메뉴 건너뛰기




Volumn 154, Issue 3, 2000, Pages 1013-1023

Proteasome mutants, pre4-2 and ump1-2, suppress the essential function but not the mitochondrial RNase P function of the Saccharomyces cerevisiae gene RPM2

Author keywords

[No Author keywords available]

Indexed keywords

PROTEASOME; RIBONUCLEASE; TRANSFER RNA;

EID: 0034006634     PISSN: 00166731     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (10)

References (64)
  • 2
    • 0030737501 scopus 로고    scopus 로고
    • Identification of the yeast 20S proteasome catalytic centers and subunit interactions required for active-site formation
    • ARENDT, C. S., and M. HOCHSTRASSER, 1997 Identification of the yeast 20S proteasome catalytic centers and subunit interactions required for active-site formation. Proc. Natl. Acad. Sci. USA 94: 7156-7161.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 7156-7161
    • Arendt, S.C.1    Hochstrasser, M.2
  • 4
    • 0031694197 scopus 로고    scopus 로고
    • Escape of mitochondrial DNA to the nucleus in yme1 yeast is mediated by vacuolar-dependent turnover of abnormal mitochondrial compartments
    • CAMPBELL, C. L., and P. E. THORSNESS, 1998 Escape of mitochondrial DNA to the nucleus in yme1 yeast is mediated by vacuolar-dependent turnover of abnormal mitochondrial compartments. J. Cell Sci. 111: 2455-2464.
    • (1998) J. Cell Sci. , vol.111 , pp. 2455-2464
    • Campbell, C.L.1    Thorsness, P.E.2
  • 5
    • 0027979074 scopus 로고
    • Mitochondrial morphological and functional defects in yeast caused by yme1 are suppressed by mutation of a 26S protease subunit homologue
    • CAMPBELL, C. L., N. TANAKA, K. H. WHITE and P. E. THORSNESS, 1994 Mitochondrial morphological and functional defects in yeast caused by yme1 are suppressed by mutation of a 26S protease subunit homologue. Mol. Biol. Cell 5: 899-905.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 899-905
    • Campbell, C.L.1    Tanaka, N.2    White, K.H.3    Thorsness, P.E.4
  • 6
    • 0026599048 scopus 로고
    • One-step transformation of yeast in stationary phase
    • CHEN, D. C., B. C. YANG and T. T. KUO, 1992 One-step transformation of yeast in stationary phase. Curr. Genet. 21: 83-84.
    • (1992) Curr. Genet. , vol.21 , pp. 83-84
    • Chen, D.C.1    Yang, B.C.2    Kuo, T.T.3
  • 7
    • 0028999726 scopus 로고
    • Biogenesis, structure and function of the yeast 20S proteasome
    • CHEN, P., and M. HOCHSTRASSER, 1995 Biogenesis, structure and function of the yeast 20S proteasome. EMBO J. 14: 2620-2030.
    • (1995) EMBO J. , vol.14 , pp. 2620-12030
    • Chen, P.1    Hochstrasser, M.2
  • 8
    • 0030595329 scopus 로고    scopus 로고
    • Autocatalytic subunit processing couples active site formation in the 20S proteasome to completion of assembly
    • CHEN, P., and M. HOCHSTRASSER, 1996 Autocatalytic subunit processing couples active site formation in the 20S proteasome to completion of assembly. Cell 86: 961-972.
    • (1996) Cell , vol.86 , pp. 961-972
    • Chen, P.1    Hochstrasser, M.2
  • 9
    • 0030308964 scopus 로고    scopus 로고
    • Ubiquitin-dependent proteolysis and cell cycle control in yeast
    • CHUN, K. T., N. MATHIAS and M. G. GOEBL, 1996 Ubiquitin-dependent proteolysis and cell cycle control in yeast. Prog. Cell Cycle Res. 2: 115-127.
