, 93:9651-9656.
    • (1996) Proc Nat Acad Sci USA , vol.93 , pp. 9651-9656
    • Bui, E.T.1    Bradley, P.J.2    Johnson, P.J.3
  • 16
    • 33846840372 scopus 로고    scopus 로고
    • Protein targeting in parasites with cryptic mitochondria
    • Burri L., Keeling P.J. Protein targeting in parasites with cryptic mitochondria. Int J Parasitol 2007, 37:265-272.
    • (2007) Int J Parasitol , vol.37 , pp. 265-272
    • Burri, L.1    Keeling, P.J.2
  • 19
    • 0034088078 scopus 로고    scopus 로고
    • Failure to detect DNA in hydrogenosomes of Trichomonas vaginalis by nick translation and immunomicroscopy
    • Clemens D.L., Johnson P.J. Failure to detect DNA in hydrogenosomes of Trichomonas vaginalis by nick translation and immunomicroscopy. Mol Biochem Parasitol 2000, 106:307-313.
    • (2000) Mol Biochem Parasitol , vol.106 , pp. 307-313
    • Clemens, D.L.1    Johnson, P.J.2
  • 20
    • 1242272091 scopus 로고    scopus 로고
    • The amitochondriate eukaryote Trichomonas vaginalis contains a divergent thioredoxin-linked peroxiredoxin antioxidant system
    • Coombs G.H., Westrop G.D., Suchan P., Puzova G., Hirt R.P., Embley T.M., Mottram J.C., Muller S. The amitochondriate eukaryote Trichomonas vaginalis contains a divergent thioredoxin-linked peroxiredoxin antioxidant system. J Biol Chem 2004, 279:5249-5256.
    • (2004) J Biol Chem , vol.279 , pp. 5249-5256
    • Coombs, G.H.1    Westrop, G.D.2    Suchan, P.3    Puzova, G.4    Hirt, R.P.5    Embley, T.M.6    Mottram, J.C.7    Muller, S.8
  • 21
    • 0030895287 scopus 로고    scopus 로고
    • Transient and selectable transformation of the parasitic protist Trichomonas vaginalis
    • Delgadillo M.G., Liston D.R., Niazi K., Johnson P.J. Transient and selectable transformation of the parasitic protist Trichomonas vaginalis. Proc Natl Acad Sci USA 1997, 94:4716-4720.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 4716-4720
    • Delgadillo, M.G.1    Liston, D.R.2    Niazi, K.3    Johnson, P.J.4
  • 22
    • 0001419545 scopus 로고
    • The establishment of various trichomonads of animals and man in axenic cultures
    • Diamond L.S. The establishment of various trichomonads of animals and man in axenic cultures. J Parasitol 1957, 43:488-490.
    • (1957) J Parasitol , vol.43 , pp. 488-490
    • Diamond, L.S.1
  • 24
    • 33746575844 scopus 로고    scopus 로고
    • Evolution of the molecular machines for protein import into mitochondria
    • Dolezal P., Likic V., Tachezy J., Lithgow T. Evolution of the molecular machines for protein import into mitochondria. Science 2006, 313:314-318.
    • (2006) Science , vol.313 , pp. 314-318
    • Dolezal, P.1    Likic, V.2    Tachezy, J.3    Lithgow, T.4
  • 25
    • 34547919212 scopus 로고    scopus 로고
    • Frataxin, a conserved mitochondrial protein, in the hydrogenosome of Trichomonas vaginalis
    • Dolezal P., Dancis A., Lesuisse E., Sutak R., Hrdy I., Embley T.M., Tachezy J. Frataxin, a conserved mitochondrial protein, in the hydrogenosome of Trichomonas vaginalis. Eukaryot Cell 2007, 6:1431-1438.
    • (2007) Eukaryot Cell , vol.6 , pp. 1431-1438
    • Dolezal, P.1    Dancis, A.2    Lesuisse, E.3    Sutak, R.4    Hrdy, I.5    Embley, T.M.6    Tachezy, J.7
  • 27
    • 0033897694 scopus 로고    scopus 로고
    • Origins of hydrogenosomes and mitochondria: evolution and organelle biogenesis
    • Dyall S.D., Johnson P.J. Origins of hydrogenosomes and mitochondria: evolution and organelle biogenesis. Curr Opin Microbiol 2000, 3:404-411.
    • (2000) Curr Opin Microbiol , vol.3 , pp. 404-411
    • Dyall, S.D.1    Johnson, P.J.2
  • 28
    • 0034023895 scopus 로고    scopus 로고
    • Presence of a member of the mitochondrial carrier family in hydrogenosomes: conservation of membrane-targeting pathways between hydrogenosomes and mitochondria
    • Dyall S.D., Koehler C.M., Delgadillo-Correa M.G., Bradley P.J., Plumper E., Leuenberger D., Turck C.W., Johnson P.J. Presence of a member of the mitochondrial carrier family in hydrogenosomes: conservation of membrane-targeting pathways between hydrogenosomes and mitochondria. Mol Cell Biol 2000, 20:2488-2497.
