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Volumn 182, Issue 10, 2000, Pages 2886-2892

Initiation of protein synthesis in Saccharomyces cerevisiae mitochondria without formylation of the initiator tRNA

Author keywords

[No Author keywords available]

Indexed keywords

METHIONINE TRANSFER RNA; TRANSFER RNA;

EID: 0034015357     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.182.10.2886-2892.2000     Document Type: Article
Times cited : (60)

References (59)
  • 1
    • 0025954883 scopus 로고
    • Compartmentation of folate-mediated one-carbon metabolism in eukaryotes
    • Appling, D. R. 1991. Compartmentation of folate-mediated one-carbon metabolism in eukaryotes. FASEB J. 5:2645-2651.
    • (1991) FASEB J. , vol.5 , pp. 2645-2651
    • Appling, D.R.1
  • 3
    • 0025028977 scopus 로고
    • 1-tetrahydrofolate synthase mutants reveals a noncatalytic function of the ADE3 gene product and an additional folate-dependent enzyme
    • 1-tetrahydrofolate synthase mutants reveals a noncatalytic function of the ADE3 gene product and an additional folate-dependent enzyme. Mol. Cell. Biol. 10:5679-5687.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 5679-5687
    • Barlowe, C.K.1    Appling, D.R.2
  • 4
    • 0017351109 scopus 로고
    • Initiation of protein synthesis without formylation in a mutant of Escherichia coli that grows in the absence of tetrahydrofolate
    • Baumstark, B. R., L. L. Spremulli, U. L. RajBhandary, and G. M. Brown. 1977. Initiation of protein synthesis without formylation in a mutant of Escherichia coli that grows in the absence of tetrahydrofolate. J. Bacteriol. 129:457-471.
    • (1977) J. Bacteriol. , vol.129 , pp. 457-471
    • Baumstark, B.R.1    Spremulli, L.L.2    RajBhandary, U.L.3    Brown, G.M.4
  • 6
    • 0015214584 scopus 로고
    • Endogenous synthesis of formyl-methionine peptides in isolated mitochondria and chloroplasts
    • Bianchetti, R., G. Lucchini, and M. L. Sartirana. 1971. Endogenous synthesis of formyl-methionine peptides in isolated mitochondria and chloroplasts. Biochem. Biophys. Res. Commun. 42:97-102.
    • (1971) Biochem. Biophys. Res. Commun. , vol.42 , pp. 97-102
    • Bianchetti, R.1    Lucchini, G.2    Sartirana, M.L.3
  • 7
    • 0343849354 scopus 로고
    • Some highlights of mitochondrial research based on analyses of Neurospora crassa mitochondrial DNA
    • Breitenberger, C. A., and U. L. RajBhandary. 1985. Some highlights of mitochondrial research based on analyses of Neurospora crassa mitochondrial DNA. Trends Biochem. Sci. 10:478-483.
    • (1985) Trends Biochem. Sci. , vol.10 , pp. 478-483
    • Breitenberger, C.A.1    RajBhandary, U.L.2
  • 8
    • 0019887778 scopus 로고
    • Alignment of the amino terminal amino acid sequence of human cytochrome c oxidase sub-units I and II with the sequence of their putative mRNAs
    • Chomyn, A., M. W. Hunkapiller, and G. Attardi. 1981. Alignment of the amino terminal amino acid sequence of human cytochrome c oxidase sub-units I and II with the sequence of their putative mRNAs. Nucleic Acids Res. 9:867-877.
    • (1981) Nucleic Acids Res. , vol.9 , pp. 867-877
    • Chomyn, A.1    Hunkapiller, M.W.2    Attardi, G.3
  • 9
    • 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. Bohni, and G. Schatz. 1982. 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) J. Biol. Chem. , vol.257 , pp. 13028-13033
    • Daum, G.1    Bohni, P.C.2    Schatz, G.3
  • 10
    • 0016357710 scopus 로고
    • Partial nucleotide sequence of a prokaryote initiator tRNA that functions in its non-formylated form
    • Delk, A. S., and J. C. Rabinowitz. 1974. Partial nucleotide sequence of a prokaryote initiator tRNA that functions in its non-formylated form. Nature 252:106-109.
    • (1974) Nature , vol.252 , pp. 106-109
    • Delk, A.S.1    Rabinowitz, J.C.2
  • 11
    • 0014198149 scopus 로고
    • Methionyl soluble ribonucleic acid transformylase. I. Purification and partial characterization
    • Dickerman, H. W., E. Steers, Jr., B. G. Redfield, and H. Weissbach. 1967. Methionyl soluble ribonucleic acid transformylase. I. Purification and partial characterization. J. Biol. Chem. 242:1522-1525.
