메뉴 건너뛰기




Volumn 4, Issue 2, 2005, Pages 337-345

Alteration of a novel dispensable mitochondrial ribosomal small-subunit protein, Rsm28p, allows translation of defective COX2 mRNAs

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C OXIDASE; CYTOCHROME C OXIDASE SUBUNIT II; MESSENGER RNA; MITOCHONDRIAL DNA; MITOCHONDRIAL PROTEIN; PROTEIN SUBUNIT; RIBOSOME PROTEIN; RSM28 PROTEIN, S CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEIN; SIGNAL PEPTIDE;

EID: 13844309959     PISSN: 15359778     EISSN: None     Source Type: Journal    
DOI: 10.1128/EC.4.2.337-345.2005     Document Type: Article
Times cited : (14)

References (68)
  • 2
    • 0025043097 scopus 로고
    • Ribosomal protein L30 is dispensable in the yeast Saccharomyces cerevisiae
    • Baronas-Lowell, D. M., and J. R. Warner. 1990. Ribosomal protein L30 is dispensable in the yeast Saccharomyces cerevisiae. Mol. Cell. Biol. 10:5235-5243.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 5235-5243
    • Baronas-Lowell, D.M.1    Warner, J.R.2
  • 3
    • 0035106396 scopus 로고    scopus 로고
    • Mitochondrial translation of Saccharomyces cerevisiae COX2 mRNA is controlled by the nucleotide sequence specifying the pre-Cox2p leader peptide
    • Bonnefoy, N., N. Bsat, and T. D. Fox. 2001. Mitochondrial translation of Saccharomyces cerevisiae COX2 mRNA is controlled by the nucleotide sequence specifying the pre-Cox2p leader peptide. Mol. Cell. Biol. 21:2359-2372.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 2359-2372
    • Bonnefoy, N.1    Bsat, N.2    Fox, T.D.3
  • 4
    • 0033959624 scopus 로고    scopus 로고
    • m reveals lack of downstream reinitiation
    • m reveals lack of downstream reinitiation. Mol. Gen. Genet. 262:1036-1046.
    • (2000) Mol. Gen. Genet. , vol.262 , pp. 1036-1046
    • Bonnefoy, N.1    Fox, T.D.2
  • 7
    • 0037474205 scopus 로고    scopus 로고
    • A dispensable yeast ribosomal protein optimizes peptidyltransferase activity and affects translocation
    • Dresios, J., P. Panopoulos, K. Suzuki, and D. Synetos. 2003. A dispensable yeast ribosomal protein optimizes peptidyltransferase activity and affects translocation. J. Biol. Chem. 278:3314-3322.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3314-3322
    • Dresios, J.1    Panopoulos, P.2    Suzuki, K.3    Synetos, D.4
  • 8
    • 0030930120 scopus 로고    scopus 로고
    • In vivo analysis of Saccharomyces cerevisiae COX2 mRNA 5′-untranslated leader functions in mitochondrial translation initiation and translational activation
    • Dunstan, H. M., N. S. Green-Willms, and T. D. Fox. 1997. In vivo analysis of Saccharomyces cerevisiae COX2 mRNA 5′-untranslated leader functions in mitochondrial translation initiation and translational activation. Genetics 147:87-100.
    • (1997) Genetics , vol.147 , pp. 87-100
    • Dunstan, H.M.1    Green-Willms, N.S.2    Fox, T.D.3
  • 9
    • 0026703547 scopus 로고
    • A simple and efficient procedure for transformation of yeast
    • Elble, R. 1992. A simple and efficient procedure for transformation of yeast. BioTechniques 13:18-20.
    • (1992) BioTechniques , vol.13 , pp. 18-20
    • Elble, R.1
  • 10
    • 0026726766 scopus 로고
    • Structure and function of MRP20 and MRP49, the nuclear genes for two proteins of the 54 S subunit of the yeast mitochondrial ribosome
    • Fearon, K., and T. L. Mason. 1992. Structure and function of MRP20 and MRP49, the nuclear genes for two proteins of the 54 S subunit of the yeast mitochondrial ribosome. J. Biol. Chem. 267:5162-5170.
