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Volumn 181, Issue 14, 1999, Pages 4257-4265

Characterization and submitochondrial localization of the α subunit of the mitochondrial processing peptidase from the aquatic fungus Blastocladiella emersonii

Author keywords

[No Author keywords available]

Indexed keywords

FUNGAL PROTEIN; MESSENGER RNA; PEPTIDASE; SIGNAL PEPTIDE;

EID: 0345593748     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.181.14.4257-4265.1999     Document Type: Article
Times cited : (8)

References (53)
  • 2
    • 0030027663 scopus 로고    scopus 로고
    • Expression of the groESL operon is cell cycle controlled in Caulobacter crescentus
    • Avedissian, M., and S. L. Gomes. 1996. Expression of the groESL operon is cell cycle controlled in Caulobacter crescentus. Mol. Microbiol. 19:79-89.
    • (1996) Mol. Microbiol. , vol.19 , pp. 79-89
    • Avedissian, M.1    Gomes, S.L.2
  • 3
    • 0030597964 scopus 로고    scopus 로고
    • Topological organization of subunits VII and VIII in the ubiquinol-cytochrome c oxidoreductase of Saccharomyces cerevisiae
    • Boumans, H., J. A. Berden, and L. A. Grivell. 1996. Topological organization of subunits VII and VIII in the ubiquinol-cytochrome c oxidoreductase of Saccharomyces cerevisiae. FEBS Lett. 390:137-141.
    • (1996) FEBS Lett. , vol.390 , pp. 137-141
    • Boumans, H.1    Berden, J.A.2    Grivell, L.A.3
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-251.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-251
    • Bradford, M.1
  • 5
    • 0029066902 scopus 로고
    • 1 complex evolutionary relics of a processing protease?
    • 1 complex evolutionary relics of a processing protease? Trends Biochem. Sci. 20:171-175.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 171-175
    • Braun, H.P.1    Schmitz, U.K.2
  • 6
    • 0027498123 scopus 로고
    • Purification and sequencing of cytochrome b from potato reveals methionine cleavage of a mitochondrially encoded protein
    • Braun, H. P., and U. K. Schmitz. 1993. Purification and sequencing of cytochrome b from potato reveals methionine cleavage of a mitochondrially encoded protein. FEBS Lett. 316:128-132.
    • (1993) FEBS Lett. , vol.316 , pp. 128-132
    • Braun, H.P.1    Schmitz, U.K.2
  • 7
    • 0026709336 scopus 로고
    • The general mitochondrial processing peptidase from potato is an integral part of cytochrome c reductase of the respiratory chain
    • Braun, H. P., M. Emmermann, V. Kruft, and U. Schmitz. 1992. The general mitochondrial processing peptidase from potato is an integral part of cytochrome c reductase of the respiratory chain. EMBO J. 11:3219-3227.
    • (1992) EMBO J. , vol.11 , pp. 3219-3227
    • Braun, H.P.1    Emmermann, M.2    Kruft, V.3    Schmitz, U.4
  • 8
    • 0016008005 scopus 로고
    • Mitochondrial fragmentation during germination in Blastocladiella emersonii
    • Bromberg, R. 1974. Mitochondrial fragmentation during germination in Blastocladiella emersonii. Dev. Biol. 36:187-194.
    • (1974) Dev. Biol. , vol.36 , pp. 187-194
    • Bromberg, R.1
  • 9
    • 0028054930 scopus 로고
    • Cloning and characterization of the gene for the catalytic subunit of cAMP-dependent protein kinase in the aquatic fungus Blastocladiella emersonii
    • de Oliveira, J. C. F., A. C. C. Borges, M. V. Marques, and S. L. Gomes. 1994. Cloning and characterization of the gene for the catalytic subunit of cAMP-dependent protein kinase in the aquatic fungus Blastocladiella emersonii. Eur. J. Biochem. 219:555-562.
    • (1994) Eur. J. Biochem. , vol.219 , pp. 555-562
    • De Oliveira, J.C.F.1    Borges, A.C.C.2    Marques, M.V.3    Gomes, S.L.4
  • 10
    • 0023561970 scopus 로고
    • The mitochondrial respiratory chain of yeast. Structure and biosynthesis and the role in cellular metabolism
    • de Vries, S., and A. M. Marres. 1987. The mitochondrial respiratory chain of yeast. Structure and biosynthesis and the role in cellular metabolism. Biochim. Biophys. Acta 895:205-239.