    • (2000) Mol Cell Biol , vol.20 , pp. 2488-2497
    • Dyall, S.D.1    Koehler, C.M.2    Delgadillo-Correa, M.G.3    Bradley, P.J.4    Plumper, E.5    Leuenberger, D.6    Turck, C.W.7    Johnson, P.J.8
  • 30
    • 1842429937 scopus 로고    scopus 로고
    • Ancient invasions: from endosymbionts to organelles
    • Dyall S.D., Brown M.T., Johnson P.J. Ancient invasions: from endosymbionts to organelles. Science 2004, 304:253-257.
    • (2004) Science , vol.304 , pp. 253-257
    • Dyall, S.D.1    Brown, M.T.2    Johnson, P.J.3
  • 32
    • 33747810433 scopus 로고    scopus 로고
    • Multiple secondary origins of the anaerobic lifestyle in eukaryotes
    • Embley T.M. Multiple secondary origins of the anaerobic lifestyle in eukaryotes. Philos Trans R Soc B-Biol Sci 2006, 361:1055-1067.
    • (2006) Philos Trans R Soc B-Biol Sci , vol.361 , pp. 1055-1067
    • Embley, T.M.1
  • 39
    • 37849026162 scopus 로고    scopus 로고
    • Glycolytic enzymes associate dynamically with mitochondria in response to respiratory demand and support substrate channeling
    • Graham J.W.A., Williams T.C.R., Morgan M., Fernie A.R., Ratcliffe R.G., Sweetlove L.J. Glycolytic enzymes associate dynamically with mitochondria in response to respiratory demand and support substrate channeling. Plant Cell 2007, 19:3723-3738.
    • (2007) Plant Cell , vol.19 , pp. 3723-3738
    • Graham, J.W.A.1    Williams, T.C.R.2    Morgan, M.3    Fernie, A.R.4    Ratcliffe, R.G.5    Sweetlove, L.J.6
  • 40
    • 38949119434 scopus 로고    scopus 로고
    • Reconstruction of pathways associated with amino acid metabolism in human mitochondria
    • Guda P., Guda C., Subramaniam S. Reconstruction of pathways associated with amino acid metabolism in human mitochondria. Genomics Proteomics Bioinformatics 2007, 5:166-176.
    • (2007) Genomics Proteomics Bioinformatics , vol.5 , pp. 166-176
    • Guda, P.1    Guda, C.2    Subramaniam, S.3
  • 41
    • 0030612496 scopus 로고    scopus 로고
    • Conservation of mitochondrial targeting sequence function in mitochondrial and hydrogenosomal proteins from the early-branching eukaryotes Crithidia, Trypanosoma and Trichomonas
    • Hausler T., Stierhof Y.D., Blattner J., Clayton C. Conservation of mitochondrial targeting sequence function in mitochondrial and hydrogenosomal proteins from the early-branching eukaryotes Crithidia, Trypanosoma and Trichomonas. Eur J Cell Biol 1997, 73:240-251.
    • (1997) Eur J Cell Biol , vol.73 , pp. 240-251
    • Hausler, T.1    Stierhof, Y.D.2    Blattner, J.3    Clayton, C.4
  • 42
    • 0842270043 scopus 로고    scopus 로고
    • Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins
    • Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., Millar A.H. Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins. Plant Cell 2004, 16:241-256.
    • (2004) Plant Cell , vol.16 , pp. 241-256
    • Heazlewood, J.L.1    Tonti-Filippini, J.S.2    Gout, A.M.3    Day, D.A.4    Whelan, J.5    Millar, A.H.6
  • 43
    • 0032915394 scopus 로고    scopus 로고
    • Molecular cloning and expression analyses of mitochondrial and plastidic isoforms of cysteine synthase (O-acetylserine(thiol)lyase) from Arabidopsis thaliana
    • Hesse H., Lipke J., Altmann T., Hofgen R. Molecular cloning and expression analyses of mitochondrial and plastidic isoforms of cysteine synthase (O-acetylserine(thiol)lyase) from Arabidopsis thaliana. Amino Acids 1999, 16:113-131.
    • (1999) Amino Acids , vol.16 , pp. 113-131
    • Hesse, H.1    Lipke, J.2    Altmann, T.3    Hofgen, R.4
  • 44
    • 1842716892 scopus 로고    scopus 로고
    • Proteomic analysis on symbiotic differentiation of mitochondria in soybean nodules
    • Hoa le T.P., Nomura M., Kajiwara H., Day D.A., Tajima S. Proteomic analysis on symbiotic differentiation of mitochondria in soybean nodules. Plant Cell Physiol 2004, 45:300-308.
