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Volumn 16, Issue 11, 1997, Pages 3198-3206

The HMG-box mitochondrial transcription factor xl-mtTFA binds DNA as a tetramer to activate bidirectional transcription

Author keywords

HMG box; Mitochondria; MtTFA; STEM; Transcription

Indexed keywords

DIMER; DNA BINDING PROTEIN; MITOCHONDRIAL DNA; TETRAMER; TRANSCRIPTION FACTOR;

EID: 0030946172     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/16.11.3198     Document Type: Article
Times cited : (34)

References (38)
  • 1
    • 0023656458 scopus 로고
    • Differences between HMG1 proteins isolated from normal and tumor cells
    • Alexandrova, E.A. and Beltchev, B.G. (1987) Differences between HMG1 proteins isolated from normal and tumor cells. Biochim. Biophys. Acta, 915, 399-405.
    • (1987) Biochim. Biophys. Acta , vol.915 , pp. 399-405
    • Alexandrova, E.A.1    Beltchev, B.G.2
  • 2
    • 0028803960 scopus 로고
    • Distinct roles for two purified factors in transcription of Xenopus mitochondnal DNA
    • Antoshechkin, I. and Bogenhagen, D.F. (1995) Distinct roles for two purified factors in transcription of Xenopus mitochondnal DNA. Mol. Cell. Biol., 15, 7032-7042.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 7032-7042
    • Antoshechkin, I.1    Bogenhagen, D.F.2
  • 3
    • 0029070956 scopus 로고
    • The HMG-1 box protein family: Classification and functional relationships
    • Baxevanis, A.D. and Landsman, D. (1995) The HMG-1 box protein family: classification and functional relationships. Nucleic Acids Res., 23, 1604-1613.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 1604-1613
    • Baxevanis, A.D.1    Landsman, D.2
  • 4
    • 0029759341 scopus 로고    scopus 로고
    • Single-stranded DNA binding alters human replication protein A structure and facilitates interaction with DNA-dependent protein kinase
    • Blackwell, L.J., Borowiec, J.A. and Mastrangelo, I.A. (1996) Single-stranded DNA binding alters human replication protein A structure and facilitates interaction with DNA-dependent protein kinase. Mol. Cell. Biol., 16, 4798-4807.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4798-4807
    • Blackwell, L.J.1    Borowiec, J.A.2    Mastrangelo, I.A.3
  • 5
    • 15844420658 scopus 로고    scopus 로고
    • Interaction of mtTFB and mtRNA polymerase at core promoters for transcription of Xenopus laevis mtDNA
    • Bogenhagen, D.F. (1996) Interaction of mtTFB and mtRNA polymerase at core promoters for transcription of Xenopus laevis mtDNA. J. Biol. Chem., 271, 12036-12041.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12036-12041
    • Bogenhagen, D.F.1
  • 6
    • 0024039764 scopus 로고
    • Purification of Xenopus laevis mitochondrial RNA polymerase and identification of a dissociable factor required for specific transcription
    • Bogenhagen, D.F. and Insdorf, N.F. (1988) Purification of Xenopus laevis mitochondrial RNA polymerase and identification of a dissociable factor required for specific transcription. Mol. Cell. Biol., 8, 2910-2916.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 2910-2916
    • Bogenhagen, D.F.1    Insdorf, N.F.2
  • 7
    • 0024044159 scopus 로고
    • Template sequences required for transcription of Xenopus laevis mitochondnal DNA from two bidirectional promoters
    • Bogenhagen, D.F. and Romanelli, M.F. (1988) Template sequences required for transcription of Xenopus laevis mitochondnal DNA from two bidirectional promoters. Mol. Cell. Biol., 8, 2917-2924.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 2917-2924
    • Bogenhagen, D.F.1    Romanelli, M.F.2
  • 8
    • 0028950413 scopus 로고
    • HMG-D is an architecture-specific protein that preferentially binds to DNA containing the dinucleotide TG
    • Churchill, M.E., Jones, D.N., Glaser, T., Hefner, H., Searles, M.A. and Travers, A.A. (1995) HMG-D is an architecture-specific protein that preferentially binds to DNA containing the dinucleotide TG. EMBO J., 14, 1264-1275.
