메뉴 건너뛰기




Volumn 22, Issue 3, 2006, Pages 329-338

Mitochondrial Transcription Is Regulated via an ATP "Sensing" Mechanism that Couples RNA Abundance to Respiration

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; RNA;

EID: 33646163885     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2006.03.031     Document Type: Article
Times cited : (83)

References (67)
  • 1
    • 0033525527 scopus 로고    scopus 로고
    • Mitochondrial gene expression is regulated at the level of transcription during early embryogenesis of Xenopus laevis
    • Ammini C.V., and Hauswirth W.W. Mitochondrial gene expression is regulated at the level of transcription during early embryogenesis of Xenopus laevis. J. Biol. Chem. 274 (1999) 6265-6271
    • (1999) J. Biol. Chem. , vol.274 , pp. 6265-6271
    • Ammini, C.V.1    Hauswirth, W.W.2
  • 3
    • 0033609502 scopus 로고    scopus 로고
    • Nucleotide sequences surrounding the nonanucleotide promoter motif influence the activity of yeast mitochondrial promoter
    • Biswas T.K. Nucleotide sequences surrounding the nonanucleotide promoter motif influence the activity of yeast mitochondrial promoter. Biochemistry 38 (1999) 9693-9703
    • (1999) Biochemistry , vol.38 , pp. 9693-9703
    • Biswas, T.K.1
  • 4
    • 0022541796 scopus 로고
    • Nucleotides flanking the promoter sequence influence the transcription of the yeast mitochondrial gene coding for ATPase subunit 9
    • Biswas T.K., and Getz G.S. Nucleotides flanking the promoter sequence influence the transcription of the yeast mitochondrial gene coding for ATPase subunit 9. Proc. Natl. Acad. Sci. USA 83 (1986) 270-274
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 270-274
    • Biswas, T.K.1    Getz, G.S.2
  • 5
    • 0025027687 scopus 로고
    • Regulation of transcriptional initiation in yeast mitochondria
    • Biswas T.K., and Getz G.S. Regulation of transcriptional initiation in yeast mitochondria. J. Biol. Chem. 265 (1990) 19053-19059
    • (1990) J. Biol. Chem. , vol.265 , pp. 19053-19059
    • Biswas, T.K.1    Getz, G.S.2
  • 6
    • 0023645707 scopus 로고
    • In vitro characterization of the yeast mitochondrial promoter using single-base substitution mutants
    • Biswas T.K., Ticho B., and Getz G.S. In vitro characterization of the yeast mitochondrial promoter using single-base substitution mutants. J. Biol. Chem. 262 (1987) 13690-13696
    • (1987) J. Biol. Chem. , vol.262 , pp. 13690-13696
    • Biswas, T.K.1    Ticho, B.2    Getz, G.S.3
  • 8
    • 0033118209 scopus 로고    scopus 로고
    • Glucose repression in yeast
    • Carlson M. Glucose repression in yeast. Curr. Opin. Microbiol. 2 (1999) 202-207
    • (1999) Curr. Opin. Microbiol. , vol.2 , pp. 202-207
    • Carlson, M.1
  • 10
    • 0030813608 scopus 로고    scopus 로고
    • Identification of three regions essential for interaction between a sigma-like factor and core RNA polymerase
    • Cliften P.F., Park J.Y., Davis B.P., Jang S.-H., and Jaehning J.A. Identification of three regions essential for interaction between a sigma-like factor and core RNA polymerase. Genes Dev. 11 (1997) 2897-2909
    • (1997) Genes Dev. , vol.11 , pp. 2897-2909
    • Cliften, P.F.1    Park, J.Y.2    Davis, B.P.3    Jang, S.-H.4    Jaehning, J.A.5
  • 12
    • 0028206309 scopus 로고
    • Regulation of mitochondrial gene expression in Saccharomyces cerevisiae
    • Dieckmann C.L., and Staples R.R. Regulation of mitochondrial gene expression in Saccharomyces cerevisiae. Int. Rev. Cytol. 152 (1994) 145-181
