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Volumn 25, Issue 15, 2005, Pages 6546-6558

Rpm2p, a component of yeast mitochondrial RNase P, acts as a transcriptional activator in the nucleus

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; CHAPERONE; DNA BINDING PROTEIN; GREEN FLUORESCENT PROTEIN; HEAT SHOCK PROTEIN 10; HEAT SHOCK PROTEIN 60; HEAT SHOCK PROTEIN 60P; HYBRID PROTEIN; LEUCINE ZIPPER PROTEIN; LEXA PROTEIN; MESSENGER RNA; MITOCHONDRIAL DNA; MITOCHONDRIAL ENZYME; PROTEIN ATP2P; PROTEIN SUBUNIT; RIBONUCLEASE P; RPM2P PROTEIN; TRANSLOCASE OF OUTER MITOCHONDRIAL MEMBRANE 20; TRANSLOCASE OF OUTER MITOCHONDRIAL MEMBRANE 22; TRANSLOCASE OF OUTER MITOCHONDRIAL MEMBRANE 37; TRANSLOCASE OF OUTER MITOCHONDRIAL MEMBRANE 40; TRANSLOCASE OF OUTER MITOCHONDRIAL MEMBRANE 40 3; TRANSLOCASE OF OUTER MITOCHONDRIAL MEMBRANE 40P; TRANSLOCASE OF OUTER MITOCHONDRIAL MEMBRANE 6; TRANSLOCASE OF OUTER MITOCHONDRIAL MEMBRANE 70; UNCLASSIFIED DRUG;

EID: 22544484179     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.25.15.6546-6558.2005     Document Type: Article
Times cited : (20)

References (68)
  • 1
    • 0035901495 scopus 로고    scopus 로고
    • Mitochondria-to-nucleus stress signaling induces phenotypic changes, tumor progression and cell invasion
    • Amuthan, G., G. Biswas, S.-Y. Zhang, A. Klein-Szanto, C. Vijayasarathy, and N. Avadhani. 2001. Mitochondria-to-nucleus stress signaling induces phenotypic changes, tumor progression and cell invasion. EMBO J. 20:1910-1920.
    • (2001) EMBO J. , vol.20 , pp. 1910-1920
    • Amuthan, G.1    Biswas, G.2    Zhang, S.-Y.3    Klein-Szanto, A.4    Vijayasarathy, C.5    Avadhani, N.6
  • 2
    • 0025597095 scopus 로고
    • A yeast mitochondrial outer membrane protein essential for protein import and cell viability
    • Baker, K. P., A. Schaniel, D. Vestweber, and G. Schatz. 1990. A yeast mitochondrial outer membrane protein essential for protein import and cell viability. Nature 348:605-609.
    • (1990) Nature , vol.348 , pp. 605-609
    • Baker, K.P.1    Schaniel, A.2    Vestweber, D.3    Schatz, G.4
  • 3
    • 0037041022 scopus 로고    scopus 로고
    • Role of the Ada2 and Ada3 transcriptional coactivators in histone acetylation
    • Balasubramanian, R., M. G. Pray-Grant, W. Selleck, P. A. Grant, and S. Tan. 2002. Role of the Ada2 and Ada3 transcriptional coactivators in histone acetylation. J. Biol. Chem. 277:7989-7995.
    • (2002) J. Biol. Chem. , vol.277 , pp. 7989-7995
    • Balasubramanian, R.1    Pray-Grant, M.G.2    Selleck, W.3    Grant, P.A.4    Tan, S.5
  • 5
    • 0028866991 scopus 로고
    • Prediction and identification of new natural substrates of the yeast mitochondrial intermediate peptidase
    • Branda, S. S., and G. Isaya. 1995. Prediction and identification of new natural substrates of the yeast mitochondrial intermediate peptidase. J. Biol. Chem. 270:27366-27373.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27366-27373
    • Branda, S.S.1    Isaya, G.2
  • 6
    • 0027425117 scopus 로고
    • Characterization of NGG1, a novel yeast gene required for glucose repression of GAL4p-regulated transcription
    • Brandl, C. J., A. M. Furlanetto, J. A. Martens, and K. S. Hamilton. 1993. Characterization of NGG1, a novel yeast gene required for glucose repression of GAL4p-regulated transcription. EMBO J. 12:5255-5265.