    • (1967) J. Biol. Chem. , vol.242 , pp. 1522-1525
    • Dickerman, H.W.1    Steers E., Jr.2    Redfield, B.G.3    Weissbach, H.4
  • 12
    • 0031842442 scopus 로고    scopus 로고
    • Initiation of protein synthesis in mammalian cells with codons other than AUG and amino acids other than methionine
    • Drabkin, H. J., and U. L. RajBhandary. 1998. Initiation of protein synthesis in mammalian cells with codons other than AUG and amino acids other than methionine. Mol. Cell. Biol. 18:5140-5147.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 5140-5147
    • Drabkin, H.J.1    RajBhandary, U.L.2
  • 13
    • 0014842751 scopus 로고
    • N-formylmethionyl transfer ribonucleic acid in mitochondria from Neurospora
    • Epler, J. L., L. R. Shugart, and W. E. Barnett. 1970. N-formylmethionyl transfer ribonucleic acid in mitochondria from Neurospora. Biochemistry 9:3575-3579.
    • (1970) Biochemistry , vol.9 , pp. 3575-3579
    • Epler, J.L.1    Shugart, L.R.2    Barnett, W.E.3
  • 14
    • 0016171653 scopus 로고
    • Mitochondrial biogenesis. Retention of terminal formylmethionine in membrane proteins and regulation of their synthesis
    • Feldman, F., and H. R. Mahler. 1974. Mitochondrial biogenesis. Retention of terminal formylmethionine in membrane proteins and regulation of their synthesis. J. Biol. Chem. 249:3702-3709.
    • (1974) J. Biol. Chem. , vol.249 , pp. 3702-3709
    • Feldman, F.1    Mahler, H.R.2
  • 15
    • 0032426882 scopus 로고    scopus 로고
    • The complete sequence of the mitochondrial genome of Saccharomyces cerevisiae
    • Foury, F., T. Roganti, N. Lecrenier, and B. Purnelle. 1998. The complete sequence of the mitochondrial genome of Saccharomyces cerevisiae. FEBS Lett. 440:325-331.
    • (1998) FEBS Lett. , vol.440 , pp. 325-331
    • Foury, F.1    Roganti, T.2    Lecrenier, N.3    Purnelle, B.4
  • 16
    • 0015243121 scopus 로고
    • Mitochondrial protein synthesis in HeLa cells
    • Galper, J. B., and J. E. Darnell. 1971. Mitochondrial protein synthesis in HeLa cells. J. Mol. Biol. 57:363-367.
    • (1971) J. Mol. Biol. , vol.57 , pp. 363-367
    • Galper, J.B.1    Darnell, J.E.2
  • 17
    • 0014692346 scopus 로고
    • The presence of N-formyl-methionyl-tRNA in HeLa cell mitochondria
    • Galper, J. B., and J. E. Darnell. 1969. The presence of N-formyl-methionyl-tRNA in HeLa cell mitochondria. Biochem. Biophys. Res. Commun. 34:205-214.
    • (1969) Biochem. Biophys. Res. Commun. , vol.34 , pp. 205-214
    • Galper, J.B.1    Darnell, J.E.2
  • 19
    • 0015011935 scopus 로고
    • Isolation of Saccharomyces cerevisiae mitochondrial formyltetrahydrofolic acid:Methionyl-tRNA transformylase and the hybridization of mitochondrial fmet-tRNA with mitochondrial DNA
    • Halbreich, A., and M. Rabinowitz. 1971. Isolation of Saccharomyces cerevisiae mitochondrial formyltetrahydrofolic acid:methionyl-tRNA transformylase and the hybridization of mitochondrial fmet-tRNA with mitochondrial DNA. Proc. Natl. Acad. Sci. USA 68:294-298.
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 294-298
    • Halbreich, A.1    Rabinowitz, M.2
  • 20
  • 21
    • 0020064025 scopus 로고
    • Defects in modification of cytoplasmic and mitochondrial transfer RNAs are caused by single nuclear mutations
    • Hopper, A. K., A. H. Furukawa, H. D. Pham, and N. C. Martin. 1982. Defects in modification of cytoplasmic and mitochondrial transfer RNAs are caused by single nuclear mutations. Cell 28:543-550.