    • (1996) Prog. Cell Cycle Res. , vol.2 , pp. 115-127
    • Chun, K.T.1    Mathias, N.2    Goebl, M.G.3
  • 10
    • 0032539909 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway: The complexity and myriad functions of protein death
    • CIECHANOVER, A., and A. L. SCHWARTZ, 1998 The ubiquitin-proteasome pathway: the complexity and myriad functions of protein death. Proc. Natl. Acad. Sci. USA 95: 2727-2730.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2727-2730
    • Ciechanover, A.1    Schwartz, A.L.2
  • 11
    • 0027290914 scopus 로고
    • Yeast mitochondrial RNase P. Sequence of the RPM2 gene and demonstration that its product is a protein subunit of the enzyme
    • DANG, Y. L., and N. C. MARTIN, 1993 Yeast mitochondrial RNase P. Sequence of the RPM2 gene and demonstration that its product is a protein subunit of the enzyme. J. Biol. Chem. 268: 19791-19796.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19791-19796
    • Dang, Y.L.1    Martin, N.C.2
  • 12
    • 0032944237 scopus 로고    scopus 로고
    • MitBASe pilot: A database on nuclear genes involved in mitochondrial biogenesis and its regulation in Saccharomyces cerevisiae
    • DE PINTO, B., S. B. MALIADI and N. ALTAMURA, 1999 MitBASe pilot: a database on nuclear genes involved in mitochondrial biogenesis and its regulation in Saccharomyces cerevisiae. Nucleic Acids Res. 27: 147-149.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 147-149
    • De Pinto, B.1    Maliadi, S.B.2    Altamura, N.3
  • 13
    • 0033553857 scopus 로고    scopus 로고
    • A role for ubiquilination in mitochondrial inheritance in Saccharomyces cerevisiae
    • FISK, H. A., and M. P. YAFFE, 1999 A role for ubiquilination in mitochondrial inheritance in Saccharomyces cerevisiae. J. Cell Biol. 145: 1199-1208.
    • (1999) J. Cell Biol. , vol.145 , pp. 1199-1208
    • Fisk, H.A.1    Yaffe, M.P.2
  • 14
    • 0031815994 scopus 로고    scopus 로고
    • The regulatory particle of the Saccharomyces cerevisiae proteasome
    • GLICKMAN, M. H., D. M. RUBIN, V. A. FREID and D. FINLEY, 1998 The regulatory particle of the Saccharomyces cerevisiae proteasome. Mol. Cell. Biol. 18: 3149-3162.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3149-3162
    • Glickman, M.H.1    Rubin, D.M.2    Freid, V.A.3    Finley, D.4
  • 15
    • 0030905981 scopus 로고    scopus 로고
    • New insights into the mechanisms and importance of the proteasome in intracellular protein degradation
    • GOLDBERG, A. L., T. N. AKOPIAN, A. F. KISSELEV, D. H. LEE and M. ROHRWOLD, 1997 New insights into the mechanisms and importance of the proteasome in intracellular protein degradation. Biol. Chem. 378: 131-140.
    • (1997) Biol. Chem. , vol.378 , pp. 131-140
    • Goldberg, A.L.1    Akopian, T.N.2    Kisselev, A.F.3    Lee, D.H.4    Rohrwold, M.5
  • 16
    • 0030897031 scopus 로고    scopus 로고
    • Structure of 20S proteasome from yeast at 2.4 a resolution
    • GROLL, M., L. DITZEL, J. LOWE, D. STOCK, M. BOCHTLER et al., 1997 Structure of 20S proteasome from yeast at 2.4 A resolution. Nature 386: 463-471.
    • (1997) Nature , vol.386 , pp. 463-471
    • Groll, M.1    Ditzel, L.2    Lowe, J.3    Stock, D.4    Bochtler, M.5
  • 18
    • 0032518643 scopus 로고    scopus 로고
    • Kluyveromyces lactis SEF1 and its Saccharomyces cerevisiae homologue bypass the unknown essential function, but not the mitochondrial RNase P function, of the S. cerevisiae RPM2 gene
    • GROOM, K. R., H. C. HEYMAN, M. C. STEFFEN, L. HAWKINS and N. C. MARTIN, 1998 Kluyveromyces lactis SEF1 and its Saccharomyces cerevisiae homologue bypass the unknown essential function, but not the mitochondrial RNase P function, of the S. cerevisiae RPM2 gene. Yeast 14: 77-87.