    • (1993) EMBO J. , vol.12 , pp. 5255-5265
    • Brandl, C.J.1    Furlanetto, A.M.2    Martens, J.A.3    Hamilton, K.S.4
  • 7
    • 33044488547 scopus 로고    scopus 로고
    • Ph.D. thesis. University of Louisville, Louisville, Ky.
    • Bristow, M. J., Jr. 2001. Ph.D. thesis. University of Louisville, Louisville, Ky.
    • (2001)
    • Bristow Jr., M.J.1
  • 8
    • 0029984469 scopus 로고    scopus 로고
    • Tetrahymena histone acetyltransferase A: A homolog to yeast Gcn5p linking histone acetylation to gene activation
    • Brownell, J. E., J. Zhou, T. Ranalli, R. Kobayashi, D. G. Edmondson, S. Y. Roth, and C. D. Allis. 1996. Tetrahymena histone acetyltransferase A: a homolog to yeast Gcn5p linking histone acetylation to gene activation. Cell 84:843-851.
    • (1996) Cell , vol.84 , pp. 843-851
    • Brownell, J.E.1    Zhou, J.2    Ranalli, T.3    Kobayashi, R.4    Edmondson, D.G.5    Roth, S.Y.6    Allis, C.D.7
  • 9
    • 1042278175 scopus 로고    scopus 로고
    • Intracellular interleukin-1α functionally interacts with histone acetyltransferase complexes
    • Buryskova, M., M. Pospisek, A. Grothney, T. Simmet, and L. Burysek. 2004. Intracellular interleukin-1α functionally interacts with histone acetyltransferase complexes. J. Biol. Chem. 279:4017-4026.
    • (2004) J. Biol. Chem. , vol.279 , pp. 4017-4026
    • Buryskova, M.1    Pospisek, M.2    Grothney, A.3    Simmet, T.4    Burysek, L.5
  • 10
    • 1842665662 scopus 로고    scopus 로고
    • Mitochondrial signaling: The retrograde response
    • Butow, R. A., and N. G. Avadhani. 2004. Mitochondrial signaling: the retrograde response. Mol. Cell 14:1-15.
    • (2004) Mol. Cell , vol.14 , pp. 1-15
    • Butow, R.A.1    Avadhani, N.G.2
  • 11
    • 0035968254 scopus 로고    scopus 로고
    • 54 hybrid protein that functions as a potent activator of RNA polymerase II transcription in yeast
    • 54 hybrid protein that functions as a potent activator of RNA polymerase II transcription in yeast. J. Biol. Chem. 276:23881-23887.
    • (2001) J. Biol. Chem. , vol.276 , pp. 23881-23887
    • Chen, B.-S.1    Sun, Z.-W.2    Hampsey, M.3
  • 12
    • 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
  • 13
    • 0033371431 scopus 로고    scopus 로고
    • 1-ATPase are required for survival of petite mutants in Saccharomyces cerevisiae
    • 1-ATPase are required for survival of petite mutants in Saccharomyces cerevisiae. Mol. Gen. Genet. 262:898-908.
    • (1999) Mol. Gen. Genet. , vol.262 , pp. 898-908
    • Chen, X.J.1    Clark-Walker, G.D.2
  • 14
    • 0032849910 scopus 로고    scopus 로고
    • The petite mutation in yeast: 50 Years on
    • Chen, X. J., and G. D. Clark-Walker. 1999. The petite mutation in yeast: 50 years on. Int. Rev. Cytol. 194:197-238.