    • (1995) EMBO J. , vol.14 , pp. 1264-1275
    • Churchill, M.E.1    Jones, D.N.2    Glaser, T.3    Hefner, H.4    Searles, M.A.5    Travers, A.A.6
  • 9
    • 0029070402 scopus 로고
    • Addition of a 29 residue carboxyl-terminal tail converts a simple HMG box-containing protein into a transcriptional activator
    • Dairaghi, D., Shadel, G. and Clayton, D. (1995) Addition of a 29 residue carboxyl-terminal tail converts a simple HMG box-containing protein into a transcriptional activator. J. Mol. Biol., 249, 11-28.
    • (1995) J. Mol. Biol. , vol.249 , pp. 11-28
    • Dairaghi, D.1    Shadel, G.2    Clayton, D.3
  • 10
    • 0025912955 scopus 로고
    • A close relative of the nuclear, chromosomal high-mobility group protein HMG1 in yeast mitochondria
    • Diffley, J.F. and Stillman, B. (1991) A close relative of the nuclear, chromosomal high-mobility group protein HMG1 in yeast mitochondria. Proc. Natl Acad. Sci. USA, 88, 7864-7868.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 7864-7868
    • Diffley, J.F.1    Stillman, B.2
  • 11
    • 0026673872 scopus 로고
    • DNA binding properties of an HMG1-related protein from yeast mitochondria
    • Diffley, J.F. and Stillman, B. (1992) DNA binding properties of an HMG1-related protein from yeast mitochondria. J. Biol. Chem., 267, 3368-3374.
    • (1992) J. Biol. Chem. , vol.267 , pp. 3368-3374
    • Diffley, J.F.1    Stillman, B.2
  • 12
    • 0023684801 scopus 로고
    • Purification and characterization of human mitochondrial transcription factor 1
    • Fisher, R.P. and Clayton, D.A. (1988) Purification and characterization of human mitochondrial transcription factor 1. Mol. Cell. Biol., 8, 3496-3509.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 3496-3509
    • Fisher, R.P.1    Clayton, D.A.2
  • 13
    • 0023658329 scopus 로고
    • Promoter selection in human mitochondria involves binding of a transcription factor to orientation-independent upstream regulatory elements
    • Fisher, R.P., Topper, J.N. and Clayton, D.A. (1987) Promoter selection in human mitochondria involves binding of a transcription factor to orientation-independent upstream regulatory elements. Cell, 50, 247-258.
    • (1987) Cell , vol.50 , pp. 247-258
    • Fisher, R.P.1    Topper, J.N.2    Clayton, D.A.3
  • 14
    • 0026640728 scopus 로고
    • DNA wrapping and bending by a mitochondrial high mobility group-like transcriptional activator protein
    • Fisher, R.P., Lisowsky, T., Parisi, M.A. and Clayton, D.A. (1992) DNA wrapping and bending by a mitochondrial high mobility group-like transcriptional activator protein. J. Biol. Chem., 267, 3358-3367.
    • (1992) J. Biol. Chem. , vol.267 , pp. 3358-3367
    • Fisher, R.P.1    Lisowsky, T.2    Parisi, M.A.3    Clayton, D.A.4
  • 15
    • 0028197368 scopus 로고
    • HMG domain proteins; architectural elements in the assembly of nucleoprotein structures
    • Grosschedl, R., Giese, K. and Pagel, J. (1994) HMG domain proteins; architectural elements in the assembly of nucleoprotein structures. Trends Genet., 10, 94-99.