    • (1998) Yeast , vol.14 , pp. 77-87
    • Groom, K.R.1    Heyman, H.C.2    Steffen, M.C.3    Hawkins, L.4    Martin, N.C.5
  • 19
    • 0013601039 scopus 로고
    • Immunochemical probes of ubiquitin pool dynamics
    • edited by M. RECHSTEINER. Plenum Press, Salt Lake City
    • HAAS, A. L., 1988 Immunochemical probes of ubiquitin pool dynamics, pp. 173-206 in Ubiquitin, edited by M. RECHSTEINER. Plenum Press, Salt Lake City.
    • (1988) Ubiquitin , pp. 173-206
    • Haas, A.L.1
  • 20
    • 0022379602 scopus 로고
    • The immunochemical detection and quantitation of intracellular ubiquitin-protein conjugates
    • HAAS, A. L., and P. M. BRIGHT, 1985 The immunochemical detection and quantitation of intracellular ubiquitin-protein conjugates. J. Biol. Chem. 260: 12464-12473.
    • (1985) J. Biol. Chem. , vol.260 , pp. 12464-12473
    • Haas, A.L.1    Bright, P.M.2
  • 21
    • 0030774890 scopus 로고    scopus 로고
    • The active sites of the eukaryotic 20S proteasome and their involvement in subunit precursor processing
    • HEINEMEYER, W., M. FISHER, T. KRIMMER, U. STACHNON and D. H. WOLF, 1997 The active sites of the eukaryotic 20S proteasome and their involvement in subunit precursor processing. J. Biol. Chem. 272: 25200-25209.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25200-25209
    • Heinemeyer, W.1    Fisher, M.2    Krimmer, T.3    Stachnon, U.4    Wolf, D.H.5
  • 22
    • 0030724422 scopus 로고    scopus 로고
    • Roles of ubiquitin-mediated proteolysis in cell cycle control
    • HERSHKO, A., 1997 Roles of ubiquitin-mediated proteolysis in cell cycle control. Curr. Opin. Cell Biol. 9: 788-799.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 788-799
    • Hershko, A.1
  • 23
    • 0032188847 scopus 로고    scopus 로고
    • Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins
    • HILL, K., K. MODEL, M. T. RYAN, K. DIETMEIER, F. MARTIN et al., 1998 Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins. Nature 395: 516-521.
    • (1998) Nature , vol.395 , pp. 516-521
    • Hill, K.1    Model, K.2    Ryan, M.T.3    Dietmeier, K.4    Martin, F.5
  • 24
    • 0029867623 scopus 로고    scopus 로고
    • Proteasomes: Destruction as a programme
    • HILT, W., and D. H. WOLF, 1996 Proteasomes: destruction as a programme. Trends Biochem. Sci. 21: 96-102.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 96-102
    • Hilt, W.1    Wolf, D.H.2
  • 25
    • 0027457543 scopus 로고
    • The PRE4 gene codes for a subunit of the yeast proteasome necessary for peptidylglutamyl-peptide-hydrolyzing activity. Mutations link the proteasome to stress- and ubiquitin-dependent proteolysis
    • HILT, W., C. ENENKEL, A. GRUHLER, T. SINGER and D. H. WOLF, 1993 The PRE4 gene codes for a subunit of the yeast proteasome necessary for peptidylglutamyl-peptide-hydrolyzing activity. Mutations link the proteasome to stress- and ubiquitin-dependent proteolysis. J. Biol. Chem. 268: 3479-3486.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3479-3486
    • Hilt, W.1    Enenkel, C.2    Gruhler, A.3    Singer, T.4    Wolf, D.H.5
  • 27
    • 0029129982 scopus 로고
    • RPM2, independently of its mitochondrial RNase P function, suppresses an 1SP42 mutant defective in mitochondrial import and is essential for normal growth
    • KASSENBROCK, C. K., G. J. GAO, K. R. GROOM, P. SULO, M. G. DOUGLAS et al., 1995 RPM2, independently of its mitochondrial RNase P function, suppresses an 1SP42 mutant defective in mitochondrial import and is essential for normal growth. Mol. Cell. Biol. 15: 4763-4770.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4763-4770
    • Kassenbrock, C.K.1    Gao, G.J.2    Groom, K.R.3    Sulo, P.4    Douglas, M.G.5
  • 29
    • 0030949874 scopus 로고    scopus 로고
    • ER quality control: The cytoplasmic connection
    • KOPTTO, R. R., 1997 ER quality control: the cytoplasmic connection. Cell 88: 427-430.