    • (1999) Int. Rev. Cytol. , vol.194 , pp. 197-238
    • Chen, X.J.1    Clark-Walker, G.D.2
  • 16
    • 0029051043 scopus 로고
    • RTG genes in yeast in communication between mitochondria and the nucleus are also required for expression of genes encoding peroxisomal proteins
    • Chielstowska, A., and R. A. Butow. 1995. RTG genes in yeast in communication between mitochondria and the nucleus are also required for expression of genes encoding peroxisomal proteins. J. Biol. Chem. 270:18141-18146.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18141-18146
    • Chielstowska, A.1    Butow, R.A.2
  • 17
    • 0034122608 scopus 로고    scopus 로고
    • Maintenance and integrity of the mitochondrial genome: A plethora of nuclear genes in the budding yeast
    • Contamine, V., and M. Picard. 2000. Maintenance and integrity of the mitochondrial genome: a plethora of nuclear genes in the budding yeast. Microbiol. Mol. Biol. Rev. 64:281-313.
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 281-313
    • Contamine, V.1    Picard, M.2
  • 18
    • 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
  • 19
    • 0037181472 scopus 로고    scopus 로고
    • Genome-wide studies on the nuclear PDR3-controlled response to mitochondrial dysfunction in yeast
    • Devaux, F., E. Carvajal, S. Moye-Rowley, and C. Jacq. 2001. Genome-wide studies on the nuclear PDR3-controlled response to mitochondrial dysfunction in yeast. FEBS Lett. 515:25-28.
    • (2001) FEBS Lett. , vol.515 , pp. 25-28
    • Devaux, F.1    Carvajal, E.2    Moye-Rowley, S.3    Jacq, C.4
  • 20
    • 0141455113 scopus 로고    scopus 로고
    • Suppression of a defect in mitochondrial protein import identifies cytosolic proteins for viability of yeast cells lacking mitochondrial DNA
    • Dunn, C. D., and R. E. Jensen. 2003. Suppression of a defect in mitochondrial protein import identifies cytosolic proteins for viability of yeast cells lacking mitochondrial DNA. Genetics 165:35-45.
    • (2003) Genetics , vol.165 , pp. 35-45
    • Dunn, C.D.1    Jensen, R.E.2
  • 23
    • 0032518643 scopus 로고    scopus 로고
    • Kluyveromyces lactis SEF1 and Saccharomyces cerevisiae homologue bypass the unknown essential function, but not the mitochondrial RNase P function, of the 5. cerevisiae RPM2 gene
    • Groom, K. R., H. C. Heyman, M. C. Steffen, L. Hawkins, and N. C. Martin. 1998. Kluyveromyces lactis SEF1 and Saccharomyces cerevisiae homologue bypass the unknown essential function, but not the mitochondrial RNase P function, of the 5. 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
  • 24
    • 0034534975 scopus 로고    scopus 로고
    • Multiple signals from dysfunctional mitochondria activate the pleiotropic drug resistance pathway in Saccharomyces cerevisiae
    • Hallstrom, T. C., and W. S. Moye-Rowley. 2000. Multiple signals from dysfunctional mitochondria activate the pleiotropic drug resistance pathway in Saccharomyces cerevisiae. J. Biol. Chem. 275:37347-37356.
    • (2000) J. Biol. Chem. , vol.275 , pp. 37347-37356
    • Hallstrom, T.C.1    Moye-Rowley, W.S.2
  • 25
    • 0022981167 scopus 로고
    • Saturation mutagenesis of the yeast his3 regulatory site: Requirements for transcriptional induction and for binding by GCN4 activator protein
    • Hill, D. E., I. A. Hope, J. P. Macke, and K. Struhl. 1986. Saturation mutagenesis of the yeast his3 regulatory site: requirements for transcriptional induction and for binding by GCN4 activator protein. Science 234:451-457.
