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Volumn 65, Issue 5, 2007, Pages 1218-1228

Type 3 peptide deformylases are required for oxidative phosphorylation in Trypanosoma brucei

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; BACTERIAL ENZYME; PEPTIDE DEFORMYLASE; TYPE 3 PEPTIDE DEFORMYLASE; UNCLASSIFIED DRUG;

EID: 34547866086     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2007.05867.x     Document Type: Article
Times cited : (12)

References (48)
  • 1
    • 0029894292 scopus 로고    scopus 로고
    • A novel epitope tag system to study protein targeting and organelle biogenesis in Trypanosoma brucei
    • Bastin, P., Bagherzadeh, A., Matthews, K.R. Gull, K. (1996) A novel epitope tag system to study protein targeting and organelle biogenesis in Trypanosoma brucei. Mol Biochem Parasitol 77 : 235 239.
    • (1996) Mol Biochem Parasitol , vol.77 , pp. 235-239
    • Bastin, P.1    Bagherzadeh, A.2    Matthews, K.R.3    Gull, K.4
  • 2
    • 15044362303 scopus 로고    scopus 로고
    • Energy generation in insect stages of Trypanosoma brucei: Metabolism in flux
    • Besteiro, S., Barrett, M.P., Riviere, L. Bringaud, F. (2005) Energy generation in insect stages of Trypanosoma brucei: metabolism in flux. Trends Parasitol 21 : 185 191.
    • (2005) Trends Parasitol , vol.21 , pp. 185-191
    • Besteiro, S.1    Barrett, M.P.2    Riviere, L.3    Bringaud, F.4
  • 3
    • 33744795591 scopus 로고    scopus 로고
    • The complexity of mitochondrial tRNA import
    • Bhattacharyya, S.N. Adhya, S. (2004) The complexity of mitochondrial tRNA import. RNA Biology 1 : 84 88.
    • (2004) RNA Biology , vol.1 , pp. 84-88
    • Bhattacharyya, S.N.1    Adhya, S.2
  • 4
    • 0037031944 scopus 로고    scopus 로고
    • Mitochondrial substrate level phosphorylation is essential for growth of procyclic Trypanosoma brucei
    • Bochud-Allemann, N. Schneider, A. (2002) Mitochondrial substrate level phosphorylation is essential for growth of procyclic Trypanosoma brucei. J Biol Chem 277 : 32849 32854.
    • (2002) J Biol Chem , vol.277 , pp. 32849-32854
    • Bochud-Allemann, N.1    Schneider, A.2
  • 5
    • 14744301187 scopus 로고    scopus 로고
    • Structure-activity relationship analysis and therapeutic potential of peptide deformylase inhibitors
    • Boularot, A., Giglione, C., Artaud, I. Meinnel, T. (2004) Structure-activity relationship analysis and therapeutic potential of peptide deformylase inhibitors. Curr Opin Investig Drugs 5 : 809 822.
    • (2004) Curr Opin Investig Drugs , vol.5 , pp. 809-822
    • Boularot, A.1    Giglione, C.2    Artaud, I.3    Meinnel, T.4
  • 7
    • 0018601361 scopus 로고
    • Cultivation an in vitro cloning of procyclic culture forms of Trypansoma brucei in a semi-defined medium
    • Brun, R. Schönenberger, M. (1979) Cultivation an in vitro cloning of procyclic culture forms of Trypansoma brucei in a semi-defined medium. Acta Tropica 36 : 289 292.
    • (1979) Acta Tropica , vol.36 , pp. 289-292
    • Brun, R.1    Schönenberger, M.2
  • 8
    • 18144381509 scopus 로고    scopus 로고
    • Mitochondrial initiation factor 2 of Trypanosoma brucei binds imported formylated elongator-type methionyl-tRNA
    • Charrière, F., Tan, T.H.P. Schneider, A. (2005) Mitochondrial initiation factor 2 of Trypanosoma brucei binds imported formylated elongator-type methionyl-tRNA. J Biol Chem 280 : 15659 15665.
    • (2005) J Biol Chem , vol.280 , pp. 15659-15665
    • Charrière, F.1    Tan, T.H.P.2    Schneider, A.3
  • 9
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczyinski, P. Sacchi, N. (1987) Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem 162 : 156 159.
