메뉴 건너뛰기




Volumn 73, Issue 3, 1997, Pages 240-251

Consevation of mitochondrial targeting sequence function in mitochondrial and hydrogenosomal proteins from the early-branching eukaryotes Crithidia, Trypanosoma and Trichomonas

Author keywords

Hydrogenosome; Mitochondrial biogenesis; Protein import

Indexed keywords

DIHYDROFOLATE REDUCTASE; HYBRID PROTEIN; PROTEIN; SIGNAL PEPTIDE; FUNGAL DNA; PROTOZOAL DNA;

EID: 0030612496     PISSN: 01719335     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (110)

References (65)
  • 1
    • 0026488195 scopus 로고
    • Glycosome assembly in trypanosomes: Variations in the acceptable degeneracy of a C-terminal microbody targeting signal
    • Blattner, J., B. Swinkels, H. Dörsam, T. Prospero, S. Subramani, C. E. Clayton: Glycosome assembly in trypanosomes: variations in the acceptable degeneracy of a C-terminal microbody targeting signal. J. Cell Biol. 119, 1129-1136 (1992).
    • (1992) J. Cell Biol. , vol.119 , pp. 1129-1136
    • Blattner, J.1    Swinkels, B.2    Dörsam, H.3    Prospero, T.4    Subramani, S.5    Clayton, C.E.6
  • 2
    • 0025793869 scopus 로고
    • Why kinetoplast networks?
    • Borst, P.: Why kinetoplast networks? Trends Genet. 7, 139-141 (1991).
    • (1991) Trends Genet. , vol.7 , pp. 139-141
    • Borst, P.1
  • 3
    • 0025171373 scopus 로고
    • Trypanosoma brucei rhodesiense bloodstream forms: Surface ricin-binding glycoproteins are localized exclusively in the flagellar pocket and the flagellar adhesion zone
    • Brickman, M. J., A.E. Balber: Trypanosoma brucei rhodesiense bloodstream forms: surface ricin-binding glycoproteins are localized exclusively in the flagellar pocket and the flagellar adhesion zone. J. Protozool. 37, 219-24 (1990).
    • (1990) J. Protozool. , vol.37 , pp. 219-224
    • Brickman, M.J.1    Balber, A.E.2
  • 4
    • 0028999123 scopus 로고
    • Characterisation of two nuclear-encoded protein components of mitochondrial ribonucleoprotein complexes from Leishmania tarentolae
    • Bringaud, F., M. Peris, K. H. Zen, L. Simpson: Characterisation of two nuclear-encoded protein components of mitochondrial ribonucleoprotein complexes from Leishmania tarentolae. Mol. Biochem. Parasitol. 71, 65-80 (1995).
    • (1995) Mol. Biochem. Parasitol. , vol.71 , pp. 65-80
    • Bringaud, F.1    Peris, M.2    Zen, K.H.3    Simpson, L.4
  • 5
    • 0029817685 scopus 로고    scopus 로고
    • A common evolutionary origin for mitochondria and hydrogenosomes
    • Bui. E. T., P. J. Bradley, P. J. Johnson: A common evolutionary origin for mitochondria and hydrogenosomes. Proc. Natl. Acad. Sci. USA 93, 9651-9656 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 9651-9656
    • Bui, E.T.1    Bradley, P.J.2    Johnson, P.J.3
  • 6
    • 0029881944 scopus 로고    scopus 로고
    • Identification and characterization of [Fe]-hydrogenases in the hydrogenosome of Trichomonas vaginalis
    • Bui, E. T. N., P. J. Johnson: Identification and characterization of [Fe]-hydrogenases in the hydrogenosome of Trichomonas vaginalis. Mol. Biochem. Parasitol. 76, 305-310 (1996).
    • (1996) Mol. Biochem. Parasitol. , vol.76 , pp. 305-310
    • Bui, E.T.N.1    Johnson, P.J.2
  • 7
    • 0020327085 scopus 로고
    • Resin development for electron microscopy and analysis of embedding at low temperature
    • Oxf.