    • (1986) Science , vol.234 , pp. 451-457
    • Hill, D.E.1    Hope, I.A.2    Macke, J.P.3    Struhl, K.4
  • 26
    • 0029018708 scopus 로고
    • Identification of a new family of tissue-specific basic helix-loop-helix proteins with two-hybrid system
    • Hollenberg, S. M., R. Sternglanz, P. F. Cheng, and H. Weintraub. 1995. Identification of a new family of tissue-specific basic helix-loop-helix proteins with two-hybrid system. Mol. Cell. Biol. 15:3813-3822.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3813-3822
    • Hollenberg, S.M.1    Sternglanz, R.2    Cheng, P.F.3    Weintraub, H.4
  • 27
    • 0022623266 scopus 로고
    • RNase P activity in the mitochondria of Saccharomyces cerevisiae depends on both mitochondrial and nucleus-encoded components
    • Hollingsworth, M. J., and N. C. Martin. 1986. RNase P activity in the mitochondria of Saccharomyces cerevisiae depends on both mitochondrial and nucleus-encoded components. Mol. Cell. Biol. 6:1058-1064.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 1058-1064
    • Hollingsworth, M.J.1    Martin, N.C.2
  • 29
    • 0031027203 scopus 로고    scopus 로고
    • A basic helix-loop-helix zipper transcription complex functions in a signaling pathway from mitochondria to the nucleus
    • Jia, Y., B. Rothermel, J. Thornton, and R. A. Butow. 1997. A basic helix-loop-helix zipper transcription complex functions in a signaling pathway from mitochondria to the nucleus. Mol. Cell. Biol. 17:1110-1117.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1110-1117
    • Jia, Y.1    Rothermel, B.2    Thornton, J.3    Butow, R.A.4
  • 31
    • 0027186299 scopus 로고
    • Genetic and biochemical characterization of ISP6, a small mitochondrial outer membrane protein associated with the protein translocation complex
    • Kassenbrock, C. K., W. Cao, and M. G. Douglas. 1993. Genetic and biochemical characterization of ISP6, a small mitochondrial outer membrane protein associated with the protein translocation complex. EMBO J. 12: 3023-3034.
    • (1993) EMBO J. , vol.12 , pp. 3023-3034
    • Kassenbrock, C.K.1    Cao, W.2    Douglas, M.G.3
  • 32
    • 0029129982 scopus 로고
    • RPM2, independently of its mitochondrial RNase P function, suppresses an ISP42 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, and N. C. Martin. 1995. RPM2, independently of its mitochondrial RNase P function, suppresses an ISP42 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    Martin, N.C.6
  • 33
    • 0033963688 scopus 로고    scopus 로고
    • Tim18p is a new component of the Tim54-Tim22p translocon in the mitochondrial inner membrane
    • Kerscher, O., N. B. Sepuri, and R. E. Jensen. 2000. Tim18p is a new component of the Tim54-Tim22p translocon in the mitochondrial inner membrane. Mol. Biol. Cell 11:103-116.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 103-116
    • Kerscher, O.1    Sepuri, N.B.2    Jensen, R.E.3
  • 34
    • 0026087180 scopus 로고
    • Preparation of high molecular weight RNA
    • Kohrer, K., and H. Domdey. 1991. Preparation of high molecular weight RNA. Methods Enzymol. 194:398-405.
    • (1991) Methods Enzymol. , vol.194 , pp. 398-405
    • Kohrer, K.1    Domdey, H.2
  • 35
    • 0036964091 scopus 로고    scopus 로고
    • Genetic and biochemical basis for viability of yeast lacking mitochondrial genomes
    • Kominsky, D. J., M. P. Brownson, D. L. Updike, and P. E. Thorsness. 2002. Genetic and biochemical basis for viability of yeast lacking mitochondrial genomes. Genetics 162:1595-1604.