    • (1987) Anal Biochem , vol.162 , pp. 156-159
    • Chomczyinski, P.1    Sacchi, N.2
  • 10
    • 0026074688 scopus 로고
    • Alterations in Krebs cycle enzyme activities and carbohydrate catabolism in two strains of Trypanosoma brucei during in vitro differentiation of their bloodstream to procyclic stages
    • Durieux, P.O., Schutz, P., Brun, R. Kohler, P. (1991) Alterations in Krebs cycle enzyme activities and carbohydrate catabolism in two strains of Trypanosoma brucei during in vitro differentiation of their bloodstream to procyclic stages. Mol Biochem Parasitol 45 : 19 27.
    • (1991) Mol Biochem Parasitol , vol.45 , pp. 19-27
    • Durieux, P.O.1    Schutz, P.2    Brun, R.3    Kohler, P.4
  • 11
    • 0034071121 scopus 로고    scopus 로고
    • Mitochondrial genome diversity in parasites
    • Feagin, J.E. (2000) Mitochondrial genome diversity in parasites. Int J Parasitol 30 : 371 390.
    • (2000) Int J Parasitol , vol.30 , pp. 371-390
    • Feagin, J.E.1
  • 12
    • 0035543404 scopus 로고    scopus 로고
    • Organellar peptide deformylases: Universality of the N-terminal methionine cleavage mechanism
    • Giglione, C. Meinnel, T. (2001a) Organellar peptide deformylases: universality of the N-terminal methionine cleavage mechanism. Trends Plant Sci 6 : 566 572.
    • (2001) Trends Plant Sci , vol.6 , pp. 566-572
    • Giglione, C.1    Meinnel, T.2
  • 13
    • 0002002492 scopus 로고    scopus 로고
    • Peptide deformylase as an emerging target for antiparasitic agents
    • Giglione, C. Meinnel, T. (2001b) Peptide deformylase as an emerging target for antiparasitic agents. Emerging Therapeutic Targets 5 : 41 57.
    • (2001) Emerging Therapeutic Targets , vol.5 , pp. 41-57
    • Giglione, C.1    Meinnel, T.2
  • 14
    • 0034329475 scopus 로고    scopus 로고
    • Identification of eukaryotic peptide deformylases reveals universality of N-terminal protein processing mechanisms
    • Giglione, C., Serero, A., Pierre, M., Boisson, B. Meinnel, T. (2000) Identification of eukaryotic peptide deformylases reveals universality of N-terminal protein processing mechanisms. EMBO J 19 : 5916 5929.
    • (2000) EMBO J , vol.19 , pp. 5916-5929
    • Giglione, C.1    Serero, A.2    Pierre, M.3    Boisson, B.4    Meinnel, T.5
  • 15
    • 0037413729 scopus 로고    scopus 로고
    • Control of protein life-span by N-terminal methionine excision
    • Giglione, C., Vallon, O. Meinnel, T. (2003) Control of protein life-span by N-terminal methionine excision. EMBO J 22 : 13 23.
    • (2003) EMBO J , vol.22 , pp. 13-23
    • Giglione, C.1    Vallon, O.2    Meinnel, T.3
  • 18
    • 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
    • Häusler, T., Stierhof, Y.-D., Blattner, J. Clayton, C. (1997) Conservation of mitochondrial targeting sequence function in mitochondrial and hydrogenosomal proteins from the early-branching eukaryotes Crithidia, Trypanosoma and Trichomonas. Eur J Cell Biol 73 : 240 251.
    • (1997) Eur J Cell Biol , vol.73 , pp. 240-251
    • Häusler, T.1    Stierhof, Y.-D.2    Blattner, J.3    Clayton, C.4
  • 19
    • 0030975596 scopus 로고    scopus 로고
    • Inhibition of the respiratory chain results on a reversible metabolic arrest in Leishmania promastigotes
    • van Hellemond, J.J. Tielens, A.G.M. (1997) Inhibition of the respiratory chain results on a reversible metabolic arrest in Leishmania promastigotes. Mol Biochem Parasitol 85 : 135 138.
    • (1997) Mol Biochem Parasitol , vol.85 , pp. 135-138
    • Van Hellemond, J.J.1    Tielens, A.G.M.2
  • 20
    • 0032539820 scopus 로고    scopus 로고
    • Trypanosomatides produce acetate via a mitochondrial acetate: Succinate CoA transferase
    • van Hellemond, J.J., Opperdoes, F.R. Tielens, A.G.M. (1998) Trypanosomatides produce acetate via a mitochondrial acetate: succinate CoA transferase. Proc Natl Acad Sci USA 95 : 3036 3041.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 3036-3041
    • Van Hellemond, J.J.1    Opperdoes, F.R.2    Tielens, A.G.M.3
  • 21
    • 0342614261 scopus 로고    scopus 로고
    • Translation of the edited mRNA for cytochrome b in trypanosome mitochondria
    • Horvath, A., Berry, E.A. Maslov, D.A. (2000a) Translation of the edited mRNA for cytochrome b in trypanosome mitochondria. Science 287 : 1639 1640.