    • (1992) J. Biol. Chem. , vol.267 , pp. 5162-5170
    • Fearon, K.1    Mason, T.L.2
  • 11
    • 0023694304 scopus 로고
    • Structure and regulation of a nuclear gene in Saccharomyces cerevisiae that specifies MRP7, a protein of the large subunit of the mitochondrial ribosome
    • Fearon, K., and T. L. Mason. 1988. Structure and regulation of a nuclear gene in Saccharomyces cerevisiae that specifies MRP7, a protein of the large subunit of the mitochondrial ribosome. Mol. Cell. Biol. 8:3636-3646.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 3636-3646
    • Fearon, K.1    Mason, T.L.2
  • 12
    • 0025284833 scopus 로고
    • Striking conservation of TFIID in Schizosaccharomyces pombe and Saccharomyces cerevisiae
    • Fikes, J. D., D. M. Becker, F. Winston, and L. Guarente. 1990. Striking conservation of TFIID in Schizosaccharomyces pombe and Saccharomyces cerevisiae. Nature 346:291-294.
    • (1990) Nature , vol.346 , pp. 291-294
    • Fikes, J.D.1    Becker, D.M.2    Winston, F.3    Guarente, L.4
  • 13
    • 0038819972 scopus 로고    scopus 로고
    • Evidence that synthesis of the Saccharomyces cerevisiae mitochondrially-encoded ribosomal protein Var1p may be membrane localized
    • Fiori, A., T. L. Mason, and T. D. Fox. 2003. Evidence that synthesis of the Saccharomyces cerevisiae mitochondrially-encoded ribosomal protein Var1p may be membrane localized. Eukaryot. Cell. 2:651-653.
    • (2003) Eukaryot. Cell. , vol.2 , pp. 651-653
    • Fiori, A.1    Mason, T.L.2    Fox, T.D.3
  • 14
    • 0028340061 scopus 로고
    • Reduced dosage of genes encoding ribosomal protein S18 suppresses a mitochondrial initiation codon mutation in Saccharomyces cerevisiae
    • Folley, L. S., and T. D. Fox. 1994. Reduced dosage of genes encoding ribosomal protein S18 suppresses a mitochondrial initiation codon mutation in Saccharomyces cerevisiae. Genetics 137:369-379.
    • (1994) Genetics , vol.137 , pp. 369-379
    • Folley, L.S.1    Fox, T.D.2
  • 15
    • 0026038577 scopus 로고
    • Site-directed mutagenesis of a Saccharomyces cerevisiae mitochondrial translation initiation codon
    • Folley, L. S., and T. D. Fox. 1991. Site-directed mutagenesis of a Saccharomyces cerevisiae mitochondrial translation initiation codon. Genetics 129:659-668.
    • (1991) Genetics , vol.129 , pp. 659-668
    • Folley, L.S.1    Fox, T.D.2
  • 16
    • 0003127739 scopus 로고    scopus 로고
    • Genetics of mitochondrial translation
    • J. W. B. Hershey, M. B. Matthews, and N. Sonenberg (ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Fox, T. D. 1996. Genetics of mitochondrial translation, p. 733-758. In J. W. B. Hershey, M. B. Matthews, and N. Sonenberg (ed.), Translational control. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1996) Translational Control , pp. 733-758
    • Fox, T.D.1
  • 18
    • 0020039866 scopus 로고
    • Isolation of intracellular membranes by means of sodium carbonate treatment: Application to endoplasmic reticulum
    • Fujiki, Y., A. L. Hubbard, S. Fowler, and P. B. Lazarow. 1982. Isolation of intracellular membranes by means of sodium carbonate treatment: application to endoplasmic reticulum. J. Cell Biol. 93:97-102.
    • (1982) J. Cell Biol. , vol.93 , pp. 97-102
    • Fujiki, Y.1    Hubbard, A.L.2    Fowler, S.3    Lazarow, P.B.4
  • 19
    • 0036428536 scopus 로고    scopus 로고
    • Tag-mediated isolation of yeast mitochondrial ribosome and mass spectrometric identification of its new components
    • Gan, X., M. Kitakawa, K. Yoshino, N. Oshiro, K. Yonezawa, and K. Isono. 2002. Tag-mediated isolation of yeast mitochondrial ribosome and mass spectrometric identification of its new components. Eur. J. Biochem. 269:5203-5214.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 5203-5214
    • Gan, X.1    Kitakawa, M.2    Yoshino, K.3    Oshiro, N.4    Yonezawa, K.5    Isono, K.6
  • 20
    • 0028856030 scopus 로고
    • Pathways and energetics of mitochondrial protein import in Saccharomyces cerevisiae
    • Glick, B. S. 1995. Pathways and energetics of mitochondrial protein import in Saccharomyces cerevisiae. Methods Enzymol. 260:224-231.