    • (1994) Trends Genet. , vol.10 , pp. 94-99
    • Grosschedl, R.1    Giese, K.2    Pagel, J.3
  • 16
    • 0028657623 scopus 로고
    • Molecular basis of mammalian sexual determination: Activation of Mullerian inhibiting substance gene expression by SRY
    • Haqq, C.M., King, C.Y., Ukiyama, E., Falsafi, S., Haqq, T.N., Donahoe, P.K. and Weiss, M.A. (1994) Molecular basis of mammalian sexual determination: activation of Mullerian inhibiting substance gene expression by SRY. Science, 266, 1494-1500.
    • (1994) Science , vol.266 , pp. 1494-1500
    • Haqq, C.M.1    King, C.Y.2    Ukiyama, E.3    Falsafi, S.4    Haqq, T.N.5    Donahoe, P.K.6    Weiss, M.A.7
  • 18
    • 0003448569 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Harlow, E. and Lane, D. (1988) Antibodies: A Laboratory Manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1988) Antibodies: A Laboratory Manual
    • Harlow, E.1    Lane, D.2
  • 19
    • 0026754764 scopus 로고
    • Multiple domains of the RNA polymerase I activator hUBF interact with the TATA-binding protein complex hSL1 to mediate transcription
    • Jantzen, H.M., Chow, A.M., King, D.S. and Tjian, R. (1992) Multiple domains of the RNA polymerase I activator hUBF interact with the TATA-binding protein complex hSL1 to mediate transcription. Genes Dev., 6, 1950-1963.
    • (1992) Genes Dev. , vol.6 , pp. 1950-1963
    • Jantzen, H.M.1    Chow, A.M.2    King, D.S.3    Tjian, R.4
  • 20
    • 0027512825 scopus 로고
    • Ribonuclease S-peptide as a carrier in fusion proteins
    • Kim, J.S. and Raines, R.T. (1993) Ribonuclease S-peptide as a carrier in fusion proteins. Protein Sci., 2, 348-356.
    • (1993) Protein Sci. , vol.2 , pp. 348-356
    • Kim, J.S.1    Raines, R.T.2
  • 21
    • 0027646025 scopus 로고
    • A signature for the HMG-1 box DNA-binding proteins
    • Landsman, D. and Bustin, M. (1993) A signature for the HMG-1 box DNA-binding proteins. BioEssays, 15, 539-546.
    • (1993) BioEssays , vol.15 , pp. 539-546
    • Landsman, D.1    Bustin, M.2
  • 22
    • 0029131298 scopus 로고
    • Structural basis for DNA bending by the architectural transcription factor LEF-1
    • Love, J.J., Li, X., Case, D.A., Giese, K., Grosschedl, R. and Wright, P.E. (1995) Structural basis for DNA bending by the architectural transcription factor LEF-1. Nature, 376, 791-795.
    • (1995) Nature , vol.376 , pp. 791-795
    • Love, J.J.1    Li, X.2    Case, D.A.3    Giese, K.4    Grosschedl, R.5    Wright, P.E.6
  • 23
    • 0024550638 scopus 로고
    • ATP-dependent assembly of double hexamers of SV40 T antigen at the viral origin of DNA replication
    • Mastrangelo, I.A., Hough, P.V., Wall, J.S., Dodson, M., Dean, F.B. and Hurwitz, J. (1989) ATP-dependent assembly of double hexamers of SV40 T antigen at the viral origin of DNA replication. Nature, 338, 658-662.
    • (1989) Nature , vol.338 , pp. 658-662
    • Mastrangelo, I.A.1    Hough, P.V.2    Wall, J.S.3    Dodson, M.4    Dean, F.B.5    Hurwitz, J.6
  • 24
    • 0026075609 scopus 로고
    • DNA looping and Sp1 multimer links: A mechanism for transcriptional synergism and enhancement
    • Mastrangelo, I.A., Courey, A.J., Wall, J.S., Jackson, S.P. and Hough, P.V. (1991) DNA looping and Sp1 multimer links: a mechanism for transcriptional synergism and enhancement. Proc. Natl Acad. Sci. USA, 88, 5670-5674.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 5670-5674
    • Mastrangelo, I.A.1    Courey, A.J.2    Wall, J.S.3    Jackson, S.P.4    Hough, P.V.5
  • 25
    • 0027170306 scopus 로고
    • RIP60 dimers and multiples of dimers assemble link structures at an origin of bidirectional replication in the dihydrofolate reductase amplicon of Chinese hamster ovary cells
    • Mastrangelo, I.A., Held, P.G., Dailey, L., Wall, J.S., Hough, P.V., Heintz, N. and Heintz, N.H. (1993) RIP60 dimers and multiples of dimers assemble link structures at an origin of bidirectional replication in the dihydrofolate reductase amplicon of Chinese hamster ovary cells. J. Mol. Biol., 232, 766-778.