    • (1997) Cell , vol.88 , pp. 427-430
    • Koptto, R.R.1
  • 31
    • 0029775087 scopus 로고    scopus 로고
    • AAa proteases with catalytic sites on opposite membrane surfaces comprise a proteolytic system for the ATP-dependent degradation of inner membrane proteins in mitochondria
    • LEONHARD, K., J. M. HERRMANN, R. A. STUART, G. MANNHAUPT, W. NEUPERT et al., 1996 AAA proteases with catalytic sites on opposite membrane surfaces comprise a proteolytic system for the ATP-dependent degradation of inner membrane proteins in mitochondria. EMBO J. 15: 4218-4229.
    • (1996) EMBO J. , vol.15 , pp. 4218-4229
    • Leonhard, K.1    Herrmann, J.M.2    Stuart, R.A.3    Mannhaupt, G.4    Neupert, W.5
  • 32
    • 0025718671 scopus 로고
    • Evidence for a paniculate location of ubiquitin conjugates and ubiquitin-conjugating enzymes in rabbit brain
    • MAGNANI, M., G. SERAFINI, A. ANTONELLI, M. MALATESTA and G. GAZZANELLI, 1991 Evidence for a paniculate location of ubiquitin conjugates and ubiquitin-conjugating enzymes in rabbit brain. J. Biol. Chem. 266: 21018-21024.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21018-21024
    • Magnani, M.1    Serafini, G.2    Antonelli, A.3    Malatesta, M.4    Gazzanelli, G.5
  • 33
    • 0026697569 scopus 로고
    • Identification of the mitochondrial receptor complex in Saccharomyces cerevisiae
    • MOCZKO, M., K. DIETMEIER, T. SOLLNER, B. SEGUI, H. F. STEGER et al., 1992 Identification of the mitochondrial receptor complex in Saccharomyces cerevisiae. FEBS Lett. 310: 265-268.
    • (1992) FEBS Lett. , vol.310 , pp. 265-268
    • Moczko, M.1    Dietmeier, K.2    Sollner, T.3    Segui, B.4    Steger, H.F.5
  • 35
    • 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
  • 36
    • 0030880547 scopus 로고    scopus 로고
    • Intermediates in the formation of mouse 20S proteasomes: Implications for the assembly of precursor beta subunits
    • NANDI, D., E. WOODWARD, D. B. GINSBURG and J. J. MONACO, 1997 Intermediates in the formation of mouse 20S proteasomes: implications for the assembly of precursor beta subunits. EMBO J. 16: 5363-5375.