    • Carlemalm, E., R. M. Garavito, W. Villinger: Resin development for electron microscopy and analysis of embedding at low temperature. J. Microsc. (Oxf.) 126, 123-143 (1982).
    • (1982) J. Microsc. , vol.126 , pp. 123-143
    • Carlemalm, E.1    Garavito, R.M.2    Villinger, W.3
  • 8
    • 0018110116 scopus 로고
    • Prediction of the secondary structure of proteins from from their amino acid sequence
    • Chou, P. Y., G. D. Fasman: Prediction of the secondary structure of proteins from from their amino acid sequence. Adv. Enzymol. 47, 45-148 (1978).
    • (1978) Adv. Enzymol. , vol.47 , pp. 45-148
    • Chou, P.Y.1    Fasman, G.D.2
  • 9
    • 0029166451 scopus 로고
    • Protein trafficking in the kinetoplastid protozoa
    • Clayton, C. E., T. Häusler, J. Blattner: Protein trafficking in the kinetoplastid protozoa. Microbiol. Rev. 59, 325-344 (1995).
    • (1995) Microbiol. Rev. , vol.59 , pp. 325-344
    • Clayton, C.E.1    Häusler, T.2    Blattner, J.3
  • 10
    • 0020479807 scopus 로고
    • Import of proteins into mitochondria: Cytochrome b2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria
    • Daum, G., P. C. Böhni, G. Schatz: Import of proteins into mitochondria: cytochrome b2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria. J. Biol. Chem. 257, 13028-13033 (1982).
    • (1982) J. Biol. Chem. , vol.257 , pp. 13028-13033
    • Daum, G.1    Böhni, P.C.2    Schatz, G.3
  • 13
    • 0027510429 scopus 로고
    • Cloning, sequencing and expression of Trypanosoma brucei dihydrolipoamide dehydrogenase
    • Else, A. J., D. W. Hough, M. J. Danson: Cloning, sequencing and expression of Trypanosoma brucei dihydrolipoamide dehydrogenase. Eur. J. Biochem. 212, 423-429 (1993).
    • (1993) Eur. J. Biochem. , vol.212 , pp. 423-429
    • Else, A.J.1    Hough, D.W.2    Danson, M.J.3
  • 14
    • 0017873321 scopus 로고
    • Analysis of the accuracy and implications of a simple method for predicting the secondary structure of globular proteins
    • Garnier, J., D. J. Osguthorpe, B. Robson: Analysis of the accuracy and implications of a simple method for predicting the secondary structure of globular proteins. J. Mol. Biol. 120, 97-120 (1978).
    • (1978) J. Mol. Biol. , vol.120 , pp. 97-120
    • Garnier, J.1    Osguthorpe, D.J.2    Robson, B.3
  • 16
    • 0026562884 scopus 로고
    • Improved method for high efficiency transformation of intact yeast cells
    • Gietz, D., A. St.Jean, R. A. Woods, R. H. Schiestl: Improved method for high efficiency transformation of intact yeast cells. Nucleic Acids Res. 20, 1425-1425 (1992).
    • (1992) Nucleic Acids Res. , vol.20 , pp. 1425-1425
    • Gietz, D.1    St.Jean, A.2    Woods, R.A.3    Schiestl, R.H.4
  • 17
    • 0025933991 scopus 로고
    • Protein import into isolated yeast mitochondria
    • Glick, B. S.: Protein import into isolated yeast mitochondria. Methods Cell Biol. 34, 389-399 (1991).
    • (1991) Methods Cell Biol. , vol.34 , pp. 389-399
    • Glick, B.S.1
  • 18
    • 0026611680 scopus 로고
    • Cytochromes c1 and b2 are sorted to the intermembrane space of yeast mitochondria by a stop-transfer mechanism
    • Glick, B. S., A. Brandt, K. Cunningham, S. Muller, R. L. Hallberg, G. Schatz: Cytochromes c1 and b2 are sorted to the intermembrane space of yeast mitochondria by a stop-transfer mechanism. Cell 69, 809-822 (1992).
