메뉴 건너뛰기




Volumn 13, Issue 4, 2014, Pages 539-547

Trypanosome alternative oxidase possesses both an N-terminal and internal mitochondrial targeting signal

Author keywords

[No Author keywords available]

Indexed keywords

DIHYDROFOLATE REDUCTASE; OXIDOREDUCTASE; PROTOZOAL PROTEIN; SIGNAL PEPTIDE;

EID: 84897396246     PISSN: 15359778     EISSN: None     Source Type: Journal    
DOI: 10.1128/EC.00312-13     Document Type: Article
Times cited : (17)

References (42)
  • 1
    • 0030969942 scopus 로고    scopus 로고
    • Protein import into mitochondria
    • Neupert W. 1997. Protein import into mitochondria. Annu. Rev. Biochem. 66:863-917. http://dx.doi.org/10.1146/annurev.biochem.66.1. 863.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 863-917
    • Neupert, W.1
  • 2
    • 0031408095 scopus 로고    scopus 로고
    • Tim54p-Tim22p complex mediates insertion of proteins into the mitochondrial inner membrane
    • Kerscher O, Holder J, Srinivasan M, Leung RS, Jensen RE. 1997. Tim54p-Tim22p complex mediates insertion of proteins into the mitochondrial inner membrane. J. Cell Biol. 139:1663-1675. http://dx.doi.org /10.1083/jcb.139.7.1663.
    • (1997) J. Cell Biol. , vol.139 , pp. 1663-1675
    • Kerscher, O.1    Holder, J.2    Srinivasan, M.3    Leung, R.S.4    Jensen, R.E.5
  • 3
    • 37849035275 scopus 로고    scopus 로고
    • The direct route: A simplified pathway for protein import into the mitochondrion of trypanosomes
    • Schneider A, Bursać D, Lithgow T. 2008. The direct route: a simplified pathway for protein import into the mitochondrion of trypanosomes. Trends Cell Biol. 18:12-18. http://dx.doi.org/10.1016/j.tcb.2007.09.009.
    • (2008) Trends Cell Biol. , vol.18 , pp. 12-18
    • Schneider, A.1    Bursać, D.2    Lithgow, T.3
  • 7
    • 0029942617 scopus 로고    scopus 로고
    • Phylogeny of trypanosomes as inferred from the small and large subunit rRNAs: Implications for the evolution of parasitism in the trypanosomatid protozoa
    • Maslov DA, Lukes J, Jirku M, Simpson L. 1996. Phylogeny of trypanosomes as inferred from the small and large subunit rRNAs: implications for the evolution of parasitism in the trypanosomatid protozoa. Mol. Biochem. Parasitol. 75:197-205. http://dx.doi.org/10.1016 /0166-6851(95)02526-X.
    • (1996) Mol. Biochem. Parasitol. , vol.75 , pp. 197-205
    • Maslov, D.A.1    Lukes, J.2    Jirku, M.3    Simpson, L.4
  • 8
    • 34249873947 scopus 로고    scopus 로고
    • Translocation of proteins into mitochondria
    • Neupert W, Herrmann JM. 2007. Translocation of proteins into mitochondria. Annu. Rev. Biochem. 76:723-749. http://dx.doi.org/10.1146 /annurev.biochem.76.052705.163409.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 723-749
    • Neupert, W.1    Herrmann, J.M.2
  • 9
    • 0001777212 scopus 로고    scopus 로고
    • Protein translocation into mitochondria: The role of TIM complexes
    • Bauer MF, Hofmann S, Neupert W, Brunner M. 2000. Protein translocation into mitochondria: the role of TIM complexes. Trends Cell Biol. 10:25-31. http://dx.doi.org/10.1016/S0962-8924(99)01684-0.
    • (2000) Trends Cell Biol. , vol.10 , pp. 25-31
    • Bauer, M.F.1    Hofmann, S.2    Neupert, W.3    Brunner, M.4
  • 10
    • 18844421618 scopus 로고    scopus 로고
    • Protein import into mitochondria: Origins and functions today
    • Lister R, Hulett JM, Lithgow T, Whelan J. 2005. Protein import into mitochondria: origins and functions today. Mol. Membr. Biol. 22:87-100. http://dx.doi.org/10.1080/09687860500041247.