    • (1994) Int. Rev. Cytol. , vol.152 , pp. 145-181
    • Dieckmann, C.L.1    Staples, R.R.2
  • 14
    • 0031443321 scopus 로고    scopus 로고
    • Transcription regulation by initiating NTP concentration: rRNA synthesis in bacteria
    • Gaal T., Bartlett M.S., Ross W., Turnbough C.L., and Gourse R.L. Transcription regulation by initiating NTP concentration: rRNA synthesis in bacteria. Science 278 (1997) 2092-2097
    • (1997) Science , vol.278 , pp. 2092-2097
    • Gaal, T.1    Bartlett, M.S.2    Ross, W.3    Turnbough, C.L.4    Gourse, R.L.5
  • 15
    • 0023259258 scopus 로고
    • Markedly different ATP requirements for rRNA synthesis and mtDNA light strand transcription versus mRNA synthesis in isolated human mitochondria
    • Gaines G., Rossi C., and Attardi G. Markedly different ATP requirements for rRNA synthesis and mtDNA light strand transcription versus mRNA synthesis in isolated human mitochondria. J. Biol. Chem. 262 (1987) 1907-1915
    • (1987) J. Biol. Chem. , vol.262 , pp. 1907-1915
    • Gaines, G.1    Rossi, C.2    Attardi, G.3
  • 16
    • 0025113386 scopus 로고
    • Structure-function studies of adenine nucleotide transport in mitochondria. II. Biochemical analysis of distinct AAC1 and AAC2 proteins in yeast
    • Gawaz M., Douglas M.G., and Klingenberg M. Structure-function studies of adenine nucleotide transport in mitochondria. II. Biochemical analysis of distinct AAC1 and AAC2 proteins in yeast. J. Biol. Chem. 265 (1990) 14202-14208
    • (1990) J. Biol. Chem. , vol.265 , pp. 14202-14208
    • Gawaz, M.1    Douglas, M.G.2    Klingenberg, M.3
  • 17
    • 0030267512 scopus 로고    scopus 로고
    • Purification and characterization of the reconstitutively active adenine nucleotide carrier from maize mitochondria
    • Genchi G., Ponzone C., Bisaccia F., De Santis A., Stefanizzi L., and Palmieri F. Purification and characterization of the reconstitutively active adenine nucleotide carrier from maize mitochondria. Plant Physiol. 112 (1996) 845-851
    • (1996) Plant Physiol. , vol.112 , pp. 845-851
    • Genchi, G.1    Ponzone, C.2    Bisaccia, F.3    De Santis, A.4    Stefanizzi, L.5    Palmieri, F.6
  • 18
    • 0031011211 scopus 로고    scopus 로고
    • A mouse model for mitochondrial myopathy and cardiomyopathy resulting from a deficiency in the heart/muscle isoform of the adenine nucleotide translocator
    • Graham B.H., Waymire K.G., Cottrell B., Trounce I.A., MacGregor G.R., and Wallace D.C. A mouse model for mitochondrial myopathy and cardiomyopathy resulting from a deficiency in the heart/muscle isoform of the adenine nucleotide translocator. Nat. Genet. 16 (1997) 226-234
    • (1997) Nat. Genet. , vol.16 , pp. 226-234
    • Graham, B.H.1    Waymire, K.G.2    Cottrell, B.3    Trounce, I.A.4    MacGregor, G.R.5    Wallace, D.C.6
  • 19
    • 2942563996 scopus 로고    scopus 로고
    • Dual functional roles of ATP in the human mitochondrial malic enzyme
    • Hsu W.C., Hung H.C., Tong L., and Chang G.G. Dual functional roles of ATP in the human mitochondrial malic enzyme. Biochemistry 43 (2004) 7382-7390
    • (2004) Biochemistry , vol.43 , pp. 7382-7390
    • Hsu, W.C.1    Hung, H.C.2    Tong, L.3    Chang, G.G.4
  • 20
    • 0032732424 scopus 로고    scopus 로고
    • Mechanisms by which T7 lysozyme specifically regulates T7 RNA polymerase during different phases of transcription