    • (1992) Cell , vol.69 , pp. 809-822
    • Glick, B.S.1    Brandt, A.2    Cunningham, K.3    Muller, S.4    Hallberg, R.L.5    Schatz, G.6
  • 19
    • 0025633802 scopus 로고
    • Biogenesis of mitochondrial c-type cytochromes
    • Gonzales, D. H., W. Neupert: Biogenesis of mitochondrial c-type cytochromes. J. Bioenerg. Biomembr. 22, 753-768 (1990).
    • (1990) J. Bioenerg. Biomembr. , vol.22 , pp. 753-768
    • Gonzales, D.H.1    Neupert, W.2
  • 21
    • 0027057583 scopus 로고
    • Endocytosed transferrin in African trypanosomes is delivered to lysosomes and may not be recycled
    • Grab, D. J., C. W. Wells, M. K. Shaw, P. Webster, D. C. W. Russo: Endocytosed transferrin in African trypanosomes is delivered to lysosomes and may not be recycled. Eur. J. Cell Biol. 59, 398-404 (1992).
    • (1992) Eur. J. Cell Biol. , vol.59 , pp. 398-404
    • Grab, D.J.1    Wells, C.W.2    Shaw, M.K.3    Webster, P.4    Russo, D.C.W.5
  • 22
    • 0027640361 scopus 로고
    • Protein import into mitochondria: A paradigm for the translocation of polypeptides across membranes
    • Hannavy, K., S. Rospert, G. Schatz: Protein import into mitochondria: a paradigm for the translocation of polypeptides across membranes. Curr. Opin. Cell Biol. 5, 694-700 (1993).
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 694-700
    • Hannavy, K.1    Rospert, S.2    Schatz, G.3
  • 23
    • 0030063301 scopus 로고    scopus 로고
    • In vitro import of proteins into mitochondria of Trypanosoma brucei and Leishmania tarentolae
    • Hauser, R., M. Pypaert, T. Häusler, E. K. Horn, A. Schneider: In vitro import of proteins into mitochondria of Trypanosoma brucei and Leishmania tarentolae. J. Cell Sci. 109, 517-523 (1996).
    • (1996) J. Cell Sci. , vol.109 , pp. 517-523
    • Hauser, R.1    Pypaert, M.2    Häusler, T.3    Horn, E.K.4    Schneider, A.5
  • 24
    • 0030034571 scopus 로고    scopus 로고
    • Import of a DHFR-hybrid protein into glycosomes in vivo is not inhibited by the folate-analogue aminopterin
    • Häusler, T., Y. D. Stierhof, E. Wirtz, C. E. Clayton: Import of a DHFR-hybrid protein into glycosomes in vivo is not inhibited by the folate-analogue aminopterin. J. Cell Biol. 132, 311-324 (1996).
    • (1996) J. Cell Biol. , vol.132 , pp. 311-324
    • Häusler, T.1    Stierhof, Y.D.2    Wirtz, E.3    Clayton, C.E.4
  • 25
    • 0022065342 scopus 로고
    • A leader peptide is sufficient to direct mitochondrial import of a chimeric protein
    • Horwich, A. L., F. Kalousek, I. Mellman, L. E. Rosenberg: A leader peptide is sufficient to direct mitochondrial import of a chimeric protein. EMBO J. 4, 1129-1135 (1985).
    • (1985) EMBO J. , vol.4 , pp. 1129-1135
    • Horwich, A.L.1    Kalousek, F.2    Mellman, I.3    Rosenberg, L.E.4
  • 26
    • 0028874227 scopus 로고
    • Primary structure and eubacterial relationships of the pyruvate : Ferredoxin oxidoreductase of the amitochondriate eukaryote Trichomonas vaginalis
    • Hrdy, I., M. Müller: Primary structure and eubacterial relationships of the pyruvate : ferredoxin oxidoreductase of the amitochondriate eukaryote Trichomonas vaginalis. J. Mol. Evol. 41, 388-396 (1995).