    • (1987) Biochim. Biophys. Acta , vol.895 , pp. 205-239
    • De Vries, S.1    Marres, A.M.2
  • 11
    • 0022587320 scopus 로고
    • Transcription factor Sp1 recognizes a DNA sequence in the mouse dihydrofolate reductase promoter
    • Dynan, W. S., S. Sazer, R. Tjian, and T. H. Ji. 1986. Transcription factor Sp1 recognizes a DNA sequence in the mouse dihydrofolate reductase promoter. Nature 319:246-248.
    • (1986) Nature , vol.319 , pp. 246-248
    • Dynan, W.S.1    Sazer, S.2    Tjian, R.3    Ji, T.H.4
  • 12
    • 0027225845 scopus 로고
    • Characterization of the bifunctional cytochrome c reductase-processing peptidase complex from potato mitochondria
    • Emmermann, M., H.-P. Braun, M. Arretz, and U. K. Schmitz. 1993. Characterization of the bifunctional cytochrome c reductase-processing peptidase complex from potato mitochondria. J. Biol. Chem. 268:18936-18942.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18936-18942
    • Emmermann, M.1    Braun, H.-P.2    Arretz, M.3    Schmitz, U.K.4
  • 14
    • 0020793569 scopus 로고
    • A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity
    • Feinberg, A. P., and B. Volgelstein. 1983. A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Anal. Biochem. 132:6-13.
    • (1983) Anal. Biochem. , vol.132 , pp. 6-13
    • Feinberg, A.P.1    Volgelstein, B.2
  • 15
    • 0022423216 scopus 로고
    • Various rat adult tissues express only major mRNA species from the glyceraldehyde-3-phosphate-dehydrogenase multigenic family
    • Fort, P., L. Marty, M. Piechiczyk, S. El Sabrout, C. Dani, P. Jeanteur, and J. M. Blanchard. 1985. Various rat adult tissues express only major mRNA species from the glyceraldehyde-3-phosphate-dehydrogenase multigenic family. Nucleic Acids Res. 13:1431-1442.
    • (1985) Nucleic Acids Res. , vol.13 , pp. 1431-1442
    • Fort, P.1    Marty, L.2    Piechiczyk, M.3    El Sabrout, S.4    Dani, C.5    Jeanteur, P.6    Blanchard, J.M.7
  • 16
    • 0020039867 scopus 로고
    • Polypeptide and phospholipid composition of the membrane of rat liver peroxisomes: Comparison with endoplasmic reticulum and mitochondrial membranes
    • Fujiki, Y., S. Fowler, H. Shio, A. L. Hubbard, and P. B. Lazarow. 1982. Polypeptide and phospholipid composition of the membrane of rat liver peroxisomes: comparison with endoplasmic reticulum and mitochondrial membranes. J. Cell Biol. 93:103-110.
    • (1982) J. Cell Biol. , vol.93 , pp. 103-110
    • Fujiki, Y.1    Fowler, S.2    Shio, H.3    Hubbard, A.L.4    Lazarow, P.B.5
  • 17
    • 0028177426 scopus 로고
    • 1 complex catalyses both electron transport and protein processing
    • 1 complex catalyses both electron transport and protein processing. FEBS Lett. 346:83-87.
    • (1994) FEBS Lett. , vol.346 , pp. 83-87
    • Glaser, E.1    Eriksson, A.2    Sjoling, S.3
  • 18
    • 0024276898 scopus 로고
    • Mitochondrial protein import: Identification of processing peptidase and of PEP, a processing enhancing protein
    • Hawlitscheck, G., H. Schneider, B. Schmidt, M. Tropschug, F. U. Hartl, and W. Neupert. 1988. Mitochondrial protein import: identification of processing peptidase and of PEP, a processing enhancing protein. Cell 53:795-806.
    • (1988) Cell , vol.53 , pp. 795-806
    • Hawlitscheck, G.1    Schneider, H.2    Schmidt, B.3    Tropschug, M.4    Hartl, F.U.5    Neupert, W.6
  • 19
    • 0000207681 scopus 로고
    • TMBASE - A database of membrane spanning protein segments
    • Hofmann, K., and W. Stoffel. 1993. TMBASE - a database of membrane spanning protein segments. Biol. Chem. 374:166.