    • (2004) Plant Cell Physiol , vol.45 , pp. 300-308
    • Hoa le, T.P.1    Nomura, M.2    Kajiwara, H.3    Day, D.A.4    Tajima, S.5
  • 45
    • 0033736055 scopus 로고    scopus 로고
    • Iron hydrogenases and the evolution of anaerobic eukaryotes
    • Horner D.S., Foster P.G., Embley T.M. Iron hydrogenases and the evolution of anaerobic eukaryotes. Mol Biol Evol 2000, 17:1695-1709.
    • (2000) Mol Biol Evol , vol.17 , pp. 1695-1709
    • Horner, D.S.1    Foster, P.G.2    Embley, T.M.3
  • 46
    • 0028874227 scopus 로고
    • Primary structure and eubacterial relationships of the pyruvate:ferredoxin oxidoreductase of the amitochondriate eukaryote Trichomonas vaginalis
    • Hrdy I., Muller M. Primary structure and eubacterial relationships of the pyruvate:ferredoxin oxidoreductase of the amitochondriate eukaryote Trichomonas vaginalis. J Mol Evol 1995, 41:388-396.
    • (1995) J Mol Evol , vol.41 , pp. 388-396
    • Hrdy, I.1    Muller, M.2
  • 47
    • 0029372609 scopus 로고
    • Primary structure of the hydrogenosomal malic enzyme of Trichomonas vaginalis and its relationship to homologous enzymes
    • Hrdy I., Muller M. Primary structure of the hydrogenosomal malic enzyme of Trichomonas vaginalis and its relationship to homologous enzymes. J Eukaryot Microbiol 1995, 42:593-603.
    • (1995) J Eukaryot Microbiol , vol.42 , pp. 593-603
    • Hrdy, I.1    Muller, M.2
  • 48
    • 10344254308 scopus 로고    scopus 로고
    • Trichomonas hydrogenosomes contain the NADH dehydrogenase module of mitochondrial complex I
    • Hrdy I., Hirt R.P., Dolezal P., Bardonova L., Foster P.G., Tachezy J., Embley T.M. Trichomonas hydrogenosomes contain the NADH dehydrogenase module of mitochondrial complex I. Nature 2004, 432:618-622.
    • (2004) Nature , vol.432 , pp. 618-622
    • Hrdy, I.1    Hirt, R.P.2    Dolezal, P.3    Bardonova, L.4    Foster, P.G.5    Tachezy, J.6    Embley, T.M.7
  • 50
    • 0025180595 scopus 로고
    • Molecular analysis of the hydrogenosomal ferredoxin of the anaerobic protist Trichomonas vaginalis
    • Johnson P.J., d'Oliveira C.E., Gorrell T.E., Muller M. Molecular analysis of the hydrogenosomal ferredoxin of the anaerobic protist Trichomonas vaginalis. Proc Nat Acad Sci USA 1990, 87:6097-6101.
    • (1990) Proc Nat Acad Sci USA , vol.87 , pp. 6097-6101
    • Johnson, P.J.1    d'Oliveira, C.E.2    Gorrell, T.E.3    Muller, M.4
  • 51
    • 0027365367 scopus 로고
    • Biogenesis of the hydrogenosome in the anaerobic protist Trichomonas vaginalis
    • Johnson P.J., Lahti C.J., Bradley P.J. Biogenesis of the hydrogenosome in the anaerobic protist Trichomonas vaginalis. J Parasitol 1993, 79:664-670.
    • (1993) J Parasitol , vol.79 , pp. 664-670
    • Johnson, P.J.1    Lahti, C.J.2    Bradley, P.J.3
  • 52
    • 38149005635 scopus 로고    scopus 로고
    • Global epidemiology and control of Trichomonas vaginalis
    • Johnston V.J., Mabey D.C. Global epidemiology and control of Trichomonas vaginalis. Curr Opin Infect Dis 2008, 21:56-64.
    • (2008) Curr Opin Infect Dis , vol.21 , pp. 56-64
    • Johnston, V.J.1    Mabey, D.C.2
  • 54
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes
    • Krogh A., Larsson B., von Heijne G., Sonnhammer E.L. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J Mol Biol 2001, 305:567-580.
    • (2001) J Mol Biol , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    von Heijne, G.3    Sonnhammer, E.L.4
  • 55
    • 1942468196 scopus 로고    scopus 로고
    • The role and structure of mitochondrial carriers
    • Kunji E.R. The role and structure of mitochondrial carriers. FEBS Lett 2004, 564:239-244.
    • (2004) FEBS Lett , vol.564 , pp. 239-244
    • Kunji, E.R.1
  • 56
    • 0026641622 scopus 로고
    • Beta-succinyl-coenzyme A synthetase from Trichomonas vaginalis is a soluble hydrogenosomal protein with an amino-terminal sequence that resembles mitochondrial presequences
    • Lahti C.J., d'Oliveira C.E., Johnson P.J. Beta-succinyl-coenzyme A synthetase from Trichomonas vaginalis is a soluble hydrogenosomal protein with an amino-terminal sequence that resembles mitochondrial presequences. J Bacteriol 1992, 174:6822-6830.