    • (1995) J. Mol. Evol. , vol.41 , pp. 388-396
    • Hrdy, I.1    Müller, M.2
  • 27
    • 0029372609 scopus 로고
    • Primary structure of the hydrogenosomal malic enzyme of Trichomonas vaginalis and its relationship to homologous enzymes
    • Hrdy, I., M. Müller: Primary structure of the hydrogenosomal malic enzyme of Trichomonas vaginalis and its relationship to homologous enzymes. J. Eukar. Mikcrobiol. 42, 596-603 (1995).
    • (1995) J. Eukar. Mikcrobiol. , vol.42 , pp. 596-603
    • Hrdy, I.1    Müller, M.2
  • 28
    • 0021676056 scopus 로고
    • The cleavable prepiece of an imported mitochondrial protein is sufficient to direct cytosolic dihydrofolate reductase into the mitochondrial matrix
    • Hurt, E. C., B. Pesold-Hurt, G. Schatz: The cleavable prepiece of an imported mitochondrial protein is sufficient to direct cytosolic dihydrofolate reductase into the mitochondrial matrix. FEBS Lett. 178, 306-310 (1984).
    • (1984) FEBS Lett. , vol.178 , pp. 306-310
    • Hurt, E.C.1    Pesold-Hurt, B.2    Schatz, G.3
  • 29
    • 0022108729 scopus 로고
    • The first twelve amino acids (less than half the presequence) of an imported mitochondrial protein can direct mouse cytosolic dihydrofolate reductase into the yeast mitochondrial matrix
    • Hurt, E. C., B. Pesold-Hurt, K. Suda, W. Oppliger, G. Schatz: The first twelve amino acids (less than half the presequence) of an imported mitochondrial protein can direct mouse cytosolic dihydrofolate reductase into the yeast mitochondrial matrix. EMBO J. 4, 2061-2068 (1985).
    • (1985) EMBO J. , vol.4 , pp. 2061-2068
    • Hurt, E.C.1    Pesold-Hurt, B.2    Suda, K.3    Oppliger, W.4    Schatz, G.5
  • 30
    • 0008479231 scopus 로고
    • Cell biology of Trichomonads: Protein targeting to the hydrogenosome
    • J. C. Boothroyd, R. Komuniecki (eds): Wiley-Liss. New York
    • Johnson, P. J., P. J. Bradley, C. J. Lahti: Cell biology of Trichomonads: protein targeting to the hydrogenosome. In: J. C. Boothroyd, R. Komuniecki (eds): Molecular Approaches to Parasitology. Vol 12. pp. 399-411. Wiley-Liss. New York 1995.
    • (1995) Molecular Approaches to Parasitology , vol.12 , pp. 399-411
    • Johnson, P.J.1    Bradley, P.J.2    Lahti, C.J.3
  • 31
    • 0025180595 scopus 로고
    • Molecular analysis of the hydrogenosomal ferredoxin of the anaerobic protist, Trichomonas vaginalis
    • Johnson, P. J., C. E. d'Oliveira, T. E. Gorrel, M. Müller: Molecular analysis of the hydrogenosomal ferredoxin of the anaerobic protist, Trichomonas vaginalis. Proc. Natl. Acad. Sci. USA 87, 6097-6101 (1990).
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 6097-6101
    • Johnson, P.J.1    D'Oliveira, C.E.2    Gorrel, T.E.3    Müller, M.4
  • 32
    • 0027365367 scopus 로고
    • Biogenesis of the hydrogenosome in the anaerobic protist, Trichomonas vaginalis
    • Johnson, P. J., C. J. Lahti, P. J. Bradley: Biogenesis of the hydrogenosome in the anaerobic protist, Trichomonas vaginalis. J. Parasitol. 79, 664-670 (1993).