    • (1993) Biol. Chem. , vol.374 , pp. 166
    • Hofmann, K.1    Stoffel, W.2
  • 20
    • 0023664271 scopus 로고
    • 1 complex of yeast mitochondria is involved in electron transport at center o and faces the matrix side of the membrane
    • 1 complex of yeast mitochondria is involved in electron transport at center o and faces the matrix side of the membrane. J. Biol. Chem. 262:5441-5444.
    • (1987) J. Biol. Chem. , vol.262 , pp. 5441-5444
    • Japa, S.1    Zhu, Q.-S.2    Beattie, D.S.3
  • 21
    • 0024199388 scopus 로고
    • Import of proteins into yeast mitochondria: The nuclear MAS2 gene encodes a component of the processing protease that is homologous to the MAS1-encoded subunit
    • Jensen, R. E., and M. P. Yaffe. 1988. Import of proteins into yeast mitochondria: the nuclear MAS2 gene encodes a component of the processing protease that is homologous to the MAS1-encoded subunit. EMBO J. 7:3863-3871.
    • (1988) EMBO J. , vol.7 , pp. 3863-3871
    • Jensen, R.E.1    Yaffe, M.P.2
  • 22
    • 0021095327 scopus 로고
    • Structural studies of cytochrome reductase - Subunit topography determined by electron microscopy of membrane crystals of a subcomplex
    • Karlsson, B., S. Hovmoller, H. Weiss, and K. Leonard. 1983. Structural studies of cytochrome reductase - subunit topography determined by electron microscopy of membrane crystals of a subcomplex. J. Mol. Biol. 165: 287-302.
    • (1983) J. Mol. Biol. , vol.165 , pp. 287-302
    • Karlsson, B.1    Hovmoller, S.2    Weiss, H.3    Leonard, K.4
  • 23
    • 0025147397 scopus 로고
    • The general mitochondrial matrix processing protease from rat liver: Structural characterization of the catalytic subunit
    • Kleiber, J., F. Kalousek, M. Swaroop, and L. E. Rosenberg. 1990. The general mitochondrial matrix processing protease from rat liver: structural characterization of the catalytic subunit. Proc. Natl. Acad. Sci. USA 87:7978-7982.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 7978-7982
    • Kleiber, J.1    Kalousek, F.2    Swaroop, M.3    Rosenberg, L.E.4
  • 24
    • 0025334980 scopus 로고
    • Improvements in protein secondary structure prediction by an enhanced neural network
    • Kneller, D. G., F. E. Cohen, and R. Langridge. 1990. Improvements in protein secondary structure prediction by an enhanced neural network. J. Mol. Biol. 214:171-182.
    • (1990) J. Mol. Biol. , vol.214 , pp. 171-182
    • Kneller, D.G.1    Cohen, F.E.2    Langridge, R.3
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 226:680-685.
    • (1970) Nature , vol.226 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0014252359 scopus 로고
    • Ultrastructural changes during sporangium formation and zoospore differentiation in Blastocladiella emersonii
    • Lessie, P. E., and J. S. Lovett. 1968. Ultrastructural changes during sporangium formation and zoospore differentiation in Blastocladiella emersonii. Am. J. Bot. 55:220-236.
    • (1968) Am. J. Bot. , vol.55 , pp. 220-236
    • Lessie, P.E.1    Lovett, J.S.2
  • 27
    • 0022821890 scopus 로고
    • Reconstitution of ubiquinol-cytochrome c reductase from Neurospora mitochondria with regard to subunits I and II
    • Linke, P., and H. Weiss. 1984. Reconstitution of ubiquinol-cytochrome c reductase from Neurospora mitochondria with regard to subunits I and II. Methods Enzymol. 126:201-211.
    • (1984) Methods Enzymol. , vol.126 , pp. 201-211
    • Linke, P.1    Weiss, H.2
  • 28
    • 0016642532 scopus 로고
    • Growth and differentiation of the water mold Blastocladiella emersonii: Cytodifferentiation and the role of ribonucleic acid and protein synthesis
    • Lovett, J. S. 1975. Growth and differentiation of the water mold Blastocladiella emersonii: cytodifferentiation and the role of ribonucleic acid and protein synthesis. Bacteriol. Rev. 39:345-404.