    • (1992) J Bacteriol , vol.174 , pp. 6822-6830
    • Lahti, C.J.1    d'Oliveira, C.E.2    Johnson, P.J.3
  • 57
    • 0028168012 scopus 로고
    • Molecular characterization of the alpha-subunit of Trichomonas vaginalis hydrogenosomal succinyl CoA synthetase
    • Lahti C.J., Bradley P.J., Johnson P.J. Molecular characterization of the alpha-subunit of Trichomonas vaginalis hydrogenosomal succinyl CoA synthetase. Mol Biochem Parasitol 1994, 66:309-318.
    • (1994) Mol Biochem Parasitol , vol.66 , pp. 309-318
    • Lahti, C.J.1    Bradley, P.J.2    Johnson, P.J.3
  • 58
    • 24044440794 scopus 로고    scopus 로고
    • Identification of a very large Rab GTPase family in the parasitic protozoan Trichomonas vaginalis
    • Lal K., Field M.C., Carlton J.M., Warwicker J., Hirt R.P. Identification of a very large Rab GTPase family in the parasitic protozoan Trichomonas vaginalis. Mol Biochem Parasitol 2005, 143:226-235.
    • (2005) Mol Biochem Parasitol , vol.143 , pp. 226-235
    • Lal, K.1    Field, M.C.2    Carlton, J.M.3    Warwicker, J.4    Hirt, R.P.5
  • 60
    • 0028132843 scopus 로고
    • Primary structure of the hydrogenosomal adenylate kinase of Trichomonas vaginalis and its phylogenetic relationships
    • Lange S., Rozario C., Muller M. Primary structure of the hydrogenosomal adenylate kinase of Trichomonas vaginalis and its phylogenetic relationships. Mol Biochem Parasitol 1994, 66:297-308.
    • (1994) Mol Biochem Parasitol , vol.66 , pp. 297-308
    • Lange, S.1    Rozario, C.2    Muller, M.3
  • 61
    • 68949128587 scopus 로고    scopus 로고
    • Function and biogenesis of iron-sulphur proteins
    • Lill R. Function and biogenesis of iron-sulphur proteins. Nature 2009, 460:831-838.
    • (2009) Nature , vol.460 , pp. 831-838
    • Lill, R.1
  • 62
    • 0034255836 scopus 로고    scopus 로고
    • Maturation of cellular Fe-S proteins: an essential function of mitochondria
    • Lill R., Kispal G. Maturation of cellular Fe-S proteins: an essential function of mitochondria. Trends Biochem Sci 2000, 25:352-356.
    • (2000) Trends Biochem Sci , vol.25 , pp. 352-356
    • Lill, R.1    Kispal, G.2
  • 63
    • 47249094614 scopus 로고    scopus 로고
    • Maturation of iron-sulfur proteins in eukaryotes: mechanisms, connected processes, and diseases
    • Lill R., Muhlenhoff U. Maturation of iron-sulfur proteins in eukaryotes: mechanisms, connected processes, and diseases. Annu Rev Biochem 2008, 77:669-700.
    • (2008) Annu Rev Biochem , vol.77 , pp. 669-700
    • Lill, R.1    Muhlenhoff, U.2
  • 64
    • 0016207444 scopus 로고
    • Superoxide dismutase in the anaerobic flagellates, Tritrichomonas foetus and Monocercomonas sp
    • Lindmark D.G., Muller M. Superoxide dismutase in the anaerobic flagellates, Tritrichomonas foetus and Monocercomonas sp. J Biol Chem 1974, 249:4634-4637.
    • (1974) J Biol Chem , vol.249 , pp. 4634-4637
    • Lindmark, D.G.1    Muller, M.2
  • 65
    • 0016734805 scopus 로고
    • Hydrogenosomes in Trichomonas vaginalis
    • Lindmark D.G., Muller M., Shio H. Hydrogenosomes in Trichomonas vaginalis. J. Parasitol. 1975, 61:552-554.
    • (1975) J. Parasitol. , vol.61 , pp. 552-554
    • Lindmark, D.G.1    Muller, M.2    Shio, H.3
  • 66
    • 77349095480 scopus 로고    scopus 로고
    • Evolution of macromolecular import pathways in mitochondria, hydrogenosomes and mitosomes
    • Lithgow T., Schneider A. Evolution of macromolecular import pathways in mitochondria, hydrogenosomes and mitosomes. Philos Trans R Soc Lond B Biol Sci 2010, 365:799-817.