    • (1997) EMBO J. , vol.16 , pp. 5363-5375
    • Nandi, D.1    Woodward, E.2    Ginsburg, D.B.3    Monaco, J.J.4
  • 37
    • 0029163565 scopus 로고
    • Degradation of cytochrome oxidase subunits in mutants of yeast lacking cytochrome c and suppression of the degradation by mutation of yme1
    • PEARCE, D. A., and F. SHERMAN, 1995 Degradation of cytochrome oxidase subunits in mutants of yeast lacking cytochrome c and suppression of the degradation by mutation of yme1. J. Biol. Chem. 270: 20879-20882.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20879-20882
    • Pearce, D.A.1    Sherman, F.2
  • 38
    • 0031465458 scopus 로고    scopus 로고
    • Differential ubiquitin-dependen degradation of the yeast apo-cytochrome c isozymes
    • PEARCE, D. A., and F. SHERMAN, 1997 Differential ubiquitin-dependen degradation of the yeast apo-cytochrome c isozymes. J. Biol. Chem. 272: 31829-31836.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31829-31836
    • Pearce, D.A.1    Sherman, F.2
  • 39
    • 0033168382 scopus 로고    scopus 로고
    • Retrograde protein translocation: ERADication of secretory proteins in health and disease
    • PLEMPER, R. K., and D. H. WOLF, 1999 Retrograde protein translocation: ERADication of secretory proteins in health and disease. Trends Biochem. Sci. 24: 266-270.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 266-270
    • Plemper, R.K.1    Wolf, D.H.2
  • 41
    • 0032548998 scopus 로고    scopus 로고
    • Umplp is required for proper maturation of the 20S proteasome and becomes its substrate upon completion of the assembly
    • RAMOS, P. C., J. HOCKENDORFF, E. S. JOHNSON, A. VARSHAVSKY and R. J. DOHMEN, 1998 Umplp is required for proper maturation of the 20S proteasome and becomes its substrate upon completion of the assembly. Cell 92: 489-499
    • (1998) Cell , vol.92 , pp. 489-499
    • Ramos, P.C.1    Hockendorff, J.2    Johnson, E.S.3    Varshavsky, A.4    Dohmen, R.J.5
  • 42
    • 0030872409 scopus 로고    scopus 로고
    • Mitochondrial protein import. Tom40 plays a major role in targeting and translocation of preproteins by forming a specific binding site for the presequence
    • RAPAPORT, D., W. NEUPERT and R. LILL, 1997 Mitochondrial protein import. Tom40 plays a major role in targeting and translocation of preproteins by forming a specific binding site for the presequence. J. Biol. Chem. 272: 18725-18731.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18725-18731
    • Rapaport, D.1    Neupert, W.2    Lill, R.3
  • 43
    • 0028349952 scopus 로고
    • Suppression of a mitochondrial point mutation a tRNa gene can cast light on the mechanisms of 3′ end-processing
    • RINALDI, T., S. FRAMCISCI, E. SENNARO, L. FRONTALI and M. BOLOTIN-FUKUHARA, 1994 Suppression of a mitochondrial point mutation a tRNA gene can cast light on the mechanisms of 3′ end-processing. Curr. Genet. 25: 451-455.
    • (1994) Curr. Genet. , vol.25 , pp. 451-455
    • Rinaldi, T.1    Framcisci, S.2    Sennaro, E.3    Frontali, L.4    Bolotin-Fukuhara, M.5
  • 44
    • 0029053890 scopus 로고
    • A Saccharomyces cerevisiae gene essential for viability has been conserved in evolution
    • RINALDI, T., M. BOLOTIN-FUKUHARA and L. FRONTALI, 1995 A Saccharomyces cerevisiae gene essential for viability has been conserved in evolution. Gene 160: 135-136.
    • (1995) Gene , vol.160 , pp. 135-136
    • Rinaldi, T.1    Bolotin-Fukuhara, M.2    Frontali, L.3
  • 45
    • 0031709394 scopus 로고    scopus 로고
    • A mutation in a novel yeast proteasomal gene, RPN11/MPR1, produces a cell cycle arrest overreplication of nuclear and mitochondrial DNA, and an altered mitochondrial morphology
    • RINALDI, T., C. RICCI, D. PORRO, M. BOLOTIS-FUKUHARA and I., FRONTALI, 1998 A mutation in a novel yeast proteasomal gene, RPN11/MPR1, produces a cell cycle arrest overreplication of nuclear and mitochondrial DNA, and an altered mitochondrial morphology. Mol. Biol. Cell 9: 2917-2931.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 2917-2931
    • Rinaldi, T.1    Ricci, C.2    Porro, D.3    Bolotis-Fukuhara, M.4    Frontali, I.5
  • 46
    • 0023545322 scopus 로고
    • A Saccharomyces cerevisiae genomic plasmid bank based on a centromere-containing shuttle vector
    • ROSE, M. D., P. NOVICK, J. H. THOMAS, D. BOTSTEIN and G. R. FINK, 1987 A Saccharomyces cerevisiae genomic plasmid bank based on a centromere-containing shuttle vector. Gene 60: 237-243.