    • Huang J., Villemain J., Padilla R., and Sousa R. Mechanisms by which T7 lysozyme specifically regulates T7 RNA polymerase during different phases of transcription. J. Mol. Biol. 293 (1999) 457-475
    • (1999) J. Mol. Biol. , vol.293 , pp. 457-475
    • Huang, J.1    Villemain, J.2    Padilla, R.3    Sousa, R.4
  • 21
    • 0001210090 scopus 로고
    • Interactions of the RNA polymerase of bacteriophage T7 with its promoter during binding and initiation of transcription
    • Ikeda R.A., and Richardson C.C. Interactions of the RNA polymerase of bacteriophage T7 with its promoter during binding and initiation of transcription. Proc. Natl. Acad. Sci. USA 83 (1986) 3614-3618
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 3614-3618
    • Ikeda, R.A.1    Richardson, C.C.2
  • 22
    • 0038168520 scopus 로고    scopus 로고
    • Reconstitution of recombinant uncoupling proteins: UCP1, -2, and -3 have similar affinities for ATP and are unaffected by coenzyme Q10
    • Jaburek M., and Garlid K.D. Reconstitution of recombinant uncoupling proteins: UCP1, -2, and -3 have similar affinities for ATP and are unaffected by coenzyme Q10. J. Biol. Chem. 278 (2003) 25825-25831
    • (2003) J. Biol. Chem. , vol.278 , pp. 25825-25831
    • Jaburek, M.1    Garlid, K.D.2
  • 23
    • 0025876118 scopus 로고
    • The yeast mitochondrial RNA polymerase specificity factor, MTF1, is similar to bacterial sigma factors
    • Jang S.-H., and Jaehning J.A. The yeast mitochondrial RNA polymerase specificity factor, MTF1, is similar to bacterial sigma factors. J. Biol. Chem. 266 (1991) 22671-22677
    • (1991) J. Biol. Chem. , vol.266 , pp. 22671-22677
    • Jang, S.-H.1    Jaehning, J.A.2
  • 24
    • 0032941868 scopus 로고    scopus 로고
    • Feasting, fasting and fermenting. Glucose sensing in yeast and other cells
    • Johnston M. Feasting, fasting and fermenting. Glucose sensing in yeast and other cells. Trends Genet. 15 (1999) 29-33
    • (1999) Trends Genet. , vol.15 , pp. 29-33
    • Johnston, M.1
  • 25
    • 0037008697 scopus 로고    scopus 로고
    • Mutations in the yeast mitochondrial RNA polymerase specificity factor, Mtf1, verify its essential role in promoter utilization
    • Karlok M.A., Jang S.-H., and Jaehning J.A. Mutations in the yeast mitochondrial RNA polymerase specificity factor, Mtf1, verify its essential role in promoter utilization. J. Biol. Chem. 277 (2002) 28143-28149
    • (2002) J. Biol. Chem. , vol.277 , pp. 28143-28149
    • Karlok, M.A.1    Jang, S.-H.2    Jaehning, J.A.3
  • 26
    • 0022828772 scopus 로고
    • Isolation of the nuclear gene encoding a subunit of the yeast mitochondrial RNA polymerase
    • Kelly J.L., Greenleaf A.L., and Lehman I.R. Isolation of the nuclear gene encoding a subunit of the yeast mitochondrial RNA polymerase. J. Biol. Chem. 261 (1986) 10348-10351
    • (1986) J. Biol. Chem. , vol.261 , pp. 10348-10351
    • Kelly, J.L.1    Greenleaf, A.L.2    Lehman, I.R.3
  • 28
    • 0037474202 scopus 로고    scopus 로고
    • Binding of the priming nucleotide in the initiation of transcription by T7 RNA polymerase
    • Kuzmine I., Gottlieb P.A., and Martin C.T. Binding of the priming nucleotide in the initiation of transcription by T7 RNA polymerase. J. Biol. Chem. 278 (2003) 2819-2823
    • (2003) J. Biol. Chem. , vol.278 , pp. 2819-2823
    • Kuzmine, I.1    Gottlieb, P.A.2    Martin, C.T.3
  • 30
    • 0029873516 scopus 로고    scopus 로고