    • (2010) Philos Trans R Soc Lond B Biol Sci , vol.365 , pp. 799-817
    • Lithgow, T.1    Schneider, A.2
  • 68
    • 1642311878 scopus 로고    scopus 로고
    • Ribosomes specifically bind to mammalian mitochondria via protease-sensitive proteins on the outer membrane
    • MacKenzie J.A., Payne R.M. Ribosomes specifically bind to mammalian mitochondria via protease-sensitive proteins on the outer membrane. J Biol Chem 2004, 279:9803-9810.
    • (2004) J Biol Chem , vol.279 , pp. 9803-9810
    • MacKenzie, J.A.1    Payne, R.M.2
  • 69
    • 0033020661 scopus 로고    scopus 로고
    • Hsp60 is targeted to a cryptic mitochondrion-derived organelle (" crypton" ) in the microaerophilic protozoan parasite Entamoeba histolytica
    • Mai Z., Ghosh S., Frisardi M., Rosenthal B., Rogers R., Samuelson J. Hsp60 is targeted to a cryptic mitochondrion-derived organelle (" crypton" ) in the microaerophilic protozoan parasite Entamoeba histolytica. Mol Cell Biol 1999, 19:2198-2205.
    • (1999) Mol Cell Biol , vol.19 , pp. 2198-2205
    • Mai, Z.1    Ghosh, S.2    Frisardi, M.3    Rosenthal, B.4    Rogers, R.5    Samuelson, J.6
  • 70
    • 27544472676 scopus 로고    scopus 로고
    • Automated genome annotation and pathway identification using the KEGG Orthology (KO) as a controlled vocabulary
    • Mao X., Cai T., Olyarchuk J.G., Wei L. Automated genome annotation and pathway identification using the KEGG Orthology (KO) as a controlled vocabulary. Bioinformatics 2005, 21:3787-3793.
    • (2005) Bioinformatics , vol.21 , pp. 3787-3793
    • Mao, X.1    Cai, T.2    Olyarchuk, J.G.3    Wei, L.4
  • 72
    • 0035197418 scopus 로고    scopus 로고
    • An overview of endosymbiotic models for the origins of eukaryotes, their ATP-producing organelles (mitochondria and hydrogenosomes), and their heterotrophic lifestyle
    • Martin W., Hoffmeister M., Rotte C., Henze K. An overview of endosymbiotic models for the origins of eukaryotes, their ATP-producing organelles (mitochondria and hydrogenosomes), and their heterotrophic lifestyle. Biol Chem 2001, 382:1521-1539.
    • (2001) Biol Chem , vol.382 , pp. 1521-1539
    • Martin, W.1    Hoffmeister, M.2    Rotte, C.3    Henze, K.4
  • 73
    • 33746016268 scopus 로고    scopus 로고
    • Mitochondria: more than just a powerhouse
    • McBride H.M., Neuspiel M., Wasiak S. Mitochondria: more than just a powerhouse. Curr Biol 2006, 16:R551-R560.
    • (2006) Curr Biol , vol.16
    • McBride, H.M.1    Neuspiel, M.2    Wasiak, S.3
  • 74
    • 54249088577 scopus 로고    scopus 로고
    • Protein import into hydrogenosomes of Trichomonas vaginalis involves both N-terminal and internal targeting signals: a case study of thioredoxin reductases
    • Mentel M., Zimorski V., Haferkamp P., Martin W., Henze K. Protein import into hydrogenosomes of Trichomonas vaginalis involves both N-terminal and internal targeting signals: a case study of thioredoxin reductases. Eukaryot Cell 2008, 7:1750-1757.
    • (2008) Eukaryot Cell , vol.7 , pp. 1750-1757
    • Mentel, M.1    Zimorski, V.2    Haferkamp, P.3    Martin, W.4    Henze, K.5
  • 75
    • 76049108776 scopus 로고    scopus 로고
    • Mitosomes in Entamoeba histolytica contain a sulfate activation pathway
    • Mi-Ichi F., Yousuf M.A., Nakada-Tsukui K., Nozaki T. Mitosomes in Entamoeba histolytica contain a sulfate activation pathway. Proc Natl Acad Sci USA 2009, 106:21731-21736.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 21731-21736
    • Mi-Ichi, F.1    Yousuf, M.A.2    Nakada-Tsukui, K.3    Nozaki, T.4
  • 76
    • 33845677739 scopus 로고    scopus 로고
    • Proteins of the glycine decarboxylase complex in the hydrogenosome of Trichomonas vaginalis
    • Mukherjee M., Brown M.T., McArthur A.G., Johnson P.J. Proteins of the glycine decarboxylase complex in the hydrogenosome of Trichomonas vaginalis. Eukaryot Cell 2006, 5:2062-2071.