    • (2005) Mol. Membr. Biol. , vol.22 , pp. 87-100
    • Lister, R.1    Hulett, J.M.2    Lithgow, T.3    Whelan, J.4
  • 11
    • 0032536045 scopus 로고    scopus 로고
    • Import of mitochondrial carriers mediated by essential proteins of the intermembrane space
    • Koehler CM, Jarosch E, Tokatlidis K, Schmid K, Schweyen RJ, Schatz G. 1998. Import of mitochondrial carriers mediated by essential proteins of the intermembrane space. Science 279:369-373. http://dx.doi.org/10. 1126/science.279.5349.369.
    • (1998) Science , vol.279 , pp. 369-373
    • Koehler, C.M.1    Jarosch, E.2    Tokatlidis, K.3    Schmid, K.4    Schweyen, R.J.5    Schatz, G.6
  • 12
    • 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 YD, 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
  • 13
    • 0029166451 scopus 로고
    • Protein trafficking in kinetoplastid protozoa
    • Clayton C, Hausler T, Blattner J. 1995. Protein trafficking in kinetoplastid protozoa. Microbiol. Rev. 59:325-344.
    • (1995) Microbiol. Rev. , vol.59 , pp. 325-344
    • Clayton, C.1    Hausler, T.2    Blattner, J.3
  • 14
    • 0024542834 scopus 로고
    • Domain structure of mitochondrial and chloroplast targeting peptides
    • von Heijne G, Steppuhn J, Herrmann RG. 1989. Domain structure of mitochondrial and chloroplast targeting peptides. Eur. J. Biochem. 180: 535-545. http://dx.doi.org/10.1111/j.1432-1033.1989.tb14679.x.
    • (1989) Eur. J. Biochem. , vol.180 , pp. 535-545
    • von Heijne, G.1    Steppuhn, J.2    Herrmann, R.G.3
  • 15
    • 1542677269 scopus 로고    scopus 로고
    • Trypanosoma brucei has two distinct mitochondrialDNApolymerase beta enzymes
    • Saxowsky TT, Chowdhary G, Klingbeli MM, Englund PT. 2003. Trypanosoma brucei has two distinct mitochondrialDNApolymerase beta enzymes. J. Biol. Chem. 278:49095-49101. http://dx.doi.org/10.1074/jbc. M308565200.
    • (2003) J. Biol. Chem. , vol.278 , pp. 49095-49101
    • Saxowsky, T.T.1    Chowdhary, G.2    Klingbeli, M.M.3    Englund, P.T.4
  • 16
    • 33748309413 scopus 로고    scopus 로고
    • Trypanosome alternative oxidase: From molecule to function
    • Chaudhuri M, Ott RD, Hill GC. 2006. Trypanosome alternative oxidase: from molecule to function. Trends Parasitol. 22:484-491. http://dx.doi. org/10.1016/j.pt.2006.08.007.
    • (2006) Trends Parasitol. , vol.22 , pp. 484-491
    • Chaudhuri, M.1    Ott, R.D.2    Hill, G.C.3
  • 17
    • 0034693765 scopus 로고    scopus 로고
    • New insight into the structure and function of the alternative oxidase
    • Berthold DA, Andersson ME, Nordlund P. 2000. New insight into the structure and function of the alternative oxidase. Biochim. Biophys. Acta 1460:241-254. http://dx.doi.org/10.1016/S0005-2728(00)00149-3.
    • (2000) Biochim. Biophys. Acta , vol.1460 , pp. 241-254
    • Berthold, D.A.1    Andersson, M.E.2    Nordlund, P.3
  • 19
    • 0029915525 scopus 로고    scopus 로고
    • Computational method to predict mitochondrially imported proteins and their targeting sequences
    • Claros MG, Vincens P. 1996. Computational method to predict mitochondrially imported proteins and their targeting sequences. Eur. J. Biochem. 241: 779-786. http://dx.doi.org/10.1111/j.1432-1033.1996.00779.x.
    • (1996) Eur. J. Biochem. , vol.241 , pp. 779-786
    • Claros, M.G.1    Vincens, P.2
  • 20
    • 0343907190 scopus 로고    scopus 로고
    • Vectors for inducible expression of toxic gene products in bloodstream and procyclic Trypanosoma brucei
    • Biebinger S, Wirtz LE, Lorenz P, Clayton C. 1997. Vectors for inducible expression of toxic gene products in bloodstream and procyclic Trypanosoma brucei. Mol. Biochem. Parasitol. 85:99-112. http://dx.doi.org/10. 1016/S0166-6851(96)02815-0.