    • Transcription in vitro with Saccharomyces cerevisiae mitochondrial RNA polymerase
    • Mangus D.A., and Jaehning J.A. Transcription in vitro with Saccharomyces cerevisiae mitochondrial RNA polymerase. Methods Enzymol. 264 (1996) 57-66
    • (1996) Methods Enzymol. , vol.264 , pp. 57-66
    • Mangus, D.A.1    Jaehning, J.A.2
  • 31
    • 0027945504 scopus 로고
    • Release of the yeast mitochondrial RNA polymerase specificity factor from transcription complexes
    • Mangus D.A., Jang S.-H., and Jaehning J.A. Release of the yeast mitochondrial RNA polymerase specificity factor from transcription complexes. J. Biol. Chem. 269 (1994) 26568-26574
    • (1994) J. Biol. Chem. , vol.269 , pp. 26568-26574
    • Mangus, D.A.1    Jang, S.-H.2    Jaehning, J.A.3
  • 32
    • 7244232840 scopus 로고    scopus 로고
    • Intrinsic promoter recognition by a "core" RNA polymerase
    • Matsunaga M., and Jaehning J.A. Intrinsic promoter recognition by a "core" RNA polymerase. J. Biol. Chem. 279 (2004) 44239-44242
    • (2004) J. Biol. Chem. , vol.279 , pp. 44239-44242
    • Matsunaga, M.1    Jaehning, J.A.2
  • 33
    • 7244233311 scopus 로고    scopus 로고
    • Expression and purification of wild type and mutant forms of the yeast mitochondrial core RNA polymerase, Rpo41
    • Matsunaga M., Jang S.-H., and Jaehning J.A. Expression and purification of wild type and mutant forms of the yeast mitochondrial core RNA polymerase, Rpo41. Protein Expr. Purif. 35 (2004) 126-130
    • (2004) Protein Expr. Purif. , vol.35 , pp. 126-130
    • Matsunaga, M.1    Jang, S.-H.2    Jaehning, J.A.3
  • 34
    • 20444458289 scopus 로고    scopus 로고
    • Drosophila mitochondrial transcription factor B1 modulates mitochondrial translation but not transcription or DNA copy number in Schneider cells
    • Matsushima Y., Adan C., Garesse R., and Kaguni L.S. Drosophila mitochondrial transcription factor B1 modulates mitochondrial translation but not transcription or DNA copy number in Schneider cells. J. Biol. Chem. 280 (2005) 16815-16820
    • (2005) J. Biol. Chem. , vol.280 , pp. 16815-16820
    • Matsushima, Y.1    Adan, C.2    Garesse, R.3    Kaguni, L.S.4
  • 35
    • 0036148610 scopus 로고    scopus 로고
    • A human mitochondrial transcription factor is related to RNA adenine methyltransferases and binds S-adenosylmethionine
    • McCulloch V., Seidel-Rogol B.L., and Shadel G.S. A human mitochondrial transcription factor is related to RNA adenine methyltransferases and binds S-adenosylmethionine. Mol. Cell. Biol. 22 (2002) 1116-1125
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 1116-1125
    • McCulloch, V.1    Seidel-Rogol, B.L.2    Shadel, G.S.3
  • 36
    • 0023663369 scopus 로고
    • T7 lysozyme inhibits transcription by T7 RNA polymerase
    • Moffatt B.A., and Studier F.W. T7 lysozyme inhibits transcription by T7 RNA polymerase. Cell 49 (1987) 221-227
    • (1987) Cell , vol.49 , pp. 221-227
    • Moffatt, B.A.1    Studier, F.W.2
  • 37
    • 0023038036 scopus 로고
    • Steady state analysis of mitochondrial RNA after growth of yeast Saccharomyces cerevisiae under catabolite repression and derepression
    • Mueller D.M., and Getz G.S. Steady state analysis of mitochondrial RNA after growth of yeast Saccharomyces cerevisiae under catabolite repression and derepression. J. Biol. Chem. 261 (1986) 11816-11822
    • (1986) J. Biol. Chem. , vol.261 , pp. 11816-11822
    • Mueller, D.M.1    Getz, G.S.2
  • 38