    • (2006) Eukaryot Cell , vol.5 , pp. 2062-2071
    • Mukherjee, M.1    Brown, M.T.2    McArthur, A.G.3    Johnson, P.J.4
  • 77
    • 33845650719 scopus 로고    scopus 로고
    • Identification and biochemical characterization of serine hydroxymethyl transferase in the hydrogenosome of Trichomonas vaginalis
    • Mukherjee M., Sievers S.A., Brown M.T., Johnson P.J. Identification and biochemical characterization of serine hydroxymethyl transferase in the hydrogenosome of Trichomonas vaginalis. Eukaryot Cell 2006, 5:2072-2078.
    • (2006) Eukaryot Cell , vol.5 , pp. 2072-2078
    • Mukherjee, M.1    Sievers, S.A.2    Brown, M.T.3    Johnson, P.J.4
  • 78
    • 0027787578 scopus 로고
    • The hydrogenosome
    • Muller M. The hydrogenosome. J Gen Microbiol 1993, 139:2879-2889.
    • (1993) J Gen Microbiol , vol.139 , pp. 2879-2889
    • Muller, M.1
  • 79
    • 0029880026 scopus 로고    scopus 로고
    • In vitro effect of tinidazole and furazolidone on metronidazole-resistant Trichomonas vaginalis
    • Narcisi E.M., Secor W.E. In vitro effect of tinidazole and furazolidone on metronidazole-resistant Trichomonas vaginalis. Antimicrob Agents Chemother 1996, 40:1121-1125.
    • (1996) Antimicrob Agents Chemother , vol.40 , pp. 1121-1125
    • Narcisi, E.M.1    Secor, W.E.2
  • 80
    • 34249873947 scopus 로고    scopus 로고
    • Translocation of proteins into mitochondria
    • Neupert W., Herrmann J.M. Translocation of proteins into mitochondria. Annu Rev Biochem 2007, 76:723-749.
    • (2007) Annu Rev Biochem , vol.76 , pp. 723-749
    • Neupert, W.1    Herrmann, J.M.2
  • 81
    • 1042266670 scopus 로고    scopus 로고
    • The yeast mitochondrial proteome, a study of fermentative and respiratory growth
    • Ohlmeier S., Kastaniotis A.J., Hiltunen J.K., Bergmann U. The yeast mitochondrial proteome, a study of fermentative and respiratory growth. J. Biol. Chem. 2004, 279:3956-3979.
    • (2004) J. Biol. Chem. , vol.279 , pp. 3956-3979
    • Ohlmeier, S.1    Kastaniotis, A.J.2    Hiltunen, J.K.3    Bergmann, U.4
  • 82
    • 0030053375 scopus 로고    scopus 로고
    • Tritrichomonas foetus and Trichomonas vaginalis: the pattern of inactivation of hydrogenase activity by oxygen and activities of catalase and ascorbate peroxidase
    • Page-Sharp M., Behm C.A., Smith G.D. Tritrichomonas foetus and Trichomonas vaginalis: the pattern of inactivation of hydrogenase activity by oxygen and activities of catalase and ascorbate peroxidase. Microbiology 1996, 142:207-211.
    • (1996) Microbiology , vol.142 , pp. 207-211
    • Page-Sharp, M.1    Behm, C.A.2    Smith, G.D.3
  • 84
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins D.N., Pappin D.J., Creasy D.M., Cottrell J.S. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 1999, 20:3551-3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 85
    • 60149110944 scopus 로고    scopus 로고
    • The single mitochondrial porin of Trypanosoma brucei is the main metabolite transporter in the outer mitochondrial membrane
    • Pusnik M., Charriere F., Maser P., Waller R.F., Dagley M.J., Lithgow T., Schneider A. The single mitochondrial porin of Trypanosoma brucei is the main metabolite transporter in the outer mitochondrial membrane. Mol Biol Evol 2009, 26:671-680.
    • (2009) Mol Biol Evol , vol.26 , pp. 671-680
    • Pusnik, M.1    Charriere, F.2    Maser, P.3    Waller, R.F.4    Dagley, M.J.5    Lithgow, T.6    Schneider, A.7
  • 87
    • 20644461004 scopus 로고    scopus 로고
    • Rubrerythrin and peroxiredoxin: two novel putative peroxidases in the hydrogenosomes of the microaerophilic protozoon Trichomonas vaginalis
    • Putz S., Gelius-Dietrich G., Piotrowski M., Henze K. Rubrerythrin and peroxiredoxin: two novel putative peroxidases in the hydrogenosomes of the microaerophilic protozoon Trichomonas vaginalis. Mol Biochem Parasitol 2005, 142:212-223.
    • (2005) Mol Biochem Parasitol , vol.142 , pp. 212-223
    • Putz, S.1    Gelius-Dietrich, G.2    Piotrowski, M.3    Henze, K.4
  • 90
    • 2142652096 scopus 로고    scopus 로고
    • Crystallographic structure and biochemical analysis of the Thermus thermophilus osmotically inducible protein C
    • Rehse P.H., Ohshima N., Nodake Y., Tahirov T.H. Crystallographic structure and biochemical analysis of the Thermus thermophilus osmotically inducible protein C. J Mol Biol 2004, 338:959-968.