    • (1997) Mol. Biochem. Parasitol. , vol.85 , pp. 99-112
    • Biebinger, S.1    Wirtz, L.E.2    Lorenz, P.3    Clayton, C.4
  • 21
    • 0033525524 scopus 로고    scopus 로고
    • A tightly regulated inducible expression system for conditional gene knock-outs and dominantnegative genetics in Trypanosoma brucei
    • Wirtz E, Leal S, Ochatt C, Cross GA. 1999. A tightly regulated inducible expression system for conditional gene knock-outs and dominantnegative genetics in Trypanosoma brucei. Mol. Biochem. Parasitol. 99: 89-101. http://dx.doi.org/10.1016/S0166-6851(99)00002-X.
    • (1999) Mol. Biochem. Parasitol. , vol.99 , pp. 89-101
    • Wirtz, E.1    Leal, S.2    Ochatt, C.3    Cross, G.A.4
  • 22
    • 0025832938 scopus 로고
    • In vitro cultivation of Trypanosoma congolense bloodstream form in the absence of feeder cell layers
    • Hirumi H, Hirumi K. 1991. In vitro cultivation of Trypanosoma congolense bloodstream form in the absence of feeder cell layers. Parasitology 102:225-236. http://dx.doi.org/10.1017/S0031182000062533.
    • (1991) Parasitology , vol.102 , pp. 225-236
    • Hirumi, H.1    Hirumi, K.2
  • 23
    • 0036638404 scopus 로고    scopus 로고
    • Trypanosome alternative oxidase is regulated post-transcriptionally at the level of RNA stability
    • Chaudhuri M, Sharan R, Hill GC. 2002. Trypanosome alternative oxidase is regulated post-transcriptionally at the level of RNA stability. J. Eukaryot. Microbiol. 49:263-269. http://dx.doi.org/10.1111/j.1550-7408. 2002.tb00367.x.
    • (2002) J. Eukaryot. Microbiol. , vol.49 , pp. 263-269
    • Chaudhuri, M.1    Sharan, R.2    Hill, G.C.3
  • 24
    • 41649121523 scopus 로고    scopus 로고
    • Characterization of the mitochondrial inner membrane protein translocator Tim17 from Trypanosoma brucei
    • Singha UK, Peprah E, Williams S, Walker R, Saha L, Chaudhuri M. 2008. Characterization of the mitochondrial inner membrane protein translocator Tim17 from Trypanosoma brucei. Mol. Biochem. Parasitol. 159:30-43. http://dx.doi.org/10.1016/j.molbiopara.2008.01.003.
    • (2008) Mol. Biochem. Parasitol. , vol.159 , pp. 30-43
    • Singha, U.K.1    Peprah, E.2    Williams, S.3    Walker, R.4    Saha, L.5    Chaudhuri, M.6
  • 26
    • 38649089796 scopus 로고    scopus 로고
    • Trypanosoma brucei: Differential requirement of membrane potential for import of proteins into mitochondria in two developmental stages
    • Williams S, Saha L, Singha UK, Chaudhuri M. 2008. Trypanosoma brucei: differential requirement of membrane potential for import of proteins into mitochondria in two developmental stages. Exp. Parasitol. 118: 420-433. http://dx.doi.org/10.1016/j.exppara.2007.10.008.
    • (2008) Exp. Parasitol. , vol.118 , pp. 420-433
    • Williams, S.1    Saha, L.2    Singha, U.K.3    Chaudhuri, M.4
  • 27
    • 76749101528 scopus 로고    scopus 로고
    • The small ubiquitine-like modifier (SUMO) is essential in cell cycle regulation in Trypanosoma brucei
    • Liao S, Wang T, Fan K, Tu X. 2010. The small ubiquitine-like modifier (SUMO) is essential in cell cycle regulation in Trypanosoma brucei. Exp. Cell Res. 316:704-715. http://dx.doi.org/10.1016/j.yexcr.2009.12.017.
    • (2010) Exp. Cell Res. , vol.316 , pp. 704-715
    • Liao, S.1    Wang, T.2    Fan, K.3    Tu, X.4
  • 28
    • 79951681150 scopus 로고    scopus 로고
    • Futile import of tRNAs and proteins into mitochondrion of Trypanosoma brucei evansi
    • Paris Z, Hashimi H, Lun S, Alfonzo JD, Lukeš J. 2011. Futile import of tRNAs and proteins into mitochondrion of Trypanosoma brucei evansi. Mol. Biochem. Parasitol. 176:116-120. http://dx.doi.org/10.1016/j.molbi opara.2010.12.010.