    • 0022978145 scopus 로고
    • Transcriptional regulation of the mitochondrial genome of yeast Saccharomyces cerevisiae
    • Mueller D.M., and Getz G.S. Transcriptional regulation of the mitochondrial genome of yeast Saccharomyces cerevisiae. J. Biol. Chem. 261 (1986) 11756-11764
    • (1986) J. Biol. Chem. , vol.261 , pp. 11756-11764
    • Mueller, D.M.1    Getz, G.S.2
  • 39
    • 0033553435 scopus 로고    scopus 로고
    • Up-regulation of nuclear and mitochondrial genes in the skeletal muscle of mice lacking the heart/muscle isoform of the adenine nucleotide translocator
    • Murdock D.G., Boone B.E., Esposito L.A., and Wallace D.C. Up-regulation of nuclear and mitochondrial genes in the skeletal muscle of mice lacking the heart/muscle isoform of the adenine nucleotide translocator. J. Biol. Chem. 274 (1999) 14429-14433
    • (1999) J. Biol. Chem. , vol.274 , pp. 14429-14433
    • Murdock, D.G.1    Boone, B.E.2    Esposito, L.A.3    Wallace, D.C.4
  • 40
    • 0041669435 scopus 로고    scopus 로고
    • Control of rRNA expression by small molecules is dynamic and nonredundant
    • Murray H.D., Schneider R.A., and Gourse R.L. Control of rRNA expression by small molecules is dynamic and nonredundant. Mol. Cell 12 (2003) 125-134
    • (2003) Mol. Cell , vol.12 , pp. 125-134
    • Murray, H.D.1    Schneider, R.A.2    Gourse, R.L.3
  • 41
    • 0018676768 scopus 로고
    • Studies of RNA chain initiation by Escherichia coli RNA polymerase bound to T7 DNA. Direct analysis of the kinetics and extent of RNA chain initiation at T7 promoter A1
    • Nierman W.C., and Chamberlin M.J. Studies of RNA chain initiation by Escherichia coli RNA polymerase bound to T7 DNA. Direct analysis of the kinetics and extent of RNA chain initiation at T7 promoter A1. J. Biol. Chem. 254 (1979) 7921-7926
    • (1979) J. Biol. Chem. , vol.254 , pp. 7921-7926
    • Nierman, W.C.1    Chamberlin, M.J.2
  • 42
    • 0014084013 scopus 로고
    • The response of the respiratory chain and adenine nucleotide system to oxidative phosphorylation in yeast mitochondria
    • Onishi T., Kroger A., Heldt H.W., Pfaff E., and Klingenberg M. The response of the respiratory chain and adenine nucleotide system to oxidative phosphorylation in yeast mitochondria. Eur. J. Biochem. 1 (1967) 301-311
    • (1967) Eur. J. Biochem. , vol.1 , pp. 301-311
    • Onishi, T.1    Kroger, A.2    Heldt, H.W.3    Pfaff, E.4    Klingenberg, M.5
  • 43
    • 0020487995 scopus 로고
    • A nonanucleotide sequence involved in promotion of ribosomal RNA synthesis and RNA priming of DNA replication in yeast mitochondria
    • Osinga K.A., De Haan M., Christianson T., and Tabak H.F. A nonanucleotide sequence involved in promotion of ribosomal RNA synthesis and RNA priming of DNA replication in yeast mitochondria. Nucleic Acids Res. 10 (1982) 7993-8006
    • (1982) Nucleic Acids Res. , vol.10 , pp. 7993-8006
    • Osinga, K.A.1    De Haan, M.2    Christianson, T.3    Tabak, H.F.4
  • 44
    • 2442486948 scopus 로고    scopus 로고
    • The Snf1 kinase controls glucose repression in yeast by modulating interactions between the Mig1 repressor and the Cyc8-Tup1 co-repressor
    • Papamichos-Chronakis M., Gligoris T., and Tzamarias D. The Snf1 kinase controls glucose repression in yeast by modulating interactions between the Mig1 repressor and the Cyc8-Tup1 co-repressor. EMBO Rep. 5 (2004) 368-372
    • (2004) EMBO Rep. , vol.5 , pp. 368-372