    • (1995) Methods Enzymol. , vol.260 , pp. 224-231
    • Glick, B.S.1
  • 21
    • 0028800976 scopus 로고
    • Isolation of highly purified mitochondria from Saccharomyces cerevisiae
    • Glick, B. S., and L. A. Pon. 1995. Isolation of highly purified mitochondria from Saccharomyces cerevisiae. Methods Enzymol. 260:213-223.
    • (1995) Methods Enzymol. , vol.260 , pp. 213-223
    • Glick, B.S.1    Pon, L.A.2
  • 23
    • 0032008126 scopus 로고    scopus 로고
    • Mitochondrial ribosomal proteins (MRPs) of yeast
    • Graack, H. R., and B. Wittmann-Liebold. 1998. Mitochondrial ribosomal proteins (MRPs) of yeast. Biochem. J. 329:433-448.
    • (1998) Biochem. J. , vol.329 , pp. 433-448
    • Graack, H.R.1    Wittmann-Liebold, B.2
  • 24
    • 0035794171 scopus 로고    scopus 로고
    • Pet111p, an inner membrane-bound translational activator that limits expression of the Saccharomyces cerevisiae mitochondrial gene COX2
    • Green-Willms, N. S., C. A. Butler, H. M. Dunstan, and T. D. Fox. 2001. Pet111p, an inner membrane-bound translational activator that limits expression of the Saccharomyces cerevisiae mitochondrial gene COX2. J. Biol. Chem. 276:6392-6397.
    • (2001) J. Biol. Chem. , vol.276 , pp. 6392-6397
    • Green-Willms, N.S.1    Butler, C.A.2    Dunstan, H.M.3    Fox, T.D.4
  • 25
    • 0031944477 scopus 로고    scopus 로고
    • Functional interactions between yeast mitochondrial ribosomes and mRNA 5′-untranslated leaders
    • Green-Willms, N. S., T. D. Fox, and M. C. Costanzo. 1998. Functional interactions between yeast mitochondrial ribosomes and mRNA 5′- untranslated leaders. Mol. Cell. Biol. 18:1826-1834.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1826-1834
    • Green-Willms, N.S.1    Fox, T.D.2    Costanzo, M.C.3
  • 27
    • 0026443285 scopus 로고
    • Suppression of carboxy-terminal truncations of the yeast mitochondrial mRNA-specific translational activator PET122 by mutations in two new genes, MRP17 and PET127
    • Haffter, P., and T. D. Fox. 1992. Suppression of carboxy-terminal truncations of the yeast mitochondrial mRNA-specific translational activator PET122 by mutations in two new genes, MRP17 and PET127. Mol. Gen. Genet. 235:64-73.
    • (1992) Mol. Gen. Genet. , vol.235 , pp. 64-73
    • Haffter, P.1    Fox, T.D.2
  • 28
    • 0026020194 scopus 로고
    • Functional interactions among two yeast mitochondrial ribosomal proteins and an mRNA-specific translational activator
    • Haffter, P., T. W. McMullin, and T. D. Fox. 1991. Functional interactions among two yeast mitochondrial ribosomal proteins and an mRNA-specific translational activator. Genetics 127:319-326.
    • (1991) Genetics , vol.127 , pp. 319-326
    • Haffter, P.1    McMullin, T.W.2    Fox, T.D.3
  • 29
    • 0027294734 scopus 로고
    • Loss of mitochondrial hsp60 function: Nonequivalent effects on matrix-targeted and intermembrane-targeted proteins
    • Hallberg, E. M., Y. Shu, and R. L. Hallberg. 1993. Loss of mitochondrial hsp60 function: nonequivalent effects on matrix-targeted and intermembrane-targeted proteins. Mol. Biol. Cell 13:3050-3057.