    • (2011) Mol. Biochem. Parasitol. , vol.176 , pp. 116-120
    • Paris, Z.1    Hashimi, H.2    Lun, S.3    Alfonzo, J.D.4    Lukeš, J.5
  • 29
    • 69949188844 scopus 로고    scopus 로고
    • Downregulation of mitochondrial porin inhibits cell growth and alters respiratory phenotype in Trypanosoma brucei
    • Singha UK, Sharma S, Chaudhuri M. 2009. Downregulation of mitochondrial porin inhibits cell growth and alters respiratory phenotype in Trypanosoma brucei. Eukaryot. Cell 8:1418-1428. http://dx.doi.org/10. 1128/EC.00132-09.
    • (2009) Eukaryot. Cell , vol.8 , pp. 1418-1428
    • Singha, U.K.1    Sharma, S.2    Chaudhuri, M.3
  • 30
    • 0035925658 scopus 로고    scopus 로고
    • Cloning and characterization of a novel serine/ threonine protein phosphatase type 5 from Trypanosoma brucei
    • Chaudhuri M. 2001. Cloning and characterization of a novel serine/ threonine protein phosphatase type 5 from Trypanosoma brucei. Gene 266:1-13. http://dx.doi.org/10.1016/S0378-1119(01)00367-5.
    • (2001) Gene , vol.266 , pp. 1-13
    • Chaudhuri, M.1
  • 31
    • 34147094091 scopus 로고    scopus 로고
    • Differential effects of arginine methylation on RBP16 mRNA binding, guide RNA (gRNA) binding, and gRNAcontaining ribonucleoprotein complex (gRNP) formation
    • Goulah CC, Read LK. 2007. Differential effects of arginine methylation on RBP16 mRNA binding, guide RNA (gRNA) binding, and gRNAcontaining ribonucleoprotein complex (gRNP) formation. J. Biol. Chem. 282:7181-7190. http://dx.doi.org/10.1074/jbc.M609485200.
    • (2007) J. Biol. Chem. , vol.282 , pp. 7181-7190
    • Goulah, C.C.1    Read, L.K.2
  • 32
    • 0032169175 scopus 로고    scopus 로고
    • Biochemical and molecular properties of the Trypanosoma brucei alternative oxidase
    • Chaudhuri M, Ajayi W, Hill GC. 1998. Biochemical and molecular properties of the Trypanosoma brucei alternative oxidase. Mol. Biochem. Parasitol. 95:53-68. http://dx.doi.org/10.1016/S0166-6851(98)00091-7.
    • (1998) Mol. Biochem. Parasitol. , vol.95 , pp. 53-68
    • Chaudhuri, M.1    Ajayi, W.2    Hill, G.C.3
  • 33
    • 41549083796 scopus 로고    scopus 로고
    • Protein phosphatase 5 is required for Hsp90 function during proteotoxic stresses in Trypanosoma brucei
    • Jones C, Anderson S, Singha UK, Chaudhuri M. 2008. Protein phosphatase 5 is required for Hsp90 function during proteotoxic stresses in Trypanosoma brucei. Parasitol. Res. 102:835-844. http://dx.doi.org/10. 1007/s00436-007-0817-z.
    • (2008) Parasitol. Res. , vol.102 , pp. 835-844
    • Jones, C.1    Anderson, S.2    Singha, U.K.3    Chaudhuri, M.4
  • 34
    • 84872077167 scopus 로고    scopus 로고
    • The N-terminal sequences of four major hydrogenosomal proteins are not essential for import into hydrogenosomes of Trichomonas vaginalis
    • Zimorski V, Major P, Hoffmann K, Brás XP, Martin WF, Gould SB. 2013. The N-terminal sequences of four major hydrogenosomal proteins are not essential for import into hydrogenosomes of Trichomonas vaginalis. J. Eukaryot. Microbiol. 60:89-97. http://dx.doi.org/10.1111/jeu. 12012.