    • Papamichos-Chronakis, M.1    Gligoris, T.2    Tzamarias, D.3
  • 45
    • 4043069926 scopus 로고    scopus 로고
    • DksA: a critical component of the transcription initiation machinery that potentiates the regulation of rRNA promoters by ppGpp and the initiating NTP
    • Paul B.J., Barker M.M., Ross W., Schneider D.A., Webb C., Foster J.W., and Gourse R.L. DksA: a critical component of the transcription initiation machinery that potentiates the regulation of rRNA promoters by ppGpp and the initiating NTP. Cell 118 (2004) 311-322
    • (2004) Cell , vol.118 , pp. 311-322
    • Paul, B.J.1    Barker, M.M.2    Ross, W.3    Schneider, D.A.4    Webb, C.5    Foster, J.W.6    Gourse, R.L.7
  • 46
    • 0037245552 scopus 로고    scopus 로고
    • Characterization of the mouse genes for mitochondrial transcription factors B1 and B2
    • Rantanen A., Gaspari M., Falkenberg M., Gustafsson C.M., and Larsson N.G. Characterization of the mouse genes for mitochondrial transcription factors B1 and B2. Mamm. Genome 14 (2003) 1-6
    • (2003) Mamm. Genome , vol.14 , pp. 1-6
    • Rantanen, A.1    Gaspari, M.2    Falkenberg, M.3    Gustafsson, C.M.4    Larsson, N.G.5
  • 47
    • 0032540298 scopus 로고    scopus 로고
    • Witnessing the evolution of transcription in mitochondria: the mitochondrial genome of the primitive brown alga Pylaiella littoralis (L.) Kjellm encodes a T7-like RNA polymerase
    • Rousvoal S., Oudot M., Fontaine J., Kloareg B., and Goer S.L. Witnessing the evolution of transcription in mitochondria: the mitochondrial genome of the primitive brown alga Pylaiella littoralis (L.) Kjellm encodes a T7-like RNA polymerase. J. Mol. Biol. 277 (1998) 1047-1057
    • (1998) J. Mol. Biol. , vol.277 , pp. 1047-1057
    • Rousvoal, S.1    Oudot, M.2    Fontaine, J.3    Kloareg, B.4    Goer, S.L.5
  • 48
    • 0025362399 scopus 로고
    • A rapid and simple method for preparation of RNA from Saccharomyces cerevisiae
    • Schmitt M.E., Brown T.A., and Trumpower B.L. A rapid and simple method for preparation of RNA from Saccharomyces cerevisiae. Nucleic Acids Res. 18 (1990) 3091-3092
    • (1990) Nucleic Acids Res. , vol.18 , pp. 3091-3092
    • Schmitt, M.E.1    Brown, T.A.2    Trumpower, B.L.3
  • 50
    • 0034326946 scopus 로고    scopus 로고
    • Mitochondrial genetics and disease
    • Schon E.A. Mitochondrial genetics and disease. Trends Biochem. Sci. 25 (2000) 555-560
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 555-560
    • Schon, E.A.1
  • 51
    • 4444268726 scopus 로고    scopus 로고
    • Coupling the mitochondrial transcription machinery to human disease
    • Shadel G.S. Coupling the mitochondrial transcription machinery to human disease. Trends Genet. 20 (2004) 513-519
    • (2004) Trends Genet. , vol.20 , pp. 513-519
    • Shadel, G.S.1
  • 52
    • 0032768263 scopus 로고    scopus 로고
    • The SNF1 kinase complex from Saccharomyces cerevisiae phosphorylates the transcriptional repressor protein Mig1p in vitro at four sites within or near regulatory domain 1
    • Smith F.C., Davies S.P., Wilson W.A., Carling D., and Hardie D.G. The SNF1 kinase complex from Saccharomyces cerevisiae phosphorylates the transcriptional repressor protein Mig1p in vitro at four sites within or near regulatory domain 1. FEBS Lett. 453 (1999) 219-223
    • (1999) FEBS Lett. , vol.453 , pp. 219-223
    • Smith, F.C.1    Davies, S.P.2    Wilson, W.A.3    Carling, D.4    Hardie, D.G.5
  • 53
    • 0034671599 scopus 로고    scopus 로고