    • (2002) Genetics , vol.162 , pp. 1595-1604
    • Kominsky, D.J.1    Brownson, M.P.2    Updike, D.L.3    Thorsness, P.E.4
  • 36
    • 0014214363 scopus 로고
    • Biochemical genetics of oxidative phosphorylation
    • Kováč, L., L. M. Lachowicz, and P. Slonimski. 1980. Biochemical genetics of oxidative phosphorylation. Science 158:1564-1567.
    • (1980) Science , vol.158 , pp. 1564-1567
    • Kováč, L.1    Lachowicz, L.M.2    Slonimski, P.3
  • 37
    • 0037341660 scopus 로고    scopus 로고
    • F1-catalysed ATP hydrolysis is required for mitochondrial biogenesis in Saccharomyces cerevisiae growing under conditions where it cannot respire
    • Lefebvre-Balguerie, A., S. Duvezin-Caubet, M. F. Giraud, P. P. Slonimski, and J. P. Di Rago. 2003. F1-catalysed ATP hydrolysis is required for mitochondrial biogenesis in Saccharomyces cerevisiae growing under conditions where it cannot respire. Mol. Microbiol. 47:1329-1339.
    • (2003) Mol. Microbiol. , vol.47 , pp. 1329-1339
    • Lefebvre-Balguerie, A.1    Duvezin-Caubet, S.2    Giraud, M.F.3    Slonimski, P.P.4    Di Rago, J.P.5
  • 38
    • 0027524176 scopus 로고
    • RTG1 and RTG2: Two yeast genes required for a novel path of communication from mitochondria to the nucleus
    • Liao, X., and R. A. Butow. 1993. RTG1 and RTG2: two yeast genes required for a novel path of communication from mitochondria to the nucleus. Cell 72:61-71.
    • (1993) Cell , vol.72 , pp. 61-71
    • Liao, X.1    Butow, R.A.2
  • 39
    • 0035799352 scopus 로고    scopus 로고
    • Combined and individual mitochondrial HSP60 and HSP10 expression in cardiac myocytes protects mitochondrial function and prevents apoptotic death induced by stimulated ischemia-reoxygenation
    • Lin, K. M., B. Lin, I. Y. Lian, R. Mestril, I. E. Scheffler, and W. H. Dillmann. 2001. Combined and individual mitochondrial HSP60 and HSP10 expression in cardiac myocytes protects mitochondrial function and prevents apoptotic death induced by stimulated ischemia-reoxygenation. Circulation 103:1787-1792.
    • (2001) Circulation , vol.103 , pp. 1787-1792
    • Lin, K.M.1    Lin, B.2    Lian, I.Y.3    Mestril, R.4    Scheffler, I.E.5    Dillmann, W.H.6
  • 40
    • 0032873464 scopus 로고    scopus 로고
    • A transcriptional switch in the expression of yeast tricarboxylic acid cycle genes in response to a reduction or loss of respiratory function
    • Liu, Z., and R. A. Butow. 1999. A transcriptional switch in the expression of yeast tricarboxylic acid cycle genes in response to a reduction or loss of respiratory function. Mol. Cell. Biol. 19:6720-6728.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 6720-6728
    • Liu, Z.1    Butow, R.A.2
  • 41
    • 0034006634 scopus 로고    scopus 로고
    • Proteasome mutants, pre4-2 and ump1-2, suppress the essential function but not the mitochondrial RNase P function of the Saccharomyces cerevisiae gene RPM2
    • Lutz, M. S., S. R. Ellis, and N. C. Martin. 2000. Proteasome mutants, pre4-2 and ump1-2, suppress the essential function but not the mitochondrial RNase P function of the Saccharomyces cerevisiae gene RPM2. Genetics 154:1013-1023.