    • (1993) J. Mol. Biol. , vol.232 , pp. 766-778
    • Mastrangelo, I.A.1    Held, P.G.2    Dailey, L.3    Wall, J.S.4    Hough, P.V.5    Heintz, N.6    Heintz, N.H.7
  • 26
    • 0023046962 scopus 로고
    • Characterization of a Xenopus laevis mitochondrial protein with a high affinity for supercoiled DNA
    • Mignotte, B. and Barat, M. (1986) Characterization of a Xenopus laevis mitochondrial protein with a high affinity for supercoiled DNA. Nucleic Acids Res., 14, 5969-5980.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 5969-5980
    • Mignotte, B.1    Barat, M.2
  • 27
    • 0029785711 scopus 로고    scopus 로고
    • Effects of Xenopus laevis mitochondrial single-stranded DNA-binding protein on primer-template binding and 3′→5′ exonuclease activity of DNA polymerase γ
    • Mikhailov, V.S. and Bogenhagen, D.F. (1996) Effects of Xenopus laevis mitochondrial single-stranded DNA-binding protein on primer-template binding and 3′→5′ exonuclease activity of DNA polymerase γ. J. Biol. Chem., 271, 18939-18946.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18939-18946
    • Mikhailov, V.S.1    Bogenhagen, D.F.2
  • 28
    • 0029978327 scopus 로고    scopus 로고
    • Analysis of mitochondrial DNA nucleoids in wild-type and a mutant strain of Saccharomyces cerevisiae that lacks the mitochondrial HMG box protein Abf2p
    • Newman, S.M., Zelenaya-Troitskaya, O., Perlman, P.S. and Butow, R.A. (1996) Analysis of mitochondrial DNA nucleoids in wild-type and a mutant strain of Saccharomyces cerevisiae that lacks the mitochondrial HMG box protein Abf2p. Nucleic Acids Res., 24, 386-393.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 386-393
    • Newman, S.M.1    Zelenaya-Troitskaya, O.2    Perlman, P.S.3    Butow, R.A.4
  • 29
    • 0022613418 scopus 로고
    • Characterization of the cell surface receptor for a multi-lineage colony-stimulating factor (CSF-2 alpha)
    • Park, L.S., Friend, D., Gillis, S. and Urdal, D.L. (1986) Characterization of the cell surface receptor for a multi-lineage colony-stimulating factor (CSF-2 alpha). J. Biol. Chem., 261, 205-210.
    • (1986) J. Biol. Chem. , vol.261 , pp. 205-210
    • Park, L.S.1    Friend, D.2    Gillis, S.3    Urdal, D.L.4
  • 30
    • 0028921099 scopus 로고
    • An SRY mutation causing human sex reversal resolves a general mechanism of structure-specific DNA recognition: Application to the four-way DNA junction
    • Peters, R., King, C.Y., Ukiyama, E., Falsafi, S., Donahoe, P.K. and Weiss, M.A. (1995) An SRY mutation causing human sex reversal resolves a general mechanism of structure-specific DNA recognition: application to the four-way DNA junction. Biochemistry, 34, 4569-4576.