    • A carbon-source-responsive element is required for regulation of the hypoxic ADP/ATP carrier (AAC3) isoform in Saccharomyces cerevisiae
    • Sokolikova B., Sabova L., Kissova I., and Kolarov J. A carbon-source-responsive element is required for regulation of the hypoxic ADP/ATP carrier (AAC3) isoform in Saccharomyces cerevisiae. Biochem. J. 352 (2000) 893-898
    • (2000) Biochem. J. , vol.352 , pp. 893-898
    • Sokolikova, B.1    Sabova, L.2    Kissova, I.3    Kolarov, J.4
  • 54
    • 0014434169 scopus 로고
    • RNA synthesis in yeast mitochondria: a derepressible activity
    • South D.J., and Mahler H.R. RNA synthesis in yeast mitochondria: a derepressible activity. Nature 218 (1968) 1226-1232
    • (1968) Nature , vol.218 , pp. 1226-1232
    • South, D.J.1    Mahler, H.R.2
  • 55
    • 0036308760 scopus 로고    scopus 로고
    • The intercalating beta-hairpin of T7 RNA polymerase plays a role in promoter DNA melting and in stabilizing the melted DNA for efficient RNA synthesis
    • Stano N.M., and Patel S.S. The intercalating beta-hairpin of T7 RNA polymerase plays a role in promoter DNA melting and in stabilizing the melted DNA for efficient RNA synthesis. J. Mol. Biol. 315 (2002) 1009-1025
    • (2002) J. Mol. Biol. , vol.315 , pp. 1009-1025
    • Stano, N.M.1    Patel, S.S.2
  • 56
    • 1942469443 scopus 로고    scopus 로고
    • T7 lysozyme represses T7 RNA polymerase transcription by destabilizing the open complex during initiation
    • Stano N.M., and Patel S.S. T7 lysozyme represses T7 RNA polymerase transcription by destabilizing the open complex during initiation. J. Biol. Chem. 279 (2004) 16136-16143
    • (2004) J. Biol. Chem. , vol.279 , pp. 16136-16143
    • Stano, N.M.1    Patel, S.S.2
  • 57
    • 0037020232 scopus 로고    scopus 로고
    • The +2 NTP binding drives open complex formation in T7 RNA polymerase
    • Stano N.M., Levin M.K., and Patel S.S. The +2 NTP binding drives open complex formation in T7 RNA polymerase. J. Biol. Chem. 277 (2002) 37292-37300
    • (2002) J. Biol. Chem. , vol.277 , pp. 37292-37300
    • Stano, N.M.1    Levin, M.K.2    Patel, S.S.3
  • 58
    • 0029904234 scopus 로고    scopus 로고
    • Expression of a recoded nuclear gene inserted into yeast mitochondrial DNA is limited by mRNA-specific translational activation
    • Steele D.F., Butler C.A., and Fox T.D. Expression of a recoded nuclear gene inserted into yeast mitochondrial DNA is limited by mRNA-specific translational activation. Proc. Natl. Acad. Sci. USA 93 (1996) 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
    • 0001070587 scopus 로고
    • Mitochondrial Structure
    • Strathem J.N., Jones E.W., and Broach J.R. (Eds), Cold Spring Harbor Laboratory, Cold Spring Harbor, New York
    • Stevens B. Mitochondrial Structure. In: Strathem J.N., Jones E.W., and Broach J.R. (Eds). The Molecular Biology of the Yeast Saccharomyces: Life Cycle and Inheritance (1981), Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 471-504
    • (1981) The Molecular Biology of the Yeast Saccharomyces: Life Cycle and Inheritance , pp. 471-504
    • Stevens, B.1
  • 60
    • 0038271638 scopus 로고    scopus 로고
    • Effect of insulin on human skeletal muscle mitochondrial ATP production, protein synthesis, and mRNA transcripts
    • Stump C.S., Short K.R., Bigelow M.L., Schimke J.M., and Nair K.S. Effect of insulin on human skeletal muscle mitochondrial ATP production, protein synthesis, and mRNA transcripts. Proc. Natl. Acad. Sci. USA 100 (2003) 7996-8001