    • (2000) Genetics , vol.154 , pp. 1013-1023
    • Lutz, M.S.1    Ellis, S.R.2    Martin, N.C.3
  • 42
    • 0030037585 scopus 로고    scopus 로고
    • Transcriptional activation by yeast Pdr1p is inhibited by its association with Ngg1/Ada3p
    • Martens, J. A., J. Genereaux, A. Saleh, and C. J. Brandi. 1996. Transcriptional activation by yeast Pdr1p is inhibited by its association with Ngg1/Ada3p. J. Biol. Chem. 271:15884-15890.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15884-15890
    • Martens, J.A.1    Genereaux, J.2    Saleh, A.3    Brandi, C.J.4
  • 44
    • 0022110054 scopus 로고
    • Mitochondrial protein synthesis is required for maintenance of intact mitochondrial genomes in Saccharomyces cerevisiae
    • Meyers, 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
    • Meyers, A.M.1    Pape, L.K.2    Tzagoloff, A.3
  • 46
    • 0030969942 scopus 로고    scopus 로고
    • Protein import into mitochondria
    • Neupert, W. 1997. Protein import into mitochondria. Annu. Rev. Biochem. 66:863-917.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 863-917
    • Neupert, W.1
  • 47
    • 0023106633 scopus 로고
    • The mitochondrial genotype can influence nuclear gene expression in yeast
    • Parikh, V. S., M. M. Morgan, R. Scott, L. S. Clements, and R. A. Butow. 1987. The mitochondrial genotype can influence nuclear gene expression in yeast. Science 235:576-580.
    • (1987) Science , vol.235 , pp. 576-580
    • Parikh, V.S.1    Morgan, M.M.2    Scott, R.3    Clements, L.S.4    Butow, R.A.5
  • 49
    • 0030910776 scopus 로고    scopus 로고
    • The Tom and Tim machine
    • Pfanner, N., and M. Meijer. 1997. The Tom and Tim machine. Curr. Biol. 7:100-103.
    • (1997) Curr. Biol. , vol.7 , pp. 100-103
    • Pfanner, N.1    Meijer, M.2
  • 50
    • 0027423613 scopus 로고
    • ADAS: A gene, identifies by resistance to GAL4-VP16, with properties similar to and different from those of ADA2
    • Pina, B., S. Berger, G. A. Marcus, N. Silverman, J. Agapite, and L. Guarente. 1993. ADAS: a gene, identifies by resistance to GAL4-VP16, with properties similar to and different from those of ADA2. Mol. Cell. Biol. 13:5981-5989.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 5981-5989
    • Pina, B.1    Berger, S.2    Marcus, G.A.3    Silverman, N.4    Agapite, J.5    Guarente, L.6
  • 51
    • 0029894544 scopus 로고    scopus 로고
    • Crosstalk between nuclear and mitochondrial genomes
    • Poyton, R. O., and J. E. McEwen. 1996. Crosstalk between nuclear and mitochondrial genomes. Annu. Rev. Biochem. 65:563-607.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 563-607
    • Poyton, R.O.1    McEwen, J.E.2
  • 52
    • 0034723175 scopus 로고    scopus 로고
    • Mitochondrial activity is involved in the regulation of myoblast differentiation through myogenin expression and activity of myogenic factors
    • Rochard, P., A. Rodier, F. Casas, I. Cassar-Malek, S. Marchal-Victorion, L. Daury, C. Wrutniak, and G. Cabello. 2000. Mitochondrial activity is involved in the regulation of myoblast differentiation through myogenin expression and activity of myogenic factors. J. Biol. Chem. 275:2733-2744.
    • (2000) J. Biol. Chem. , vol.275 , pp. 2733-2744
    • Rochard, P.1    Rodier, A.2    Casas, F.3    Cassar-Malek, I.4    Marchal-Victorion, S.5    Daury, L.6    Wrutniak, C.7    Cabello, G.8
  • 53
    • 0030839873 scopus 로고    scopus 로고
    • Rtg3p, a basic helix-loop-helix protein that functions in mitochondrial-induced changes in gene expression, contains independent activation domains
    • Rothermel, B. A., J. Thornton, and R. A. Butow. 1997. Rtg3p, a basic helix-loop-helix protein that functions in mitochondrial-induced changes in gene expression, contains independent activation domains. J. Biol. Chem. 272: 19801-19807.