    • (1993) J. Parasitol. , vol.79 , pp. 664-670
    • Johnson, P.J.1    Lahti, C.J.2    Bradley, P.J.3
  • 33
    • 0025606107 scopus 로고
    • Identification of a mitochondrial receptor complex required for recognition and membrane insertion of precursor proteins
    • Kiebler, M., R. Pfaller, T. Sollner, G. Griffiths, H. Horstmann, N. Pfanner, W. Neupert: Identification of a mitochondrial receptor complex required for recognition and membrane insertion of precursor proteins. Nature 348, 610-616 (1990).
    • (1990) Nature , vol.348 , pp. 610-616
    • Kiebler, M.1    Pfaller, R.2    Sollner, T.3    Griffiths, G.4    Horstmann, H.5    Pfanner, N.6    Neupert, W.7
  • 34
    • 0028168012 scopus 로고
    • Molecular characterization of the alpha subunit of Trichomonas vaginalis hydrogenosomal succinyl coA synthase
    • Lahti, C. J., P.J. Bradley, P. J. Johnson: Molecular characterization of the alpha subunit of Trichomonas vaginalis hydrogenosomal succinyl coA synthase. Mol. Biochem. Parasitol. 66, 309-318 (1994).
    • (1994) Mol. Biochem. Parasitol. , vol.66 , pp. 309-318
    • Lahti, C.J.1    Bradley, P.J.2    Johnson, P.J.3
  • 35
    • 0026641622 scopus 로고
    • β-succinyl-coenzyme A synthetase from Trichomonas vaginalis is a soluble hydrogenosomal protein with an amino-terminal sequence that resembles mitochondrial presequences
    • Lahti, C. J., C. E. d'Oliveira, P. J. Johnson: β-succinyl-coenzyme A synthetase from Trichomonas vaginalis is a soluble hydrogenosomal protein with an amino-terminal sequence that resembles mitochondrial presequences. J. Bacteriol. 174, 6822-6830 (1992).
    • (1992) J. Bacteriol. , vol.174 , pp. 6822-6830
    • Lahti, C.J.1    D'Oliveira, C.E.2    Johnson, P.J.3
  • 36
    • 0028132843 scopus 로고
    • Primary structure of the hydrogenosomal adenylate kinase of Trichomonas vaginalis and its phylogenetic relationships
    • Länge, S., C. Rozario, M. Müller: Primary structure of the hydrogenosomal adenylate kinase of Trichomonas vaginalis and its phylogenetic relationships. Mol. Biochem. Parasitol. 66, 297-308 (1994).
    • (1994) Mol. Biochem. Parasitol. , vol.66 , pp. 297-308
    • Länge, S.1    Rozario, C.2    Müller, M.3
  • 37
    • 0027241047 scopus 로고
    • Small subunit ribosomal RNA+ of Hexamita inflata and the quest for the first branch in the eucaryotic tree
    • Leipe, D. D., J. H. Gunderson, T. A. Nerad, M. L. Sogin: Small subunit ribosomal RNA+ of Hexamita inflata and the quest for the first branch in the eucaryotic tree. Mol. Biochem. Parasitol. 59, 41-48 (1993).
    • (1993) Mol. Biochem. Parasitol. , vol.59 , pp. 41-48
    • Leipe, D.D.1    Gunderson, J.H.2    Nerad, T.A.3    Sogin, M.L.4
  • 38
    • 0024317055 scopus 로고
    • The mitochondrial targeting function of randomly generated peptide sequences correlates with predicted helical amphiphilicity
    • Lemire, B. D., C. Fankhauser, A. Baker, G. Schatz: The mitochondrial targeting function of randomly generated peptide sequences correlates with predicted helical amphiphilicity. J. Biol. Chem. 264, 20206-20215 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 20206-20215
    • Lemire, B.D.1    Fankhauser, C.2    Baker, A.3    Schatz, G.4
  • 39
    • 0026512613 scopus 로고
    • Kinetoplast DNA and molecular karyotypes of Trypanosoma evansi and Typanosoma equiperdum from China
    • Lun, Z.-R., R. Brun, W. Gibson: Kinetoplast DNA and molecular karyotypes of Trypanosoma evansi and Typanosoma equiperdum from China. Mol. Biochem. Parasitol. 50, 189-196 (1992).