    • (1975) Bacteriol. Rev. , vol.39 , pp. 345-404
    • Lovett, J.S.1
  • 30
    • 0026556669 scopus 로고
    • Coordinate pretranslational control of cAMP-dependent protein kinase subunit expression during development in the water mold Blastocladiella emersonii
    • Marques, M. V., A. C. C. Borges, J. C. F. de Oliveira, and S. L. Gomes. 1992. Coordinate pretranslational control of cAMP-dependent protein kinase subunit expression during development in the water mold Blastocladiella emersonii. Dev. Biol. 149:432-439.
    • (1992) Dev. Biol. , vol.149 , pp. 432-439
    • Marques, M.V.1    Borges, A.C.C.2    De Oliveira, J.C.F.3    Gomes, S.L.4
  • 32
    • 0023461268 scopus 로고
    • Specific synthesis of DNA in vitro via a polymerase-catalysed chain reaction
    • Mullis, K. B., and F. A. Faloona. 1987. Specific synthesis of DNA in vitro via a polymerase-catalysed chain reaction. Methods Enzymol. 155:335-350.
    • (1987) Methods Enzymol. , vol.155 , pp. 335-350
    • Mullis, K.B.1    Faloona, F.A.2
  • 33
    • 0024554495 scopus 로고
    • A new DNA binding and dimerization motif in immunoglobulin enhancer binding, daughterless, MyoD, and myc proteins
    • Murre, C., P. Schonheber, and D. Baltimore. 1989. A new DNA binding and dimerization motif in immunoglobulin enhancer binding, daughterless, MyoD, and myc proteins. Cell 56:777-783.
    • (1989) Cell , vol.56 , pp. 777-783
    • Murre, C.1    Schonheber, P.2    Baltimore, D.3
  • 34
    • 0024468352 scopus 로고
    • Purification and characterization of a processing protease from rat liver mitochondria
    • Ou, W.-J., A. Ito, H. Okasaki, and T. Omura. 1989. Purification and characterization of a processing protease from rat liver mitochondria. EMBO J. 8:2605-2612.
    • (1989) EMBO J. , vol.8 , pp. 2605-2612
    • Ou, W.-J.1    Ito, A.2    Okasaki, H.3    Omura, T.4
  • 35
    • 0023657503 scopus 로고
    • Subunit II of yeast QH2:Cytochrome c oxidoreductase. Nucleotide sequence of the gene and features of the protein
    • Oudshoorn, P., H. Van Steeg, B. W. Swinkeels, P. Schoppink, and L. A. Grivell. 1987. Subunit II of yeast QH2:cytochrome c oxidoreductase. Nucleotide sequence of the gene and features of the protein. Eur. J. Biochem. 163:97-103.
    • (1987) Eur. J. Biochem. , vol.163 , pp. 97-103
    • Oudshoorn, P.1    Van Steeg, H.2    Swinkeels, B.W.3    Schoppink, P.4    Grivell, L.A.5
  • 36
    • 0023989064 scopus 로고
    • Improved tolls for biological sequence comparison
    • Pearson, W. R., and D. J. Lipman. 1988. Improved tolls for biological sequence comparison. Proc. Natl. Acad. Sci. USA 85:2444-2448.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 37
    • 0025360581 scopus 로고
    • The mitochondrial protein import apparatus
    • Pfanner, N., and W. Neupert. 1990. The mitochondrial protein import apparatus. Annu. Rev. Biochem. 59:331-353.
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 331-353
    • Pfanner, N.1    Neupert, W.2
  • 38
    • 0024119655 scopus 로고
    • The processing peptidase of yeast mitochondria: The two cooperating components MPP and PEP are structurally related
    • Pollock, R. A., F.-U. Hartl, M. Y. Cheng, J. Ostermann, A. Horwich, and W. Neupert. 1988. The processing peptidase of yeast mitochondria: the two cooperating components MPP and PEP are structurally related. EMBO J. 7:3493-3500.
    • (1988) EMBO J. , vol.7 , pp. 3493-3500
    • Pollock, R.A.1    Hartl, F.-U.2    Cheng, M.Y.3    Ostermann, J.4    Horwich, A.5    Neupert, W.6
  • 39
    • 0031877337 scopus 로고    scopus 로고
    • Isolation, characterization, and expression of the gene encoding the β-subunit of the mitochondrial processing peptidase from Blastocladiella emersonii
    • Rocha, C. R. C., and S. L. Gomes. 1998. Isolation, characterization, and expression of the gene encoding the β-subunit of the mitochondrial processing peptidase from Blastocladiella emersonii. J. Bacteriol. 180:3967-3972.