    • (1987) Gene , vol.60 , pp. 237-243
    • Rose, M.D.1    Novick, P.2    Thomas, J.H.3    Botstein, D.4    Fink, G.R.5
  • 47
    • 0025979877 scopus 로고
    • Targeting, disruption, replacement, and allele rescue: Integrative DNA transformation in yeast
    • ROTHSTEIN, R., 1991 Targeting, disruption, replacement, and allele rescue: integrative DNA transformation in yeast. Methods Enzymol. 194: 281-301.
    • (1991) Methods Enzymol. , vol.194 , pp. 281-301
    • Rothstein, R.1
  • 49
    • 0025978949 scopus 로고
    • Getting started with yeast
    • SHERMAN, F., 1991 Getting started with yeast. Methods Enzymol. 194: 3-21.
    • (1991) Methods Enzymol. , vol.194 , pp. 3-21
    • Sherman, F.1
  • 50
    • 0025978950 scopus 로고
    • Micromanipulation and dissection of asci
    • SHERMAN, F., and J. HICKS, 1991 Micromanipulation and dissection of asci. Methods Enzymol. 194: 21-37.
    • (1991) Methods Enzymol. , vol.194 , pp. 21-37
    • Sherman, F.1    Hicks, J.2
  • 51
    • 0026013147 scopus 로고
    • A gene required for RNase P activity in Candida (Torulopsis) grabrata mitochondria codes for a 227-nucleotide RNa with homology to bacterial RNase P RNA
    • SHU, H. H., C. A. WISE, G. D. CLARK-WALKER and N. C. MARTIN, 1991 A gene required for RNase P activity in Candida (Torulopsis) grabrata mitochondria codes for a 227-nucleotide RNA with homology to bacterial RNase P RNA. Mol. Cell. Biol. 11: 1662-1667.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 1662-1667
    • Shu, H.H.1    Wise, C.A.2    Clark-Walker, G.D.3    Martin, N.C.4
  • 52
    • 0026090063 scopus 로고
    • In vitro mutagenesis and plasmid shuflling: From cloned gene to mutant yeast
    • SIKORSKI, R. S., and J. D. BOEKI, 1991 In vitro mutagenesis and plasmid shuflling: from cloned gene to mutant yeast. Methods Enzymol. 194: 302-318.
    • (1991) Methods Enzymol. , vol.194 , pp. 302-318
    • Sikorski, R.S.1    Boeki, J.D.2
  • 53
    • 0024669291 scopus 로고
    • A system of shuttle vectors and y 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 y 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
  • 54
    • 0032897575 scopus 로고    scopus 로고
    • The dominant temperature-sensitive lethal DTS7 of Drosophila melanogaster encodes an altered 20S proteasome beta-type subunit
    • SMYTH, K. A., and J. M. BELOIE, 1999 The dominant temperature-sensitive lethal DTS7 of Drosophila melanogaster encodes an altered 20S proteasome beta-type subunit. Genetics 151: 211-220.
    • (1999) Genetics , vol.151 , pp. 211-220
    • Smyth, K.A.1    Beloie, J.M.2
  • 55
    • 0029890885 scopus 로고    scopus 로고
    • Yeast mitochondrial RNase P RNa synthesis is altered in an RNase P protein subunit mutant: Insights into the biogenesis of a mitochondrial RNA-processing enzyme
    • STRIBINSKIS, V., G. J. GAO, P. SULO, Y. L. DANG and N. C. MARTIN, 1996 Yeast mitochondrial RNase P RNA synthesis is altered in an RNase P protein subunit mutant: insights into the biogenesis of a mitochondrial RNA-processing enzyme. Mol. Cell. Biol. 16: 3429-3436.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3429-3436
    • Stribinskis, V.1    Gao, G.J.2    Sulo, P.3    Dang, Y.L.4    Martin, N.C.5
  • 56
    • 0009585097 scopus 로고    scopus 로고
    • Sperm mitochondrial ubiquitination and a model explaining the stricly maternal mtDNa inheritance in mammals
    • SUTOVSKY, P., R. MORENO and G. SCHATTEN, 1998 Sperm mitochondrial ubiquitination and a model explaining the stricly maternal mtDNA inheritance in mammals. Mol. Biol. Cell. 9: 309a.