    • (1992) Mol. Biochem. Parasitol. , vol.50 , pp. 189-196
    • Lun, Z.-R.1    Brun, R.2    Gibson, W.3
  • 40
    • 0024151128 scopus 로고
    • Energy metabolism of protozoa without mitochondria
    • Müller, M.: Energy metabolism of protozoa without mitochondria. Annu. Rev. Microbiol. 42, 465-488 (1988).
    • (1988) Annu. Rev. Microbiol. , vol.42 , pp. 465-488
    • Müller, M.1
  • 41
    • 0027787578 scopus 로고
    • The hydrogenosome
    • Müller, M.: The hydrogenosome. J. Gen. Microbiol. 139, 2879-2889 (1993).
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 2879-2889
    • Müller, M.1
  • 43
    • 0026595197 scopus 로고
    • Molecular cloning and expression of the gene encoding the kinetoplast-associated type II DNA topoisomerase of Crithidia fasciculata
    • Pasion, S. G., J. C. Hines, R. Aebersold, D. S. Ray: Molecular cloning and expression of the gene encoding the kinetoplast-associated type II DNA topoisomerase of Crithidia fasciculata. Mol. Biochem. Parasitol. 50, 57-68 (1992).
    • (1992) Mol. Biochem. Parasitol. , vol.50 , pp. 57-68
    • Pasion, S.G.1    Hines, J.C.2    Aebersold, R.3    Ray, D.S.4
  • 44
    • 0027511323 scopus 로고
    • Characterization of a Trypanosoma brucei nuclear gene encoding a protein homologous to a subunit of bovine NADH:ubiquinone oxidoreductase (complex I)
    • Peterson, G. C., A. E. Souza, M. Parsons: Characterization of a Trypanosoma brucei nuclear gene encoding a protein homologous to a subunit of bovine NADH:ubiquinone oxidoreductase (complex I). Mol. Biochem. Parasitol. 58, 63-70 (1993).
    • (1993) Mol. Biochem. Parasitol. , vol.58 , pp. 63-70
    • Peterson, G.C.1    Souza, A.E.2    Parsons, M.3
  • 45
    • 0028180651 scopus 로고
    • Developmental regulation of mitochondrial biogenesis in Trypanosoma brucei
    • Priest, J. W., S. L. Hajduk: Developmental regulation of mitochondrial biogenesis in Trypanosoma brucei. J. Biocnerg. Biomembr. 26, 179-191 (1994).
    • (1994) J. Biocnerg. Biomembr. , vol.26 , pp. 179-191
    • Priest, J.W.1    Hajduk, S.L.2
  • 46
    • 0027915913 scopus 로고
    • Cytochromes c1 of kinetoplastid protozoa lack mitochondrial targeting presequences
    • Priest, J. W., Z. A. Wood, S. L. Hajduk: Cytochromes c1 of kinetoplastid protozoa lack mitochondrial targeting presequences. Biochim. Biophys. Acta 1144, 229-231 (1993).
    • (1993) Biochim. Biophys. Acta , vol.1144 , pp. 229-231
    • Priest, J.W.1    Wood, Z.A.2    Hajduk, S.L.3
  • 47
    • 0028783455 scopus 로고
    • How proteins penetrate peroxisomes
    • Rachubinski, R. A., S. Subramani: How proteins penetrate peroxisomes. Cell 83, 525-528 (1995).