    • (2000) Science , vol.287 , pp. 1639-1640
    • Horvath, A.1    Berry, E.A.2    Maslov, D.A.3
  • 22
    • 0040187760 scopus 로고    scopus 로고
    • Detection of the mitochondrially encoded cytochrome c oxidase subunit I in the trypanosomatid protozoan Leishmania tarentolae
    • Horvath, A., Kingan, T.G. Maslov, D.A. (2000b) Detection of the mitochondrially encoded cytochrome c oxidase subunit I in the trypanosomatid protozoan Leishmania tarentolae. J Biol Chem 275 : 17160 17165.
    • (2000) J Biol Chem , vol.275 , pp. 17160-17165
    • Horvath, A.1    Kingan, T.G.2    Maslov, D.A.3
  • 23
    • 15044345677 scopus 로고    scopus 로고
    • Proline metabolism in procyclic Trypanosoma brucei is down-regulated in the presence of glucose
    • Lamour, N., Riviere, L., Coustou, V., Coombs, G.H., Barrett, M.P. Bringaud, F. (2005) Proline metabolism in procyclic Trypanosoma brucei is down-regulated in the presence of glucose. J Biol Chem 280 : 11902 11910.
    • (2005) J Biol Chem , vol.280 , pp. 11902-11910
    • Lamour, N.1    Riviere, L.2    Coustou, V.3    Coombs, G.H.4    Barrett, M.P.5    Bringaud, F.6
  • 24
    • 9644268250 scopus 로고    scopus 로고
    • Human mitochondrial peptide deformylase, a new anticancer target of actinonin-based antibiotics
    • Lee, M.D., She, Y., Soskis, M.J., Borella, C.P., Gardner, J.R., Hayes, P.A., et al. (2004) Human mitochondrial peptide deformylase, a new anticancer target of actinonin-based antibiotics. J Clin Invest 114 : 1107 1116.
    • (2004) J Clin Invest , vol.114 , pp. 1107-1116
    • Lee, M.D.1    She, Y.2    Soskis, M.J.3    Borella, C.P.4    Gardner, J.R.5    Hayes, P.A.6
  • 25
    • 33748430340 scopus 로고    scopus 로고
    • Peptide deformylase as an antibacterial target: A critical assessment
    • Leeds, J.A. Dean, C.R. (2006) Peptide deformylase as an antibacterial target: a critical assessment. Curr Opin Pharmacol 5 : 445 452.
    • (2006) Curr Opin Pharmacol , vol.5 , pp. 445-452
    • Leeds, J.A.1    Dean, C.R.2
  • 26
    • 33847132229 scopus 로고    scopus 로고
    • Chemotherapeutic strategies against Trypanosoma brucei: Drug targets vs. drug targeting
    • Lüscher, A., de Koning, H. Mäser, P. (2007) Chemotherapeutic strategies against Trypanosoma brucei: drug targets vs. drug targeting. Curr Pharm Des 13 : 555 567.
    • (2007) Curr Pharm des , vol.13 , pp. 555-567
    • Lüscher, A.1    De Koning, H.2    Mäser, P.3
  • 28
    • 0037022284 scopus 로고    scopus 로고
    • Location alters tRNA identity: Trypanosoma brucei's cytosolic elongator methionyl tRNA is both the initiator and elongator in mitochondria
    • Martin, N.C. (2002) Location alters tRNA identity: Trypanosoma brucei's cytosolic elongator methionyl tRNA is both the initiator and elongator in mitochondria. Proc Natl Acad Sci USA 99 : 1110 1112.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 1110-1112
    • Martin, N.C.1
  • 29
    • 0037417874 scopus 로고    scopus 로고
    • Secondary loss of chlorosplasts in trypanosomes
    • Martin, W. Borst, P. (2003) Secondary loss of chlorosplasts in trypanosomes. Proc Natl Acad Sci USA 100 : 765 767.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 765-767
    • Martin, W.1    Borst, P.2
  • 31
    • 0034177339 scopus 로고    scopus 로고
    • Peptide deformylase of eukaryotic: A target for new antiparasitic agents?
    • Meinnel, T. (2000) Peptide deformylase of eukaryotic: a target for new antiparasitic agents? Parasitol Today 16 : 165 168.