    • (1993) Mol. Biol. Cell , vol.13 , pp. 3050-3057
    • Hallberg, E.M.1    Shu, Y.2    Hallberg, R.L.3
  • 31
    • 0030952628 scopus 로고    scopus 로고
    • Membrane translocation of mitochondrially coded Cox2p: Distinct requirements for export of amino- and carboxy-termini, and dependence on the conserved protein Oxa1p
    • He, S., and T. D. Fox. 1997. Membrane translocation of mitochondrially coded Cox2p: distinct requirements for export of amino- and carboxy-termini, and dependence on the conserved protein Oxa1p. Mol. Biol. Cell 8:1449-1460.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1449-1460
    • He, S.1    Fox, T.D.2
  • 32
    • 0022781503 scopus 로고
    • Yeast/E. coli shuttle vectors with multiple unique restriction sites
    • Hill, J. E., A. M. Myers, T. J. Koerner, and A. Tzagoloff. 1986. Yeast/E. coli shuttle vectors with multiple unique restriction sites. Yeast 2:163-167.
    • (1986) Yeast , vol.2 , pp. 163-167
    • Hill, J.E.1    Myers, A.M.2    Koerner, T.J.3    Tzagoloff, A.4
  • 33
    • 0037064022 scopus 로고    scopus 로고
    • Cbp1 Is Required for Translation of the Mitochondrial Cytochrome b mRNA of Saccharomyces cerevisiae
    • Islas-Osuna, M. A., T. P. Ellis, L. L. Marnell, T. M. Mittelmeier, and C. L. Dieckmann. 2002. Cbp1 Is Required for Translation of the Mitochondrial Cytochrome b mRNA of Saccharomyces cerevisiae. J. Biol. Chem. 277:37987-37990.
    • (2002) J. Biol. Chem. , vol.277 , pp. 37987-37990
    • Islas-Osuna, M.A.1    Ellis, T.P.2    Marnell, L.L.3    Mittelmeier, T.M.4    Dieckmann, C.L.5
  • 34
    • 0348136787 scopus 로고    scopus 로고
    • Yeast Oxa1 interacts with mitochondrial ribosomes: The importance of the C-terminal region of Oxa14
    • Jia, L., M. Dienhart, M. Schramp, M. McCauley, K. Hell, and R. A. Stuart. 2003. Yeast Oxa1 interacts with mitochondrial ribosomes: the importance of the C-terminal region of Oxa14. EMBO J. 22:6438-6447.
    • (2003) EMBO J. , vol.22 , pp. 6438-6447
    • Jia, L.1    Dienhart, M.2    Schramp, M.3    McCauley, M.4    Hell, K.5    Stuart, R.A.6
  • 35
    • 0038349948 scopus 로고    scopus 로고
    • Sequencing and comparison of yeast species to identify genes and regulatory elements
    • Kellis, M., N. Patterson, M. Endrizzi, B. Birren, and E. S. Lander. 2003. Sequencing and comparison of yeast species to identify genes and regulatory elements. Nature 423:241-254.
    • (2003) Nature , vol.423 , pp. 241-254
    • Kellis, M.1    Patterson, N.2    Endrizzi, M.3    Birren, B.4    Lander, E.S.5
  • 36
    • 0035380711 scopus 로고    scopus 로고
    • The small subunit of the mammalian mitochondrial ribosome. Identification of the full complement of ribosomal proteins present
    • Koc, E. C., W. Burkhart, K. Blackburn, A. Moseley, and L. L. Spremulli. 2001. The small subunit of the mammalian mitochondrial ribosome. Identification of the full complement of ribosomal proteins present J. Biol. Chem. 276:19363-19374.
    • (2001) J. Biol. Chem. , vol.276 , pp. 19363-19374
    • Koc, E.C.1    Burkhart, W.2    Blackburn, K.3    Moseley, A.4    Spremulli, L.L.5
  • 37
    • 0035941287 scopus 로고    scopus 로고
    • The large subunit of the mammalian mitochondrial ribosome: Analysis of the complement of ribosomal proteins present
    • Koc, E. C., W. Burkhart, K. Blackburn, M. B. Moyer, D. M. Schlatzer, A. Moseley, and L. L. Spremulli. 2001. The large subunit of the mammalian mitochondrial ribosome: Analysis of the complement of ribosomal proteins present. J. Biol. Chem. 276:43958-43969.