    • (1982) Cell , vol.28 , pp. 543-550
    • Hopper, A.K.1    Furukawa, A.H.2    Pham, H.D.3    Martin, N.C.4
  • 22
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • Ito, H., Y. Fukuda, K. Murata, and A. Kimura. 1983. Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153:163-168.
    • (1983) J. Bacteriol. , vol.153 , pp. 163-168
    • Ito, H.1    Fukuda, Y.2    Murata, K.3    Kimura, A.4
  • 23
    • 0020570527 scopus 로고
    • Comparison of initiation of protein synthesis in procaryotes, eucaryotes, and organelles
    • Kozak, M. 1983. Comparison of initiation of protein synthesis in procaryotes, eucaryotes, and organelles. Microbiol. Rev. 47:1-45.
    • (1983) Microbiol. Rev. , vol.47 , pp. 1-45
    • Kozak, M.1
  • 24
    • 0026757771 scopus 로고
    • Striking effects of coupling mutations in the acceptor stem on recognition of tRNAs by Escherichia coli Met-tRNA synthetase and Met-tRNA transformylase
    • Lee, C. P., M. R. Dyson, N. Mandal, U. Varshney, B. Bahramian, and U. L. RajBhandary. 1992. Striking effects of coupling mutations in the acceptor stem on recognition of tRNAs by Escherichia coli Met-tRNA synthetase and Met-tRNA transformylase. Proc. Natl. Acad. Sci. USA 89:9262-9266.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 9262-9266
    • Lee, C.P.1    Dyson, M.R.2    Mandal, N.3    Varshney, U.4    Bahramian, B.5    RajBhandary, U.L.6
  • 25
    • 0026095269 scopus 로고
    • Structural and sequence elements important for recognition of Escherichia coli formylmethionine tRNA by methionyl-tRNA transformylase are clustered in the acceptor stem
    • Lee, C. P., B. L. Seong, and U. L. RajBhandary. 1991. Structural and sequence elements important for recognition of Escherichia coli formylmethionine tRNA by methionyl-tRNA transformylase are clustered in the acceptor stem. J. Biol. Chem. 266:18012-18017.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18012-18017
    • Lee, C.P.1    Seong, B.L.2    RajBhandary, U.L.3
  • 26
    • 0025836573 scopus 로고
    • Initiation of protein synthesis in animal mitochondria. Purification and characterization of translational initiation factor 2
    • Liao, H.-X., and L. L. Spremulli. 1991. Initiation of protein synthesis in animal mitochondria. Purification and characterization of translational initiation factor 2. J. Biol. Chem. 266:20714-20719.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20714-20719
    • Liao, H.-X.1    Spremulli, L.L.2
  • 27
    • 0028959298 scopus 로고
    • Cloning and sequence analysis of the human mitochondrial translation initiation factor 2 cDNA
    • Ma, L., and L. L. Spremulli. 1995. Cloning and sequence analysis of the human mitochondrial translation initiation factor 2 cDNA. J. Biol. Chem. 270:1859-1865.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1859-1865
    • Ma, L.1    Spremulli, L.L.2
  • 28
    • 0015524102 scopus 로고
    • Formate as a specific label foi mitochondrial translation products
    • Mahler, H. R., K. Dawidowicz, and F. Feldman. 1972. Formate as a specific label foi mitochondrial translation products. J. Biol. Chem. 247:7439-7442.
    • (1972) J. Biol. Chem. , vol.247 , pp. 7439-7442
    • Mahler, H.R.1    Dawidowicz, K.2    Feldman, F.3
  • 29
    • 85025361814 scopus 로고
    • N-formyl-methionyl-sRNA
    • Marcker, K., and F. Sanger. 1964. N-Formyl-methionyl-sRNA. J. Mol. Biol. 8:835-840.
    • (1964) J. Mol. Biol. , vol.8 , pp. 835-840
    • Marcker, K.1    Sanger, F.2
  • 30
    • 0022110054 scopus 로고
    • Mitochondrial protein synthesis is required for maintenance of intact mitochondrial genomes in Saccharomyces cerevisiae
    • Myers, A. M., L. K. Pape, and A. Tzagoloff. 1985. Mitochondrial protein synthesis is required for maintenance of intact mitochondrial genomes in Saccharomyces cerevisiae. EMBO J. 4:2087-2092.