    • (1995) Biochemistry , vol.34 , pp. 4569-4576
    • Peters, R.1    King, C.Y.2    Ukiyama, E.3    Falsafi, S.4    Donahoe, P.K.5    Weiss, M.A.6
  • 31
    • 0017848160 scopus 로고
    • Evidence for a mitochondrial chromosome in Xenopus laevis oocytes
    • Pinon, H., Barat, M., Tourte, M., Dufresne, C. and Mounolou, J. (1978) Evidence for a mitochondrial chromosome in Xenopus laevis oocytes. Chromosoma, 65, 383-389.
    • (1978) Chromosoma , vol.65 , pp. 383-389
    • Pinon, H.1    Barat, M.2    Tourte, M.3    Dufresne, C.4    Mounolou, J.5
  • 33
    • 0020362442 scopus 로고
    • Influence of metal ions on prothrombin self-association. Demonstration of dimer formation by intermolecular cross-linking with dithiobis(succinimidylpropionate)
    • Tarvers, R.C., Noyes, C.M., Roberts, H.R. and Lundblad, R.L. (1982) Influence of metal ions on prothrombin self-association. Demonstration of dimer formation by intermolecular cross-linking with dithiobis(succinimidylpropionate). J. Biol. Chem., 257, 10708-10714.
    • (1982) J. Biol. Chem. , vol.257 , pp. 10708-10714
    • Tarvers, R.C.1    Noyes, C.M.2    Roberts, H.R.3    Lundblad, R.L.4
  • 34
    • 0029117147 scopus 로고
    • Two mutations in the HMG-box with very different structural consequences provide insights into the nature of binding to four-way junction DNA
    • Teo, S.H., Grasser, K.D., Hardman, C.H., Broadhurst, R.W., Laue, E.D. and Thomas, J.O. (1995) Two mutations in the HMG-box with very different structural consequences provide insights into the nature of binding to four-way junction DNA. EMBO J., 14, 3844-3853.
    • (1995) EMBO J. , vol.14 , pp. 3844-3853
    • Teo, S.H.1    Grasser, K.D.2    Hardman, C.H.3    Broadhurst, R.W.4    Laue, E.D.5    Thomas, J.O.6
  • 35
    • 0026696874 scopus 로고
    • Sequence-specific interaction of the HMG box proteins TCF-1 and SRY occurs within the minor groove of a Watson-Crick double helix
    • van de Wetering, M. and Clevers, H. (1992) Sequence-specific interaction of the HMG box proteins TCF-1 and SRY occurs within the minor groove of a Watson-Crick double helix. EMBO J., 11, 3039-3044.
    • (1992) EMBO J. , vol.11 , pp. 3039-3044
    • Van De Wetering, M.1    Clevers, H.2
  • 36
    • 0002439836 scopus 로고
    • Biological scanning transmission electron microscopy
    • Hren J., Goldstein J. and Jay, D. (eds), Plenum Press, New York
    • Wall, J.S. (1979) Biological scanning transmission electron microscopy. In Hren J., Goldstein J. and Jay, D. (eds), Analytical Electron Microscopy. Plenum Press, New York, pp. 333-342.
    • (1979) Analytical Electron Microscopy , pp. 333-342
    • Wall, J.S.1
  • 37
    • 0029075461 scopus 로고
    • Molecular basis of human 46X, Y sex reversal revealed from the three-dimensional solution structure of the human SRY-DNA complex
    • Werner, M.H., Huth, J.R., Gronenborn, A.M. and Clore, G.M. (1995) Molecular basis of human 46X, Y sex reversal revealed from the three-dimensional solution structure of the human SRY-DNA complex. Cell, 81, 705-714.
    • (1995) Cell , vol.81 , pp. 705-714
    • Werner, M.H.1    Huth, J.R.2    Gronenborn, A.M.3    Clore, G.M.4
  • 38
    • 0026598146 scopus 로고
    • Assignment of a yeast protein necessary for mitochondrial transcription initiation
    • Xu, B. and Clayton, D.A. (1992) Assignment of a yeast protein necessary for mitochondrial transcription initiation. Nucleic Acids Res., 20, 1053-1059.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 1053-1059
    • Xu, B.1    Clayton, D.A.2


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