    • (2001) J. Biol. Chem. , vol.276 , pp. 43958-43969
    • Koc, E.C.1    Burkhart, W.2    Blackburn, K.3    Moyer, M.B.4    Schlatzer, D.M.5    Moseley, A.6    Spremulli, L.L.7
  • 38
    • 2542440568 scopus 로고    scopus 로고
    • The mitochondrial message-specific mRNA protectors Cbp1 and Pet309 are associated in a high-molecular weight complex
    • Krause, K., R. Lopes de Souza, D. G. Roberts, and C. L. Dieckmann. 2004. The mitochondrial message-specific mRNA protectors Cbp1 and Pet309 are associated in a high-molecular weight complex. Mol. Biol. Cell 15:2674-2683.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 2674-2683
    • Krause, K.1    Lopes De Souza, R.2    Roberts, D.G.3    Dieckmann, C.L.4
  • 39
    • 0034015357 scopus 로고    scopus 로고
    • Initiation of protein synthesis in Saccharomyces cerevisiae mitochondria without formylation of the initiator tRNA
    • Li, Y., W. B. Holmes, D. R. Appling, and U. L. RajBhandary. 2000. Initiation of protein synthesis in Saccharomyces cerevisiae mitochondria without formylation of the initiator tRNA. J. Bacteriol. 182:2886-2892.
    • (2000) J. Bacteriol. , vol.182 , pp. 2886-2892
    • Li, Y.1    Holmes, W.B.2    Appling, D.R.3    RajBhandary, U.L.4
  • 40
    • 0025161198 scopus 로고
    • A novel small subunit ribosomal protein of yeast mitochondria that interacts functionally with an mRNA-spccific translational activator
    • McMullin, T. W., P. Haffter, and T. D. Fox. 1990. A novel small subunit ribosomal protein of yeast mitochondria that interacts functionally with an mRNA-spccific translational activator. Mol. Cell. Biol. 10:4590-4595.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 4590-4595
    • McMullin, T.W.1    Haffter, P.2    Fox, T.D.3
  • 41
    • 0027768785 scopus 로고
    • Alteration of the Saccharomyces cerevisiae COX2 5′-untranslated leader by mitochondrial gene replacement and functional interaction with the translational activator protein PET111
    • Mulero, J. J., and T. D. Fox. 1993. Alteration of the Saccharomyces cerevisiae COX2 5′-untranslated leader by mitochondrial gene replacement and functional interaction with the translational activator protein PET111. Mol. Biol. Cell 4:1327-1335.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 1327-1335
    • Mulero, J.J.1    Fox, T.D.2
  • 42
    • 0027526328 scopus 로고
    • PET111 acts in the 5′-leader of the Saccharomyces cerevisiae mitochondrial COX2 mRNA to promote its translation
    • Mulero, J. J., and T. D. Fox. 1993. PET111 acts in the 5′-leader of the Saccharomyces cerevisiae mitochondrial COX2 mRNA to promote its translation. Genetics 133:509-516.
    • (1993) Genetics , vol.133 , pp. 509-516
    • Mulero, J.J.1    Fox, T.D.2
  • 43
    • 0028198146 scopus 로고
    • Reduced but accurate translation from a mutant AUA initiation codon in the mitochondrial COX2 mRNA of Saccharomyces cerevisiae
    • Mulero, J. J., and T. D. Fox. 1994. Reduced but accurate translation from a mutant AUA initiation codon in the mitochondrial COX2 mRNA of Saccharomyces cerevisiae. Mol. Gen. Genet. 242:383-390.