    • (1985) EMBO J. , vol.4 , pp. 2087-2092
    • Myers, A.M.1    Pape, L.K.2    Tzagoloff, A.3
  • 31
    • 0033529488 scopus 로고    scopus 로고
    • Formylation is not essential for initiation of protein synthesis in all eubacteria
    • Newton, D. T., C. Creuzenet, and D. Mangroo. 1999. Formylation is not essential for initiation of protein synthesis in all eubacteria. J. Biol. Chem. 274:22143-22146.
    • (1999) J. Biol. Chem. , vol.274 , pp. 22143-22146
    • Newton, D.T.1    Creuzenet, C.2    Mangroo, D.3
  • 32
    • 0038696703 scopus 로고
    • Tetrazolium overlay technique for population studies of respiration deficiency in yeast
    • Ogur, M., R. St. John, and S. Nagai. 1957. Tetrazolium overlay technique for population studies of respiration deficiency in yeast. Science 125:928-929.
    • (1957) Science , vol.125 , pp. 928-929
    • Ogur, M.1    St. John, R.2    Nagai, S.3
  • 33
    • 0028125575 scopus 로고
    • Initiator transfer RNAs
    • RajBhandary, U. L. 1994. Initiator transfer RNAs. J. Bacteriol. 176:547-552.
    • (1994) J. Bacteriol. , vol.176 , pp. 547-552
    • RajBhandary, U.L.1
  • 34
    • 0026727645 scopus 로고
    • A hit-and-run system for targeted genetic manipulations in yeast
    • Roca, J., M. R. Gartenberg, Y. Oshima, and J. C. Wang. 1992. A hit-and-run system for targeted genetic manipulations in yeast. Nucleic Acids Res. 20: 4671-4672.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 4671-4672
    • Roca, J.1    Gartenberg, M.R.2    Oshima, Y.3    Wang, J.C.4
  • 35
    • 0014828935 scopus 로고
    • Peptide chain initiation in homologous and heterologous systems from mitochondria and bacteria
    • Sala, F., and H. Kuntzel. 1970. Peptide chain initiation in homologous and heterologous systems from mitochondria and bacteria. Eur. J. Biochem. 15:280-286.
    • (1970) Eur. J. Biochem. , vol.15 , pp. 280-286
    • Sala, F.1    Kuntzel, H.2
  • 36
    • 0014940537 scopus 로고
    • Evidence against the folate-mediated formulation of formyl-accepting methionyl transfer ribonucleic acid in Streptococcus faecalis R*
    • Samuel, C. E., L. D'Ari, and J. C. Rabinowitz. 1970. Evidence against the folate-mediated formulation of formyl-accepting methionyl transfer ribonucleic acid in Streptococcus faecalis R*. J. Biol. Chem. 245:5115-5121.
    • (1970) J. Biol. Chem. , vol.245 , pp. 5115-5121
    • Samuel, C.E.1    D'Ari, L.2    Rabinowitz, J.C.3
  • 37
    • 0032404016 scopus 로고    scopus 로고
    • Crystal structure of methionyl-tRNAfMet transformylase complexed with the initiator formyl-methionyl-tRNAfMet
    • Schmitt, E., M. Panvert, S. Blanquet, and Y. Mechulam. 1998. Crystal structure of methionyl-tRNAfMet transformylase complexed with the initiator formyl-methionyl-tRNAfMet. EMBO J. 17:6819-6826.
    • (1998) EMBO J. , vol.17 , pp. 6819-6826
    • Schmitt, E.1    Panvert, M.2    Blanquet, S.3    Mechulam, Y.4
  • 38
    • 0014430579 scopus 로고
    • Cupric ion catalysis in hydrolysis of aminoacyl-tRNA
    • Schofield, P., and P. C. Zamecnik. 1968. Cupric ion catalysis in hydrolysis of aminoacyl-tRNA. Biochim. Biophys. Acta 155:410-416.
    • (1968) Biochim. Biophys. Acta , vol.155 , pp. 410-416
    • Schofield, P.1    Zamecnik, P.C.2
  • 39
    • 0014202488 scopus 로고
    • Involvement of N-formylmethionine in initiation of protein synthesis in cell-free extracts of Euglena gracilis
    • Schwartz, J. H., R. Meyer, J. M. Eisenstadt, and G. Brawerman. 1967. Involvement of N-formylmethionine in initiation of protein synthesis in cell-free extracts of Euglena gracilis. J. Mol. Biol. 25:571-574.