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 7996-8001
    • Stump, C.S.1    Short, K.R.2    Bigelow, M.L.3    Schimke, J.M.4    Nair, K.S.5
  • 61
    • 23444455020 scopus 로고
    • Glucose repression of yeast mitochondrial transcription: kinetics of derepression and role of nuclear genes
    • Ulery T.L., Jang S.-H., and Jaehning J.A. Glucose repression of yeast mitochondrial transcription: kinetics of derepression and role of nuclear genes. Mol. Cell. Biol. 14 (1994) 1160-1170
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 1160-1170
    • Ulery, T.L.1    Jang, S.-H.2    Jaehning, J.A.3
  • 62
    • 0032483398 scopus 로고    scopus 로고
    • Specificity in transcriptional regulation in the absence of specific DNA binding sites: the case of T7 lysozyme
    • Villemain J., and Sousa R. Specificity in transcriptional regulation in the absence of specific DNA binding sites: the case of T7 lysozyme. J. Mol. Biol. 281 (1998) 793-802
    • (1998) J. Mol. Biol. , vol.281 , pp. 793-802
    • Villemain, J.1    Sousa, R.2
  • 63
    • 0031567783 scopus 로고    scopus 로고
    • Role of open complex instability in kinetic promoter selection by bacteriophage T7 RNA polymerase
    • Villemain J., Guajardo R., and Sousa R. Role of open complex instability in kinetic promoter selection by bacteriophage T7 RNA polymerase. J. Mol. Biol. 273 (1997) 958-977
    • (1997) J. Mol. Biol. , vol.273 , pp. 958-977
    • Villemain, J.1    Guajardo, R.2    Sousa, R.3
  • 64
    • 0030293885 scopus 로고    scopus 로고
    • Glucose repression/derepression in budding yeast: SNF1 protein kinase is activated by phosphorylation under derepressing conditions, and this correlates with a high AMP:ATP ratio
    • Wilson W.A., Hawley S.A., and Hardie D.G. Glucose repression/derepression in budding yeast: SNF1 protein kinase is activated by phosphorylation under derepressing conditions, and this correlates with a high AMP:ATP ratio. Curr. Biol. 6 (1996) 1426-1434
    • (1996) Curr. Biol. , vol.6 , pp. 1426-1434
    • Wilson, W.A.1    Hawley, S.A.2    Hardie, D.G.3
  • 65
    • 0022397934 scopus 로고
    • A multicomponent mitochondrial RNA polymerase from Saccharomyces cerevisiae
    • Winkley C.S., Keller M.J., and Jaehning J.A. A multicomponent mitochondrial RNA polymerase from Saccharomyces cerevisiae. J. Biol. Chem. 260 (1985) 14214-14223
    • (1985) J. Biol. Chem. , vol.260 , pp. 14214-14223
    • Winkley, C.S.1    Keller, M.J.2    Jaehning, J.A.3
  • 66
    • 0028070457 scopus 로고
    • Yeast SNF1 is functionally related to mammalian AMP-activated protein kinase and regulates acetyl-CoA carboxylase in vivo
    • Woods A., Munday M.R., Scott J., Yang X., Carlson M., and Carling D. Yeast SNF1 is functionally related to mammalian AMP-activated protein kinase and regulates acetyl-CoA carboxylase in vivo. J. Biol. Chem. 269 (1994) 19509-19515
    • (1994) J. Biol. Chem. , vol.269 , pp. 19509-19515
    • Woods, A.1    Munday, M.R.2    Scott, J.3    Yang, X.4    Carlson, M.5    Carling, D.6
  • 67
    • 0037123763 scopus 로고    scopus 로고
    • Views of transcription initiation
    • Young B.A., Gruber T.M., and Gross C.A. Views of transcription initiation. Cell 109 (2002) 417-420
    • (2002) Cell , vol.109 , pp. 417-420
    • Young, B.A.1    Gruber, T.M.2    Gross, C.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.