    • (1994) Mol. Gen. Genet. , vol.242 , pp. 383-390
    • Mulero, J.J.1    Fox, T.D.2
  • 44
    • 0037238395 scopus 로고    scopus 로고
    • Interactions among COX1, COX2 and COX3 mRNA-specific translational activator proteins on the inner surface of the mitochondrial inner membrane of Saccharomyces cerevisiae
    • Naithani, S., S. A. Saracco, C. A. Butler, and T. D. Fox. 2003. Interactions among COX1, COX2 and COX3 mRNA-specific translational activator proteins on the inner surface of the mitochondrial inner membrane of Saccharomyces cerevisiae. Mol. Biol. Cell 14:324-333.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 324-333
    • Naithani, S.1    Saracco, S.A.2    Butler, C.A.3    Fox, T.D.4
  • 45
    • 0034674626 scopus 로고    scopus 로고
    • Mammalian mitochondrial ribosomal proteins (4). Amino acid sequencing, characterization, and identification of corresponding gene sequences
    • O'Brien, T. W., J. Liu, J. E. Sylvester, E. B. Mougey, N. Fischel-Ghodsian, B. Thiede, B. Wittmann-Liebold, and H. R. Graack. 2000. Mammalian mitochondrial ribosomal proteins (4). Amino acid sequencing, characterization, and identification of corresponding gene sequences. J. Biol. Chem. 275:18153-18159.
    • (2000) J. Biol. Chem. , vol.275 , pp. 18153-18159
    • O'Brien, T.W.1    Liu, J.2    Sylvester, J.E.3    Mougey, E.B.4    Fischel-Ghodsian, N.5    Thiede, B.6    Wittmann-Liebold, B.7    Graack, H.R.8
  • 46
    • 0023778760 scopus 로고
    • Structure and regulation of a nuclear gene in Saccharomyces cerevisiae that specifies MRP13, a protein of the small subunit of the mitochondrial ribosome
    • Partaledis, J. A., and T. L. Mason. 1988. Structure and regulation of a nuclear gene in Saccharomyces cerevisiae that specifies MRP13, a protein of the small subunit of the mitochondrial ribosome. Mol. Cell. Biol. 8:3647-3660.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 3647-3660
    • Partaledis, J.A.1    Mason, T.L.2
  • 47
    • 0028291836 scopus 로고
    • T7 RNA polymerase-dependent expression of COXII in yeast mitochondria
    • Pinkham, J. L., A. M. Dudley, and T. L. Mason. 1994. T7 RNA polymerase-dependent expression of COXII in yeast mitochondria. Mol. Cell. Biol. 14:4643-4652.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 4643-4652
    • Pinkham, J.L.1    Dudley, A.M.2    Mason, T.L.3
  • 48
    • 0024972079 scopus 로고
    • Characterization of the yeast HSP60 gene coding for a mitochondrial assembly factor
    • Reading, D. S., R. L. Hallberg, and A. M. Myers. 1989. Characterization of the yeast HSP60 gene coding for a mitochondrial assembly factor. Nature 337:655-659.
    • (1989) Nature , vol.337 , pp. 655-659
    • Reading, D.S.1    Hallberg, R.L.2    Myers, A.M.3
  • 49
    • 0032828715 scopus 로고    scopus 로고
    • A generic protein purification method for protein complex characterization and proteome exploration
    • Rigaut, G., A. Shevchenko, B. Rutz, M. Wilm, M. Mann, and B. Seraphin. 1999. A generic protein purification method for protein complex characterization and proteome exploration. Nat. Biotcchnol. 17:1030-1032.
    • (1999) Nat. Biotcchnol. , vol.17 , pp. 1030-1032
    • Rigaut, G.1    Shevchenko, A.2    Rutz, B.3    Wilm, M.4    Mann, M.5    Seraphin, B.6
  • 50
    • 1842332123 scopus 로고    scopus 로고
    • Translational activator proteins required for cytochrome b synthesis in Saccharomyces cerevisiae
    • Rödel, G. 1997. Translational activator proteins required for cytochrome b synthesis in Saccharomyces cerevisiae. Curr. Genet. 31:375-379.
    • (1997) Curr. Genet. , vol.31 , pp. 375-379
    • Rödel, G.1
  • 51
    • 0025975312 scopus 로고
    • Cloning genes by complementation in yeast
    • Rose, M. D., and J. R. Broach. 1991. Cloning genes by complementation in yeast. Methods Enzymol. 194:195-230.
    • (1991) Methods Enzymol. , vol.194 , pp. 195-230
    • Rose, M.D.1    Broach, J.R.2
  • 52
    • 0032189225 scopus 로고    scopus 로고
    • Accumulation of mitochondrially synthesized Saccharomyces cerevisiae Cox2p and Cox3p depends on targeting information in untranslated portions of their mRNAs
    • Sanchirico, M. E., T. D. Fox, and T. L. Mason. 1998. Accumulation of mitochondrially synthesized Saccharomyces cerevisiae Cox2p and Cox3p depends on targeting information in untranslated portions of their mRNAs. EMBO J. 17:5796-5804.