    • (1998) Mol. Biol. Cell. , vol.9
    • Sutovsky, P.1    Moreno, R.2    Schatten, G.3
  • 57
    • 0027304446 scopus 로고
    • Inactivation of YME1, a member of the ftsH-SEC18-PASI-CDC48 family of putative ATPase-encoding genes, causes increased escape of DNa from mitochondrial in Saccharomyces cerevisiae
    • THORNESS, P. E., K. H. WHITE and T. D. FOX, 1993 Inactivation of YME1, a member of the ftsH-SEC18-PASI-CDC48 family of putative ATPase-encoding genes, causes increased escape of DNA from mitochondrial in Saccharomyces cerevisiae. Mol. Cell. Biol. 13: 5418-5426.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 5418-5426
    • Thorness, P.E.1    White, K.H.2    Fox, T.D.3
  • 58
    • 0024424988 scopus 로고
    • A 42K outer-membrane protein is a componenr of the yeast mitochondrial protein import site
    • VESTWEBER, D., J. BRUNNER, A. BAKER and G. SCHATZ, 1989 A 42K outer-membrane protein is a componenr of the yeast mitochondrial protein import site. Nature 341: 205-209.
    • (1989) Nature , vol.341 , pp. 205-209
    • Vestweber, D.1    Brunner, J.2    Baker, A.3    Schatz, G.4
  • 59
    • 0029871347 scopus 로고    scopus 로고
    • PCR-synthesis of cassettes with long flanking homology regions for gene disruptions in S. cerevisiae
    • WACH, A., 1996 PCR-synthesis of cassettes with long flanking homology regions for gene disruptions in S. cerevisiae. Yeast 12: 259-265.
    • (1996) Yeast , vol.12 , pp. 259-265
    • Wach, A.1
  • 60
    • 0028676232 scopus 로고
    • New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae
    • WACH, A., A. BRACHAT, R. POHLMAN and P. PHILIPPSEN, 1994 New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae. Yeast 10: 1793-1808.
    • (1994) Yeast , vol.10 , pp. 1793-1808
    • Wach, A.1    Brachat, A.2    Pohlman, R.3    Philippsen, P.4
  • 61
    • 0030020360 scopus 로고    scopus 로고
    • Biochemical and functional analysis of the YNE1 gene product, and ATP and zinc-dependent mitochondrial protease from S, cerevisiae
    • WEBER, E. R., T. HANKAMP and P. E. THORSNESS, 1996 Biochemical and functional analysis of the YNE1 gene product, and ATP and zinc-dependent mitochondrial protease from S, cerevisiae. Mol. Biol. Cell. 7: 307-317.
    • (1996) Mol. Biol. Cell. , vol.7 , pp. 307-317
    • Weber, E.R.1    Hankamp, T.2    Thorsness, P.E.3
  • 63
    • 0024416864 scopus 로고
    • Ubiquitin is involved in the in vitro insertion of monoamine oxidase B into mitochondrial outer membranes
    • ZHAUNG, Z. P., and R. MCCAULEY, 1989 Ubiquitin is involved in the in vitro insertion of monoamine oxidase B into mitochondrial outer membranes. J. Biol. Chem. 264: 14594-14596.
    • (1989) J. Biol. Chem. , vol.264 , pp. 14594-14596
    • Zhaung, Z.P.1    Mccauley, R.2
  • 64
    • 0029066943 scopus 로고
    • Suppression of mutations in two Saccharomyces cerevisiae genes by the adenovirus ELA protein
    • ZIELER, H. A., M. WALIBERG and P. BERG, 1995 Suppression of mutations in two Saccharomyces cerevisiae genes by the adenovirus ELA protein. Mol. Cell. Biol. 15: 3227-3237.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3227-3237
    • Zieler, H.A.1    Waliberg, M.2    Berg, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.