    • (1997) J. Biol. Chem. , vol.272 , pp. 19801-19807
    • Rothermel, B.A.1    Thornton, J.2    Butow, R.A.3
  • 54
    • 0031052033 scopus 로고    scopus 로고
    • Identification of native complexes containing the yeast coactivator/repressor proteins NGG1/ADA3 and ADA2
    • Saleh, A., V. Lang, R. Cook, and C. J. Brandi. 1997. Identification of native complexes containing the yeast coactivator/repressor proteins NGG1/ADA3 and ADA2. J. Biol. Chem. 272:5571-5578.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5571-5578
    • Saleh, A.1    Lang, V.2    Cook, R.3    Brandi, C.J.4
  • 56
    • 0034046342 scopus 로고    scopus 로고
    • Mitochondria-to-nucleus signaling is regulated by the subcellular localization of the transcription factors Rtg1p and Rtg3p
    • Sekito, T., J. Thornton, and R. A. Butow. 2000. Mitochondria-to-nucleus signaling is regulated by the subcellular localization of the transcription factors Rtg1p and Rtg3p. Mol. Biol. Cell 11:2103-2115.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2103-2115
    • Sekito, T.1    Thornton, J.2    Butow, R.A.3
  • 57
    • 0346882887 scopus 로고    scopus 로고
    • Transcription of TIM9, a new factor required for the petite-positive phenotype of Saccharomyces cerevisiae, is defective in spt7 mutants
    • Senapin, S., X. J. Chen, and G. D. Clark-Walker. 2003. Transcription of TIM9, a new factor required for the petite-positive phenotype of Saccharomyces cerevisiae, is defective in spt7 mutants. Curr. Genet. 44: 202-210.
    • (2003) Curr. Genet. , vol.44 , pp. 202-210
    • Senapin, S.1    Chen, X.J.2    Clark-Walker, G.D.3
  • 58
    • 0042330503 scopus 로고    scopus 로고
    • Hsp10 and Hsp60 modulate Bcl-2 family and mitochondria apoptosis signaling induced by doxorubicin in cardiac muscle cells
    • Shan, Y.-X., T.-J. Liu, H.-F. Su, A. Samsamshariat, R. Mestril, and P. H. Wang. 2003. Hsp10 and Hsp60 modulate Bcl-2 family and mitochondria apoptosis signaling induced by doxorubicin in cardiac muscle cells. J. Mol. Cell. Cardiol. 35:1135-1143.
    • (2003) J. Mol. Cell. Cardiol. , vol.35 , pp. 1135-1143
    • Shan, Y.-X.1    Liu, T.-J.2    Su, H.-F.3    Samsamshariat, A.4    Mestril, R.5    Wang, P.H.6
  • 59
    • 0037163029 scopus 로고    scopus 로고
    • The adenovirus E1A protein targets the SAGA but not the ADA transcriptional regulatory complex through multiple independent domains
    • Shuen, M., N. Avvakumov, P. G. Walfish, C. J. Brandl, and J. S. Mymryk. 2002. The adenovirus E1A protein targets the SAGA but not the ADA transcriptional regulatory complex through multiple independent domains. J. Biol. Chem. 277:30844-30851.
    • (2002) J. Biol. Chem. , vol.277 , pp. 30844-30851
    • Shuen, M.1    Avvakumov, N.2    Walfish, P.G.3    Brandl, C.J.4    Mymryk, J.S.5
  • 60
    • 0026090063 scopus 로고
    • In vitro mutagenesis and plasmid shuffling: From cloned gene to mutant yeast
    • Sikorski, R. S., and J. D. Boeke. 1991. In vitro mutagenesis and plasmid shuffling: from cloned gene to mutant yeast. Methods Enzymol. 194:302-318.