    • (1998) EMBO J. , vol.17 , pp. 5796-5804
    • Sanchirico, M.E.1    Fox, T.D.2    Mason, T.L.3
  • 53
    • 0035844183 scopus 로고    scopus 로고
    • Identification of 12 new yeast mitochondrial ribosomal proteins including 6 that have no prokaryotic homologues
    • Saveanu, C., M. Fromont-Racine, A. Harington, F. Ricard, A. Namane, and A. Jacquier. 2001. Identification of 12 new yeast mitochondrial ribosomal proteins including 6 that have no prokaryotic homologues. J. Biol. Chem. 276:15861-15867.
    • (2001) J. Biol. Chem. , vol.276 , pp. 15861-15867
    • Saveanu, C.1    Fromont-Racine, M.2    Harington, A.3    Ricard, F.4    Namane, A.5    Jacquier, A.6
  • 54
    • 0028841139 scopus 로고
    • Use of polymerase chain reaction epitope tagging for protein tagging in Saccharomyces cerevisiae
    • Schneider, B. L., W. Seufert, B. Steiner, Q. H. Yang, and A. B. Futcher. 1995. Use of polymerase chain reaction epitope tagging for protein tagging in Saccharomyces cerevisiae. Yeast 11:1265-1274.
    • (1995) Yeast , vol.11 , pp. 1265-1274
    • Schneider, B.L.1    Seufert, W.2    Steiner, B.3    Yang, Q.H.4    Futcher, A.B.5
  • 55
    • 0024372916 scopus 로고
    • Substitution of an invariant nucleotide at the base of the highly conserved "530-loop" of 15S rRNA causes suppression of mitochondrial ochre mutations
    • Shen, Z., and T. D. Fox. 1989. Substitution of an invariant nucleotide at the base of the highly conserved "530-loop" of 15S rRNA causes suppression of mitochondrial ochre mutations. Nucleic Acids Res. 17:4535-4539.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 4535-4539
    • Shen, Z.1    Fox, T.D.2
  • 57
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R. S., and P. Hieter. 1989. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122:19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 58
    • 0029904234 scopus 로고    scopus 로고
    • Expression of a receded nuclear gene inserted into yeast mitochondrial DNA is limited by mRNA-specific translational activation
    • Steele, D. F., C. A. Butler, and T. D. Fox. 1996. Expression of a receded nuclear gene inserted into yeast mitochondrial DNA is limited by mRNA-specific translational activation. Proc. Natl. Acad. Sci. USA 93:5253-5257.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5253-5257
    • Steele, D.F.1    Butler, C.A.2    Fox, T.D.3
  • 59
    • 0035980117 scopus 로고    scopus 로고
    • Proteomic analysis of the mammalian mitochondrial ribosome. Identification of protein components in the 28 S small subunit
    • Suzuki, T., M. Terasaki, C. Takemoto-Hori, T. Kanada, T. Ueda, A. Wada, and K. Watanabe. 2001. Proteomic analysis of the mammalian mitochondrial ribosome. Identification of protein components in the 28 S small subunit. J. Biol. Chem. 276:33181-33195.
    • (2001) J. Biol. Chem. , vol.276 , pp. 33181-33195
    • Suzuki, T.1    Terasaki, M.2    Takemoto-Hori, C.3    Kanada, T.4    Ueda, T.5    Wada, A.6    Watanabe, K.7
  • 60
    • 0035877697 scopus 로고    scopus 로고
    • Structural compensation for the deficit of rRNA with proteins in the mammalian mitochondrial ribosome. Systematic analysis of protein components of the large ribosomal subunit from mammalian mitochondria
    • Suzuki, T., M. Terasaki, C. Takemoto-Hori, T. Hanada, T. Ueda, A. Wada, and K. Watanabe. 2001. Structural compensation for the deficit of rRNA with proteins in the mammalian mitochondrial ribosome. Systematic analysis of protein components of the large ribosomal subunit from mammalian mitochondria. J. Biol. Chem. 276:21724-21736.