    • (2000) Parasitol Today , vol.16 , pp. 165-168
    • Meinnel, T.1
  • 32
    • 0028916186 scopus 로고
    • Enzymatic properties of Escherichia coli peptide deformylase
    • Meinnel, T. Blanquet, S. (1995) Enzymatic properties of Escherichia coli peptide deformylase. J Bact 177 : 1883 1887.
    • (1995) J Bact , vol.177 , pp. 1883-1887
    • Meinnel, T.1    Blanquet, S.2
  • 33
    • 0030004178 scopus 로고    scopus 로고
    • The C-terminal domain of peptide deformylase is disordered and dispensable for activity
    • Meinnel, T., Lazennec, C., Dardel, F., Schmitter, J.M. Blanquet, S. (1996) The C-terminal domain of peptide deformylase is disordered and dispensable for activity. FEBS Lett 385 : 91 95.
    • (1996) FEBS Lett , vol.385 , pp. 91-95
    • Meinnel, T.1    Lazennec, C.2    Dardel, F.3    Schmitter, J.M.4    Blanquet, S.5
  • 34
    • 0031552348 scopus 로고    scopus 로고
    • Structure-function relationships within the peptide deformylase family. Evidence for a conserved architecture of the active site involving three conserved motifs and a metal ion
    • Meinnel, T., Lazennec, C., Villoing, S. Blanquet, S. (1997) Structure-function relationships within the peptide deformylase family. Evidence for a conserved architecture of the active site involving three conserved motifs and a metal ion. J Mol Biol 267 : 749 761.
    • (1997) J Mol Biol , vol.267 , pp. 749-761
    • Meinnel, T.1    Lazennec, C.2    Villoing, S.3    Blanquet, S.4
  • 35
    • 0042473206 scopus 로고    scopus 로고
    • Characterization of a human peptide deformylase: Implications for antibacterial drug design
    • Nguyen, K.T., Hu, X., Colton, C., Chakrabarti, R., Zhu, M.X. Pei, D. (2003) Characterization of a human peptide deformylase: implications for antibacterial drug design. Biochemistry 42 : 9952 9958.
    • (2003) Biochemistry , vol.42 , pp. 9952-9958
    • Nguyen, K.T.1    Hu, X.2    Colton, C.3    Chakrabarti, R.4    Zhu, M.X.5    Pei, D.6
  • 36
    • 0032540979 scopus 로고    scopus 로고
    • Control of peptide deformylase activity by metal cations
    • Ragusa, S., Blanquet, S. Meinnel, T. (1998) Control of peptide deformylase activity by metal cations. J Mol Biol 280 : 515 523.
    • (1998) J Mol Biol , vol.280 , pp. 515-523
    • Ragusa, S.1    Blanquet, S.2    Meinnel, T.3
  • 37
    • 0033603628 scopus 로고    scopus 로고
    • Substrate recognition and selectivity of peptide deformylase. Similarities and differences with metzincins and thermolysin
    • Ragusa, S., Mouchet, P., Lazennec, C., Dive, V. Meinnel, T. (1999) Substrate recognition and selectivity of peptide deformylase. Similarities and differences with metzincins and thermolysin. J Mol Biol 289 : 1445 1457.
    • (1999) J Mol Biol , vol.289 , pp. 1445-1457
    • Ragusa, S.1    Mouchet, P.2    Lazennec, C.3    Dive, V.4    Meinnel, T.5
  • 38
    • 28644444076 scopus 로고    scopus 로고
    • The F1-ATP synthase complex in bloodstream stage trypanosomes has an unusual and essential function
    • Schnaufer, A., Clark-Walker, G.D., Steinberg, A.G. Stuart, K. (2005) The F1-ATP synthase complex in bloodstream stage trypanosomes has an unusual and essential function. EMBO J 24 : 4029 4040.
    • (2005) EMBO J , vol.24 , pp. 4029-4040
    • Schnaufer, A.1    Clark-Walker, G.D.2    Steinberg, A.G.3    Stuart, K.4
  • 39
    • 0034791244 scopus 로고    scopus 로고
    • Unique aspects of mitochondrial biogenesis in trypanosomatids
    • Schneider, A. (2001) Unique aspects of mitochondrial biogenesis in trypanosomatids. Int J Parasitol 31 : 1403 1415.
    • (2001) Int J Parasitol , vol.31 , pp. 1403-1415
    • Schneider, A.1
  • 40
    • 0034578344 scopus 로고    scopus 로고
    • Mitochondrial tRNA import: Are there distinct mechanisms?