    • (2013) J. Eukaryot. Microbiol. , vol.60 , pp. 89-97
    • Zimorski, V.1    Major, P.2    Hoffmann, K.3    Brás, X.P.4    Martin, W.F.5    Gould, S.B.6
  • 35
    • 0033897694 scopus 로고    scopus 로고
    • Origins of hydrogenosomes and mitochondria: Evolution and organelle biogenesis
    • Dyall SD, Johnson PJ. 2000. Origins of hydrogenosomes and mitochondria: evolution and organelle biogenesis. Curr. Opin. Microbiol. 3:404-411. http://dx.doi.org/10.1016/S1369-5274(00)00112-0.
    • (2000) Curr. Opin. Microbiol. , vol.3 , pp. 404-411
    • Dyall, S.D.1    Johnson, P.J.2
  • 36
    • 0031010331 scopus 로고    scopus 로고
    • Targeting and translocation of proteins into the hydrogenosome of the protist Trichomonas: Similarities with mitochondrial protein import
    • Bradley PJ, Lahti CJ, Plümper E, Johnson PJ. 1997. Targeting and translocation of proteins into the hydrogenosome of the protist Trichomonas: similarities with mitochondrial protein import. EMBO J. 16:3484-3493. http://dx.doi.org/10.1093/emboj/16.12.3484.
    • (1997) EMBO J. , vol.16 , pp. 3484-3493
    • Bradley, P.J.1    Lahti, C.J.2    Plümper, E.3    Johnson, P.J.4
  • 37
    • 2642638742 scopus 로고    scopus 로고
    • Two distinct and independent mitochondrial targeting signals function in the sorting of an inner membrane protein, cytochrome c1
    • Arnold I, Fölsch H, Neupert W, Stuart RA. 1998. Two distinct and independent mitochondrial targeting signals function in the sorting of an inner membrane protein, cytochrome c1. J. Biol. Chem. 273:1469-1476.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1469-1476
    • Arnold, I.1    Fölsch, H.2    Neupert, W.3    Stuart, R.A.4
  • 38
    • 0023663892 scopus 로고
    • Successive translocation into and out of the mitochondrial matrix: Targeting of proteins to the intermembrane space by a bipartite signal peptide
    • Hartl FU, Ostermann J, Guiard B, Neupert W. 1987. Successive translocation into and out of the mitochondrial matrix: targeting of proteins to the intermembrane space by a bipartite signal peptide. Cell 51:1027-1036. http://dx.doi.org/10.1016/0092-8674(87)90589-7.
    • (1987) Cell , vol.51 , pp. 1027-1036
    • Hartl, F.U.1    Ostermann, J.2    Guiard, B.3    Neupert, W.4
  • 39
    • 0030042248 scopus 로고    scopus 로고
    • Internal targeting signal of the BCS1 protein: A novel mechanism of import into mitochondria
    • Fölsch H, Guiard B, Neupert W, Stuart RA. 1996. Internal targeting signal of the BCS1 protein: a novel mechanism of import into mitochondria. EMBO J. 15:479-487.
    • (1996) EMBO J. , vol.15 , pp. 479-487
    • Fölsch, H.1    Guiard, B.2    Neupert, W.3    Stuart, R.A.4
  • 40
    • 0037379222 scopus 로고    scopus 로고
    • Mitochondrial protein import: Recognition of internal import signals of BCS1 by theTOMcomplex
    • Stan T, Brix J, Schneider-Mergener J, Pfanner N, Neupert W, Rapaport D. 2003. Mitochondrial protein import: recognition of internal import signals of BCS1 by theTOMcomplex. Mol. Cell. Biol. 23:2239-2250. http: //dx.doi.org/10.1128/MCB.23.7.2239-2250.2003.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 2239-2250
    • Stan, T.1    Brix, J.2    Schneider-Mergener, J.3    Pfanner, N.4    Neupert, W.5    Rapaport, D.6
  • 42
    • 84873289420 scopus 로고    scopus 로고
    • Tim50 in Trypanosoma brucei possesses a dual specificity phosphatase activity and is critical for mitochondrial protein import
    • Duncan MR, Fullerton M, Chaudhuri M. 2013. Tim50 in Trypanosoma brucei possesses a dual specificity phosphatase activity and is critical for mitochondrial protein import. J. Biol. Chem. 288:3184-3197. http://dx. doi.org/10.1074/jbc.M112.436378.
    • (2013) J. Biol. Chem. , vol.288 , pp. 3184-3197
    • Duncan, M.R.1    Fullerton, M.2    Chaudhuri, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.