    • (1967) J. Mol. Biol. , vol.25 , pp. 571-574
    • Schwartz, J.H.1    Meyer, R.2    Eisenstadt, J.M.3    Brawerman, G.4
  • 40
    • 0018578028 scopus 로고
    • Identification of amino acid substitutions in the dicyclohexylcarbodiimide-binding subunit of the mitochondrial ATPase complex from oligomycin-resistant mutants of Saccharomyces cerevisiae
    • Sebald, W., E. Wachter, and A. Tzagoloff. 1979. Identification of amino acid substitutions in the dicyclohexylcarbodiimide-binding subunit of the mitochondrial ATPase complex from oligomycin-resistant mutants of Saccharomyces cerevisiae. Eur. J. Biochem. 100:599-607.
    • (1979) Eur. J. Biochem. , vol.100 , pp. 599-607
    • Sebald, W.1    Wachter, E.2    Tzagoloff, A.3
  • 43
    • 0026701349 scopus 로고
    • The sequence of an 8 kb segment on the left arm of chromosome II from Saccharomyces cerevisiae identifies five new open reading frames of unknown functions, two tRNA genes and two transposable elements
    • Skala, J., L. van Dyck, B. Purnelle, and A. Goffeau. 1992. The sequence of an 8 kb segment on the left arm of chromosome II from Saccharomyces cerevisiae identifies five new open reading frames of unknown functions, two tRNA genes and two transposable elements. Yeast 8:777-785.
    • (1992) Yeast , vol.8 , pp. 777-785
    • Skala, J.1    Van Dyck, L.2    Purnelle, B.3    Goffeau, A.4
  • 44
    • 0014414329 scopus 로고
    • N-formylmethionyl transfer RNA in mitochondria from yeast and rat liver
    • Smith, A. E., and K. A. Marcker. 1968. N-formylmethionyl transfer RNA in mitochondria from yeast and rat liver. J. Mol. Biol. 38:241-243.
    • (1968) J. Mol. Biol. , vol.38 , pp. 241-243
    • Smith, A.E.1    Marcker, K.A.2
  • 45
    • 0001869616 scopus 로고
    • Formation of formylmethionyl-tRNA and initiation of protein synthesis
    • R. L. Blakley and S. J. Benkovic (ed.), John Wiley & Sons, Inc., New York, N.Y.
    • Staben, C., and J. C. Rabinowitz. 1984. Formation of formylmethionyl-tRNA and initiation of protein synthesis, p. 457-495. In R. L. Blakley and S. J. Benkovic (ed.), Folates and pterins. vol. 1. John Wiley & Sons, Inc., New York, N.Y.
    • (1984) Folates and Pterins , vol.1 , pp. 457-495
    • Staben, C.1    Rabinowitz, J.C.2
  • 46
    • 0018460106 scopus 로고
    • Studies on cytochrome c oxidase IV. Primary structure and function of subunit II. Hoppe Seylers Z
    • Steffens, G. J., and G. Buse. 1979. Studies on cytochrome c oxidase IV. Primary structure and function of subunit II. Hoppe Seylers Z. Physiol. Chem. 360:613-619.
    • (1979) Physiol. Chem. , vol.360 , pp. 613-619
    • Steffens, G.J.1    Buse, G.2
  • 47
    • 0032510952 scopus 로고    scopus 로고
    • Mammalian mitochondrial methionyl-tRNA transformylase from bovine liver. Purification, characterization, and gene structure
    • Takeuchi, N., M. Kawakami, A. Omori, T. Ueda, L. L. Spremulli, and K. Watanabe. 1998. Mammalian mitochondrial methionyl-tRNA transformylase from bovine liver. Purification, characterization, and gene structure. J. Biol. Chem. 273:15085-15090.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15085-15090
    • Takeuchi, N.1    Kawakami, M.2    Omori, A.3    Ueda, T.4    Spremulli, L.L.5    Watanabe, K.6
  • 48
    • 84912586454 scopus 로고
    • Site directed mutagenesis of the anticodon region: The "universal U" is not essential to tRNA synthesis and function
    • M. Grunberg-Manago and B. Safer (ed.), Interaction of translational and transcriptional controls in the regulation of gene expression. Elsevier Science Publishing Co., New York, N.Y.
    • Thompson, R. C., S. W. Cline, and M. Yarus. 1982. Site directed mutagenesis of the anticodon region: the "universal U" is not essential to tRNA synthesis and function, p. 189-202. In M. Grunberg-Manago and B. Safer (ed.), Interaction of translational and transcriptional controls in the regulation of gene expression. Developments in biochemistry series, vol. 24. Elsevier Science Publishing Co., New York, N.Y.