    • (2004) J Mol Biol , vol.338 , pp. 959-968
    • Rehse, P.H.1    Ohshima, N.2    Nodake, Y.3    Tahirov, T.H.4
  • 91
    • 33745851905 scopus 로고    scopus 로고
    • Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics
    • Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A. Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics. J Proteome Res 2006, 5:1543-1554.
    • (2006) J Proteome Res , vol.5 , pp. 1543-1554
    • Reinders, J.1    Zahedi, R.P.2    Pfanner, N.3    Meisinger, C.4    Sickmann, A.5
  • 92
    • 33745618402 scopus 로고    scopus 로고
    • Evolution of the Isd11-IscS complex reveals a single alpha-proteobacterial endosymbiosis for all eukaryotes
    • Richards T.A., van der Giezen M. Evolution of the Isd11-IscS complex reveals a single alpha-proteobacterial endosymbiosis for all eukaryotes. Mol Biol Evol 2006, 23:1341-1344.
    • (2006) Mol Biol Evol , vol.23 , pp. 1341-1344
    • Richards, T.A.1    van der Giezen, M.2
  • 93
    • 0842302344 scopus 로고    scopus 로고
    • Mitochondrial morphology is dynamic and varied
    • Rube D.A., van der Bliek A.M. Mitochondrial morphology is dynamic and varied. Mol Cell Biochem 2004, 256-257:331-339.
    • (2004) Mol Cell Biochem , pp. 331-339
    • Rube, D.A.1    van der Bliek, A.M.2
  • 94
    • 0034066471 scopus 로고    scopus 로고
    • Membrane proteins and proteomics: un amour impossible?
    • Santoni V., Molloy M., Rabilloud T. Membrane proteins and proteomics: un amour impossible?. Electrophoresis 2000, 21:1054-1070.
    • (2000) Electrophoresis , vol.21 , pp. 1054-1070
    • Santoni, V.1    Molloy, M.2    Rabilloud, T.3
  • 95
    • 77957955710 scopus 로고    scopus 로고
    • Mitochondrion-related organelles in eukaryotic protists
    • Shiflett A.M., Johnson P.J. Mitochondrion-related organelles in eukaryotic protists. Annu Rev Microbiol 2010, 64:409-429.
    • (2010) Annu Rev Microbiol , vol.64 , pp. 409-429
    • Shiflett, A.M.1    Johnson, P.J.2
  • 97
    • 30944435242 scopus 로고    scopus 로고
    • Pyruvate-phosphate dikinase of oxymonads and parabasalia and the evolution of pyrophosphate-dependent glycolysis in anaerobic eukaryotes
    • Slamovits C.H., Keeling P.J. Pyruvate-phosphate dikinase of oxymonads and parabasalia and the evolution of pyrophosphate-dependent glycolysis in anaerobic eukaryotes. Eukaryot Cell 2006, 5:148-154.
    • (2006) Eukaryot Cell , vol.5 , pp. 148-154
    • Slamovits, C.H.1    Keeling, P.J.2
  • 99
    • 67650553054 scopus 로고    scopus 로고
    • MitoMiner, an integrated database for the storage and analysis of mitochondrial proteomics data
    • Smith A.C., Robinson A.J. MitoMiner, an integrated database for the storage and analysis of mitochondrial proteomics data. Mol Cell Proteomics 2009, 8:1324-1337.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 1324-1337
    • Smith, A.C.1    Robinson, A.J.2
  • 100
    • 35549005324 scopus 로고    scopus 로고
    • Exploring the mitochondrial proteome of the ciliate protozoon Tetrahymena thermophila: direct analysis by tandem mass spectrometry
    • Smith D.G., Gawryluk R.M., Spencer D.F., Pearlman R.E., Siu K.W., Gray M.W. Exploring the mitochondrial proteome of the ciliate protozoon Tetrahymena thermophila: direct analysis by tandem mass spectrometry. J Mol Biol 2007, 374:837-863.
    • (2007) J Mol Biol , vol.374 , pp. 837-863
    • Smith, D.G.1    Gawryluk, R.M.2    Spencer, D.F.3    Pearlman, R.E.4    Siu, K.W.5    Gray, M.W.6
  • 101
    • 58149350000 scopus 로고    scopus 로고
    • Flavodiiron protein from Trichomonas vaginalis hydrogenosomes: the terminal oxygen reductase
    • Smutna T., Goncalves V.L., Saraiva L.M., Tachezy J., Teixeira M., Hrdy I. Flavodiiron protein from Trichomonas vaginalis hydrogenosomes: the terminal oxygen reductase. Eukaryot Cell 2009, 8:47-55.