    • (1998) J. Bacteriol. , vol.180 , pp. 3967-3972
    • Rocha, C.R.C.1    Gomes, S.L.2
  • 40
    • 0023920458 scopus 로고
    • Mitochondrial presequences
    • Roise, D., and G. Schatz. 1988. Mitochondrial presequences. J. Biol. Chem. 263:4509-4511.
    • (1988) J. Biol. Chem. , vol.263 , pp. 4509-4511
    • Roise, D.1    Schatz, G.2
  • 41
    • 0029988881 scopus 로고    scopus 로고
    • Control of messenger RNA stability in higher eukaryotes
    • Ross, J. 1996. Control of messenger RNA stability in higher eukaryotes. Trends Genet. 12:171-175.
    • (1996) Trends Genet. , vol.12 , pp. 171-175
    • Ross, J.1
  • 44
    • 0022548832 scopus 로고
    • Developmental changes in translatable RNA species and protein synthesis during sporulation in the aquatic fungus Blastocladiella emersonii
    • Silva, A. M., J. C. C. Maia, and M. H. Juliani. 1986. Developmental changes in translatable RNA species and protein synthesis during sporulation in the aquatic fungus Blastocladiella emersonii. Cell Differ. 18:263-274.
    • (1986) Cell Differ. , vol.18 , pp. 263-274
    • Silva, A.M.1    Maia, J.C.C.2    Juliani, M.H.3
  • 45
  • 46
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedures and some applications
    • Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedures and some applications. Proc. Natl. Acad. Sci. USA 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 47
    • 0025194064 scopus 로고
    • 1 complexes of microorganisms
    • 1 complexes of microorganisms. Microbiol. Rev. 54:101-129.
    • (1990) Microbiol. Rev. , vol.54 , pp. 101-129
    • Trumpower, B.L.1
  • 48
    • 0022555846 scopus 로고
    • Genetics of mitochondrial biogenesis
    • Tzagoloff, A., and A. M. Myers. 1986. Genetics of mitochondrial biogenesis. Annu. Rev. Biochem. 55:249-285.
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 249-285
    • Tzagoloff, A.1    Myers, A.M.2
  • 49
    • 0029910729 scopus 로고    scopus 로고
    • Large-subunit rrna sequence of the chytridiomycete Blastocladiella emersonii, and implications for the evolution of zoosporic fungi
    • van der Auwera, G. V. D., and R. De Wachter. 1996. Large-subunit rRNA sequence of the chytridiomycete Blastocladiella emersonii, and implications for the evolution of zoosporic fungi. J. Mol. Evol. 43:476-483.
    • (1996) J. Mol. Evol. , vol.43 , pp. 476-483
    • Van Der Auwera, G.V.D.1    De Wachter, R.2
  • 50
    • 0022731676 scopus 로고
    • Mitochondrial targeting sequences may form amphiphilic helices
    • von Heijne, G. 1986. Mitochondrial targeting sequences may form amphiphilic helices. EMBO J. 5:1335-1342.
    • (1986) EMBO J. , vol.5 , pp. 1335-1342
    • Von Heijne, G.1
  • 51
    • 0024542834 scopus 로고
    • Domain structure of mitochondrial and chloroplast targeting peptides
    • von Heijne, G., J. Steppuhn, and R. G. Hermann. 1989. Domain structure of mitochondrial and chloroplast targeting peptides. Eur. J. Biochem. 180:535-545.
    • (1989) Eur. J. Biochem. , vol.180 , pp. 535-545
    • Von Heijne, G.1    Steppuhn, J.2    Hermann, R.G.3
  • 52
    • 0027241482 scopus 로고
    • Monophyletic origins of the metazoa: An evolutionary link with fungi
    • Wainright, P. O., G. Hinkle, M. L. Sogin, and S. K. Stickel. 1993. Monophyletic origins of the metazoa: an evolutionary link with fungi. Science 260:340-342.
    • (1993) Science , vol.260 , pp. 340-342
    • Wainright, P.O.1    Hinkle, G.2    Sogin, M.L.3    Stickel, S.K.4


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