    • (1995) Cell , vol.83 , pp. 525-528
    • Rachubinski, R.A.1    Subramani, S.2
  • 48
    • 0028842614 scopus 로고
    • Protein translocation across mitochondrial membranes: What a long, strange trip it is
    • Ryan, K. R., R. E. Jensen: Protein translocation across mitochondrial membranes: what a long, strange trip it is. Cell 83, 517-519 (1995).
    • (1995) Cell , vol.83 , pp. 517-519
    • Ryan, K.R.1    Jensen, R.E.2
  • 49
    • 0028800022 scopus 로고
    • Shedding light on the chloroplast protein import machinery
    • Schnell, D. J.: Shedding light on the chloroplast protein import machinery. Cell 83, 521-524 (1995).
    • (1995) Cell , vol.83 , pp. 521-524
    • Schnell, D.J.1
  • 50
    • 0027267007 scopus 로고
    • Expression of a mitochondrial stress protein in the protozoan parasite Leishmania major
    • Searle, S., M. V. McCrossan, D. F. Smith: Expression of a mitochondrial stress protein in the protozoan parasite Leishmania major. J. Cell Sci. 104, 1091-1100 (1993).
    • (1993) J. Cell Sci. , vol.104 , pp. 1091-1100
    • Searle, S.1    McCrossan, M.V.2    Smith, D.F.3
  • 51
    • 0026496870 scopus 로고
    • Transport of proteins into the various subcompartments of mitochondria
    • Segui-Real, B., R. A. Stuart, W. Neupert: Transport of proteins into the various subcompartments of mitochondria. FEBS Lett. 313, 2-7 (1992).
    • (1992) FEBS Lett. , vol.313 , pp. 2-7
    • Segui-Real, B.1    Stuart, R.A.2    Neupert, W.3
  • 52
    • 0025251762 scopus 로고
    • RNA-editing - A novel genetic phenomenon?
    • Simpson, L.: RNA-editing - a novel genetic phenomenon? Science 250, 512-513 (1990).
    • (1990) Science , vol.250 , pp. 512-513
    • Simpson, L.1
  • 53
    • 0024962760 scopus 로고
    • Phylogenetic meaning of the kingdom concept: An unusual ribosomal RNA from Giardia lamblia
    • Sogin, M. L., J. H. Gunderson, H. J. Elwood, R. A. Alonso, D. A. Peattie: Phylogenetic meaning of the kingdom concept: an unusual ribosomal RNA from Giardia lamblia. Science 243, 75-77 (1989).
    • (1989) Science , vol.243 , pp. 75-77
    • Sogin, M.L.1    Gunderson, J.H.2    Elwood, H.J.3    Alonso, R.A.4    Peattie, D.A.5
  • 54
    • 0027054829 scopus 로고
    • In vivo import of firefly luciferase into the glycosomes of Trypanosoma brucei and mutational analysis of the C-terminal targeting signal
    • Sommer, J. M., Q.-L. Cheng, G.-A. Keller, C. C. Wang: In vivo import of firefly luciferase into the glycosomes of Trypanosoma brucei and mutational analysis of the C-terminal targeting signal. Mol. Biol. Cell 3, 749-759 (1992).
    • (1992) Mol. Biol. Cell , vol.3 , pp. 749-759
    • Sommer, J.M.1    Cheng, Q.-L.2    Keller, G.-A.3    Wang, C.C.4
  • 55
    • 0028838956 scopus 로고
    • Role of the N-terminal 118 amino acids in the processing of the rat renal mitochondrial glutaminase precursor
    • Srinivasan, M., F. Kalousek, L. Farrell, N. P. Curthoys: Role of the N-terminal 118 amino acids in the processing of the rat renal mitochondrial glutaminase precursor. J. Biol. Chem. 270, 1191-1197 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 1191-1197
    • Srinivasan, M.1    Kalousek, F.2    Farrell, L.3    Curthoys, N.P.4
  • 56
    • 0026014690 scopus 로고
    • RNA editing in trypanosomatid mitochondria
    • Stuart, K.: RNA editing in trypanosomatid mitochondria. Annu. Rev. Microbiol. 45, 327-344 (1991).