    • (1982) Developments in Biochemistry Series , vol.24 , pp. 189-202
    • Thompson, R.C.1    Cline, S.W.2    Yarus, M.3
  • 49
    • 0025145542 scopus 로고
    • PET genes of Saccharomyces cerevisiae
    • Tzagoloff, A., and C. L. Dieckmann. 1990. PET genes of Saccharomyces cerevisiae. Microbiol. Rev. 54:211-225.
    • (1990) Microbiol. Rev. , vol.54 , pp. 211-225
    • Tzagoloff, A.1    Dieckmann, C.L.2
  • 50
    • 0018654081 scopus 로고
    • Mitochondrial genes and translation products
    • Tzagoloff, A., G. Macino, and W. Sebald. 1979. Mitochondrial genes and translation products. Annu. Rev. Biochem. 48:419-441.
    • (1979) Annu. Rev. Biochem. , vol.48 , pp. 419-441
    • Tzagoloff, A.1    Macino, G.2    Sebald, W.3
  • 51
    • 0025953617 scopus 로고
    • Mitochondrial translational-initiation and elongation factors in Saccharomyces cerevisiae
    • Vambutas, A., S. H. Ackerman, and A. Tzagoloff. 1991. Mitochondrial translational-initiation and elongation factors in Saccharomyces cerevisiae. Eur. J. Biochem. 201:643-652.
    • (1991) Eur. J. Biochem. , vol.201 , pp. 643-652
    • Vambutas, A.1    Ackerman, S.H.2    Tzagoloff, A.3
  • 52
    • 0026350896 scopus 로고
    • Direct analysis of aminoacylation levels of tRNAs in vivo
    • Varshney, U., C.-P. Lee, and U. L. RajBhandary. 1991. Direct analysis of aminoacylation levels of tRNAs in vivo. J. Biol. Chem. 266:24712-24718.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24712-24718
    • Varshney, U.1    Lee, C.-P.2    RajBhandary, U.L.3
  • 54
    • 0023275830 scopus 로고
    • A family of yeast expression vectors containing the phage f1 intergenic region
    • Vernet, T., D. Dignard, and D. Y. Thomas. 1987. A family of yeast expression vectors containing the phage f1 intergenic region. Gene 52:225-233.
    • (1987) Gene , vol.52 , pp. 225-233
    • Vernet, T.1    Dignard, D.2    Thomas, D.Y.3
  • 55
    • 0025923549 scopus 로고
    • Identification of the subunits of F1F0-ATPase from bovine heart mitochondria
    • Walker, J. E., R. Lutter, A. Dupuis, and M. J. Runswick. 1991. Identification of the subunits of F1F0-ATPase from bovine heart mitochondria. Biochemistry 30:5369-5378.
    • (1991) Biochemistry , vol.30 , pp. 5369-5378
    • Walker, J.E.1    Lutter, R.2    Dupuis, A.3    Runswick, M.J.4
  • 57
    • 0027530611 scopus 로고
    • Cloning and characterization of the Saccharomyces cerevisiae gene encoding NAD-dependent 5,10-methylenetetrahydrofolate dehydrogenase
    • West, M. G., C. K. Barlowe, and D. R. Appling. 1993. Cloning and characterization of the Saccharomyces cerevisiae gene encoding NAD-dependent 5,10-methylenetetrahydrofolate dehydrogenase. J. Biol. Chem. 268:153-160.
    • (1993) J. Biol. Chem. , vol.268 , pp. 153-160
    • West, M.G.1    Barlowe, C.K.2    Appling, D.R.3
  • 58
    • 0029929264 scopus 로고    scopus 로고
    • Metabolic role of cytoplasmic isozymes of 5,10-methylenetetrahydrofolate dehydrogenase in Saccharomyces cerevisiae
    • West, M. G., D. W. Horne, and D. R. Appling. 1996. Metabolic role of cytoplasmic isozymes of 5,10-methylenetetrahydrofolate dehydrogenase in Saccharomyces cerevisiae. Biochemistry 35:3122-3132.
    • (1996) Biochemistry , vol.35 , pp. 3122-3132
    • West, M.G.1    Horne, D.W.2    Appling, D.R.3
  • 59
    • 0025975314 scopus 로고
    • Analysis of mitochondrial function and assembly
    • Yaffe, M. P. 1991. Analysis of mitochondrial function and assembly. Methods Enzymol. 194:627-643.
    • (1991) Methods Enzymol. , vol.194 , pp. 627-643
    • Yaffe, M.P.1


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