    • (2009) Eukaryot Cell , vol.8 , pp. 47-55
    • Smutna, T.1    Goncalves, V.L.2    Saraiva, L.M.3    Tachezy, J.4    Teixeira, M.5    Hrdy, I.6
  • 103
    • 0034804608 scopus 로고    scopus 로고
    • Mitochondrial type iron-sulfur cluster assembly in the amitochondriate eukaryotes Trichomonas vaginalis and Giardia intestinalis, as indicated by the phylogeny of IscS
    • Tachezy J., Sanchez L.B., Muller M. Mitochondrial type iron-sulfur cluster assembly in the amitochondriate eukaryotes Trichomonas vaginalis and Giardia intestinalis, as indicated by the phylogeny of IscS. Mol Biol Evol 2001, 18:1919-1928.
    • (2001) Mol Biol Evol , vol.18 , pp. 1919-1928
    • Tachezy, J.1    Sanchez, L.B.2    Muller, M.3
  • 105
    • 0032988857 scopus 로고    scopus 로고
    • The mitosome, a novel organelle related to mitochondria in the amitochondrial parasite Entamoeba histolytica
    • Tovar J., Fischer A., Clark C.G. The mitosome, a novel organelle related to mitochondria in the amitochondrial parasite Entamoeba histolytica. Mol Microbiol 1999, 32:1013-1021.
    • (1999) Mol Microbiol , vol.32 , pp. 1013-1021
    • Tovar, J.1    Fischer, A.2    Clark, C.G.3
  • 107
    • 0034786532 scopus 로고    scopus 로고
    • The HMMTOP transmembrane topology prediction server
    • Tusnady G.E., Simon I. The HMMTOP transmembrane topology prediction server. Bioinformatics 2001, 17:849-850.
    • (2001) Bioinformatics , vol.17 , pp. 849-850
    • Tusnady, G.E.1    Simon, I.2
  • 108
    • 2942536494 scopus 로고    scopus 로고
    • The iron-sulfur cluster assembly genes iscS and iscU of Entamoeba histolytica were acquired by horizontal gene transfer
    • van der Giezen M., Cox S., Tovar J. The iron-sulfur cluster assembly genes iscS and iscU of Entamoeba histolytica were acquired by horizontal gene transfer. BMC Evol Biol 2004, 4:7.
    • (2004) BMC Evol Biol , vol.4 , pp. 7
    • van der Giezen, M.1    Cox, S.2    Tovar, J.3
  • 110
    • 57249083976 scopus 로고    scopus 로고
    • SPOCTOPUS: a combined predictor of signal peptides and membrane protein topology
    • Viklund H., Bernsel A., Skwark M., Elofsson A. SPOCTOPUS: a combined predictor of signal peptides and membrane protein topology. Bioinformatics 2008, 24:2928-2929.
    • (2008) Bioinformatics , vol.24 , pp. 2928-2929
    • Viklund, H.1    Bernsel, A.2    Skwark, M.3    Elofsson, A.4
  • 112
    • 33748755115 scopus 로고    scopus 로고
    • Cysteine biosynthesis in Trichomonas vaginalis involves cysteine synthase utilizing O-phosphoserine
    • Westrop G.D., Goodall G., Mottram J.C., Coombs G.H. Cysteine biosynthesis in Trichomonas vaginalis involves cysteine synthase utilizing O-phosphoserine. J Biol Chem 2006, 281:25062-25075.
    • (2006) J Biol Chem , vol.281 , pp. 25062-25075
    • Westrop, G.D.1    Goodall, G.2    Mottram, J.C.3    Coombs, G.H.4
  • 113
    • 84859217336 scopus 로고    scopus 로고
    • WHO, World Health Organization, Global Prevalence and Incidence of Selected Curable Sexually Transmitted Infections.
    • WHO, 2001. World Health Organization, Global Prevalence and Incidence of Selected Curable Sexually Transmitted Infections. http://www.who.int/docstore/hiv/GRSTI/006.htm.
    • (2001)
  • 114
    • 0037158721 scopus 로고    scopus 로고
    • A mitochondrial remnant in the microsporidian Trachipleistophora hominis
    • Williams B.A., Hirt R.P., Lucocq J.M., Embley T.M. A mitochondrial remnant in the microsporidian Trachipleistophora hominis. Nature 2002, 418:865-869.
    • (2002) Nature , vol.418 , pp. 865-869
    • Williams, B.A.1    Hirt, R.P.2    Lucocq, J.M.3    Embley, T.M.4
  • 115
    • 33747868144 scopus 로고    scopus 로고
    • KOBAS server: a web-based platform for automated annotation and pathway identification
    • Wu J., Mao X., Cai T., Luo J., Wei L. KOBAS server: a web-based platform for automated annotation and pathway identification. Nucleic Acids Res 2006, 34:W720-W724.
    • (2006) Nucleic Acids Res , vol.34
    • Wu, J.1    Mao, X.2    Cai, T.3    Luo, J.4    Wei, L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.