    • Schneider, A. Marechal-Drouard, L. (2000) Mitochondrial tRNA import: are there distinct mechanisms? Trends Cell Biol 10 : 509 513.
    • (2000) Trends Cell Biol , vol.10 , pp. 509-513
    • Schneider, A.1    Marechal-Drouard, L.2
  • 41
    • 0023110716 scopus 로고
    • Subpellicular and flagellar microtubules of Trypanosoma brucei contain the same alpha tubulin isotypes
    • Schneider, A., Sherwin, T., Sasse, R., Russell, D., Gull, K. Seebeck, T. (1987) Subpellicular and flagellar microtubules of Trypanosoma brucei contain the same alpha tubulin isotypes. J Cell Biol 104 : 431 438.
    • (1987) J Cell Biol , vol.104 , pp. 431-438
    • Schneider, A.1    Sherwin, T.2    Sasse, R.3    Russell, D.4    Gull, K.5    Seebeck, T.6
  • 42
    • 34547921079 scopus 로고    scopus 로고
    • ATP production in isolated mitochondria of procyclic Trypanosoma brucei
    • Schneider, A., Bouzaidi-Tiali, N., Chanez, A.-L. Bulliard, L. (2007) ATP production in isolated mitochondria of procyclic Trypanosoma brucei. Methods Mol Biol 372 : 379 387.
    • (2007) Methods Mol Biol , vol.372 , pp. 379-387
    • Schneider, A.1    Bouzaidi-Tiali, N.2    Chanez, A.-L.3    Bulliard, L.4
  • 43
    • 0035824874 scopus 로고    scopus 로고
    • Distinctive features of the two classes of eukaryotic peptide deformylases
    • Serero, A., Giglione, C. Meinnel, T. (2001) Distinctive features of the two classes of eukaryotic peptide deformylases. J Mol Biol 314 : 695 708.
    • (2001) J Mol Biol , vol.314 , pp. 695-708
    • Serero, A.1    Giglione, C.2    Meinnel, T.3
  • 44
    • 0347993051 scopus 로고    scopus 로고
    • An unusual peptide deformylase features in the human mitochondrial N-terminal methionine excision pathway
    • Serero, A., Giglione, C., Sardini, A., Martinez-Sanz, J. Meinnel, T. (2003) An unusual peptide deformylase features in the human mitochondrial N-terminal methionine excision pathway. J Biol Chem 278 : 52953 52963.
    • (2003) J Biol Chem , vol.278 , pp. 52953-52963
    • Serero, A.1    Giglione, C.2    Sardini, A.3    Martinez-Sanz, J.4    Meinnel, T.5
  • 45
    • 0037022225 scopus 로고    scopus 로고
    • Eukaryotic-type elongator tRNAMet of Trypanosoma brucei becomes formylated after import into mitochondria
    • Tan, T.H.P., Bochud-Allemannn, N., Horn, E.K. Schneider, A. (2002) Eukaryotic-type elongator tRNAMet of Trypanosoma brucei becomes formylated after import into mitochondria. Proc Natl Acad Sci USA 99 : 1152 1157.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 1152-1157
    • Tan, T.H.P.1    Bochud-Allemannn, N.2    Horn, E.K.3    Schneider, A.4
  • 46
    • 0037630432 scopus 로고    scopus 로고
    • Procyclic Trypanosoma brucei do not use Krebs cycle activity for energy generation
    • van Weelden, S.W., Fast, B., Vogt, A., van der Meer, P., Saas, J., van Hellemond, J.J., et al. (2003) Procyclic Trypanosoma brucei do not use Krebs cycle activity for energy generation. J Biol Chem 278 : 12854 12863.
    • (2003) J Biol Chem , vol.278 , pp. 12854-12863
    • Van Weelden, S.W.1    Fast, B.2    Vogt, A.3    Van Der Meer, P.4    Saas, J.5    Van Hellemond, J.J.6
  • 48
    • 0033525524 scopus 로고    scopus 로고
    • A tightly regulated inducible expression system for conditional gene knock-outs and dominant-negative genetics in Trypanosoma brucei
    • Wirtz, E., Leal, S., Ochatt, C. Cross, G.A. (1999) A tightly regulated inducible expression system for conditional gene knock-outs and dominant-negative genetics in Trypanosoma brucei. Mol Biochem Parasitol 99 : 89 101.
    • (1999) Mol Biochem Parasitol , vol.99 , pp. 89-101
    • Wirtz, E.1    Leal, S.2    Ochatt, C.3    Cross, G.A.4


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