    • (2001) J. Biol. Chem. , vol.276 , pp. 21724-21736
    • Suzuki, T.1    Terasaki, M.2    Takemoto-Hori, C.3    Hanada, T.4    Ueda, T.5    Wada, A.6    Watanabe, K.7
  • 61
    • 0345732691 scopus 로고    scopus 로고
    • Ribosome binding to the Oxa1 complex facilitates co-translational protein insertion in mitochondria
    • Szyrach, G., M. Ott, N. Bonnefoy, W. Neupert, and J. M. Herrmann. 2003. Ribosome binding to the Oxa1 complex facilitates co-translational protein insertion in mitochondria. EMBO J. 22:6448-6457.
    • (2003) EMBO J. , vol.22 , pp. 6448-6457
    • Szyrach, G.1    Ott, M.2    Bonnefoy, N.3    Neupert, W.4    Herrmann, J.M.5
  • 62
    • 0027304446 scopus 로고
    • Inactivation of YME1, a member of the ftsH-SEC18-PAS1-CDC48 family of putative ATPase-encoding genes, causes increased escape of DNA from mitochondria in Saccharomyces cerevisiae
    • Thorsness, P. E., K. H. White, and T. D. Fox. 1993. Inactivation of YME1, a member of the ftsH-SEC18-PAS1-CDC48 family of putative ATPase-encoding genes, causes increased escape of DNA from mitochondria in Saccharomyces cerevisiae. Mol. Cell. Biol. 13:5418-5426.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 5418-5426
    • Thorsness, P.E.1    White, K.H.2    Fox, T.D.3
  • 63
    • 0041856177 scopus 로고    scopus 로고
    • Mammalian mitochondrial initiation factor 2 supports yeast mitochondrial translation without formylated initiator tRNA
    • Tibbetts, A. S., L. Oesterlin, S. Y. Chan, G. Kramer, B. Hardesty, and D. R. Appling. 2003. Mammalian mitochondrial initiation factor 2 supports yeast mitochondrial translation without formylated initiator tRNA. J. Biol. Chem.
    • (2003) J. Biol. Chem.
    • Tibbetts, A.S.1    Oesterlin, L.2    Chan, S.Y.3    Kramer, G.4    Hardesty, B.5    Appling, D.R.6
  • 64
    • 0025953617 scopus 로고
    • Mitochondrial translational-initiation and elongation factors in Saccharomyces cerevisiae
    • Vambutas, A., S. J. 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.J.2    Tzagoloff, A.3
  • 65
    • 0028989018 scopus 로고
    • Analysis of the Saccharomyces cerevisiae mitochondrial COX3 mRNA 5′-untranslated leader: Translational activation and mRNA processing
    • Wiesenberger, G., M. C. Costanzo, and T. D. Fox. 1995. Analysis of the Saccharomyces cerevisiae mitochondrial COX3 mRNA 5′-untranslated leader: translational activation and mRNA processing. Mol. Cell. Biol. 15:3291-3300.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3291-3300
    • Wiesenberger, G.1    Costanzo, M.C.2    Fox, T.D.3
  • 66
    • 0037377349 scopus 로고    scopus 로고
    • Antagonistic signals within the COX2 mRNA coding sequence control its translation in Saccharomyces cerevisiae mitochondria
    • Williams, E. H., and T. D. Fox. 2003. Antagonistic signals within the COX2 mRNA coding sequence control its translation in Saccharomyces cerevisiae mitochondria. RNA 9:419-431.
    • (2003) RNA , vol.9 , pp. 419-431
    • Williams, E.H.1    Fox, T.D.2
  • 67
    • 2942588955 scopus 로고    scopus 로고
    • MrpL36p, a highly diverged L31 ribosomal protein homolog with additional functional domains in Saccharomyces cerevisiae mitochondria
    • Williams, E. H., X. Perez-Martinez, and T. D. Fox. 2004. MrpL36p, a highly diverged L31 ribosomal protein homolog with additional functional domains in Saccharomyces cerevisiae mitochondria. Genetics 167:65-75.
    • (2004) Genetics , vol.167 , pp. 65-75
    • Williams, E.H.1    Perez-Martinez, X.2    Fox, T.D.3
  • 68
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.