    • (1991) Annu. Rev. Microbiol. , vol.45 , pp. 327-344
    • Stuart, K.1
  • 58
    • 0027397584 scopus 로고
    • Protein stability regulates the expression of cytochrome c during the developmental cycle of Trypanosoma brucei
    • Torri, A. F., K. I. Bertrand, S. L. Hajduk: Protein stability regulates the expression of cytochrome c during the developmental cycle of Trypanosoma brucei. Mol. Biochem. Parasitol. 57, 305-316 (1993).
    • (1993) Mol. Biochem. Parasitol. , vol.57 , pp. 305-316
    • Torri, A.F.1    Bertrand, K.I.2    Hajduk, S.L.3
  • 59
    • 0028954473 scopus 로고
    • A DNA polymerase beta in the mitochondrion of the trypanosomatid Crithidia fasciculata
    • Torri, A. F., P. T. Englund: A DNA polymerase beta in the mitochondrion of the trypanosomatid Crithidia fasciculata. J. Biol. Chem. 270, 3495-3497 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 3495-3497
    • Torri, A.F.1    Englund, P.T.2
  • 60
    • 0023796283 scopus 로고
    • Posttranscriptional regulation of cytochrome c expression during the developmental cycle of Trypanosoma brucei
    • Torri, A. F., S. L. Hajduk: Posttranscriptional regulation of cytochrome c expression during the developmental cycle of Trypanosoma brucei. Mol. Cell. Biol. 8, 4625-4633 (1988).
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 4625-4633
    • Torri, A.F.1    Hajduk, S.L.2
  • 61
    • 0024317248 scopus 로고
    • Tight folding of a passenger protein can interfere with the targeting function of a mitochondrial presequence
    • Verner, K., B. D. Lemire: Tight folding of a passenger protein can interfere with the targeting function of a mitochondrial presequence. EMBO J. 8, 1491-1495 (1989).
    • (1989) EMBO J. , vol.8 , pp. 1491-1495
    • Verner, K.1    Lemire, B.D.2
  • 62
    • 0022731676 scopus 로고
    • Mitochondrial targeting sequences may form amphiphilic alpha helices
    • Von Heijne, G.: Mitochondrial targeting sequences may form amphiphilic alpha helices. EMBO J. 5, 1335-1342 (1986).
    • (1986) EMBO J. , vol.5 , pp. 1335-1342
    • Von Heijne, G.1
  • 63
    • 0024418265 scopus 로고
    • Endocytosis by African trypanosomes. II. Occurrence in different life-cycle stages and intracellular sorting
    • Webster, P., W. R. Fish: Endocytosis by African trypanosomes. II. Occurrence in different life-cycle stages and intracellular sorting. Eur. J. Cell Biol. 49, 303-310 (1989).
    • (1989) Eur. J. Cell Biol. , vol.49 , pp. 303-310
    • Webster, P.1    Fish, W.R.2
  • 64
    • 0028989439 scopus 로고
    • Inducible gene expression in trypanosomes mediated by a procaryotic repressor
    • Wirtz, L. E., C. E. Clayton: Inducible gene expression in trypanosomes mediated by a procaryotic repressor. Science 268, 1179-1183 (1995).
    • (1995) Science , vol.268 , pp. 1179-1183
    • Wirtz, L.E.1    Clayton, C.E.2
  • 65
    • 0027499503 scopus 로고
    • Isolation of proteins associated with kinetoplast DNA networks in vivo
    • Xu, C., D. S. Ray: Isolation of proteins associated with kinetoplast DNA networks in vivo. Proc. Natl. Acad. Sci. USA 90, 1786-1789 (1993).
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1786-1789
    • Xu, C.1    Ray, D.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.