    • (1991) Methods Enzymol. , vol.194 , pp. 302-318
    • Sikorski, R.S.1    Boeke, J.D.2
  • 61
    • 0034051227 scopus 로고    scopus 로고
    • Acetylation of histones and transcription-related factors
    • Sterner, D. E., and S. L. Berger. 2000. Acetylation of histones and transcription-related factors. Microbiol. Mol. Biol. Rev. 64:435-459.
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 435-459
    • Sterner, D.E.1    Berger, S.L.2
  • 62
    • 0029890885 scopus 로고    scopus 로고
    • Yeast mitochondrial RNase P RNA synthesis is altered in an RNase P protein subunit: 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: 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
  • 63
    • 0035445925 scopus 로고    scopus 로고
    • Rpm2p: Separate domains promote tRNA and Rpm1r maturation in Saccharomyces cerevisiae mitochondria
    • Stribinskis, V., G.-J. Gao, P. Sulo, S. R. Ellis, and N. C. Martin. 2001. Rpm2p: separate domains promote tRNA and Rpm1r maturation in Saccharomyces cerevisiae mitochondria. Nucleic Acids Res. 29:3631-3637.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 3631-3637
    • Stribinskis, V.1    Gao, G.-J.2    Sulo, P.3    Ellis, S.R.4    Martin, N.C.5
  • 64
    • 0034976294 scopus 로고    scopus 로고
    • Rpm2p, the protein subunit of mitochondrial RNase P in Saccharomyces cerevisiae, also has a role in the translation of mitochondrially encoded subunits of cytochrome c oxidase
    • Stribinskis, V., G.-J. Gao, S. R. Ellis, and N. C. Martin. 2001. Rpm2p, the protein subunit of mitochondrial RNase P in Saccharomyces cerevisiae, also has a role in the translation of mitochondrially encoded subunits of cytochrome c oxidase. Genetics 158:573-585.
    • (2001) Genetics , vol.158 , pp. 573-585
    • Stribinskis, V.1    Gao, G.-J.2    Ellis, S.R.3    Martin, N.C.4
  • 65
    • 0016227958 scopus 로고
    • A nuclear mutant of S. cerevisiae non-tolerating the cytoplasmic petite mutation
    • Subik, J. 1974. A nuclear mutant of S. cerevisiae non-tolerating the cytoplasmic petite mutation. FEBS Lett. 42:309-312.
    • (1974) FEBS Lett. , vol.42 , pp. 309-312
    • Subik, J.1
  • 66
    • 0035830867 scopus 로고    scopus 로고
    • Interorganellar communication. Altered nuclear gene expression profiles in a yeast mitochondrial DNA mutant
    • Traven, A., J. M. S. Wong, D. Xu, M. Sopta, and J. C. Ingles. 2001. Interorganellar communication. Altered nuclear gene expression profiles in a yeast mitochondrial DNA mutant. J. Biol. Chem. 276:4020-4027.
    • (2001) J. Biol. Chem. , vol.276 , pp. 4020-4027
    • Traven, A.1    Wong, J.M.S.2    Xu, D.3    Sopta, M.4    Ingles, J.C.5
  • 68
    • 0029006505 scopus 로고
    • Mutations in the mitochondrial ATP synthase gamma subunit suppress a slow-growth phenotype of yme1 yeast lacking mitochondrial DNA
    • Weber, E. R., R. S. Rooks, K. S. Shafer, J. W. Chase, and P. E. Thorsness. 1995. Mutations in the mitochondrial ATP synthase gamma subunit suppress a slow-growth phenotype of yme1 yeast lacking mitochondrial DNA. Genetics 140:435-442.
    • (1995) Genetics , vol.140 , pp. 435-442
    • Weber, E.R.1    Rooks, R.S.2    Shafer, K.S.3    Chase, J.W.4    Thorsness, P.E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.