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Volumn 279, Issue 12, 2012, Pages 2108-2119

A S-adenosylmethionine methyltransferase-like domain within the essential, Fe-S-containing yeast protein Dre2

Author keywords

Dre2; iron sulfur cluster; NMR; SAM methyltransferase fold; yeast

Indexed keywords

ANAMORSIN; ESSENTIAL YEAST PROTEIN; IRON SULFUR CLUSTER CONTAINING PROTEIN; IRON SULFUR PROTEIN; MONOMER; PROTEIN; UNCLASSIFIED DRUG; YEAST PROTEIN DRE2;

EID: 84861849278     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2012.08597.x     Document Type: Article
Times cited : (25)

References (36)
  • 1
    • 0042475409 scopus 로고    scopus 로고
    • Characterization of mutations that are synthetic lethal with pol3-13, a mutated allele of DNA polymerase delta in Saccharomyces cerevisiae
    • Chanet R, &, Heude M, (2003) Characterization of mutations that are synthetic lethal with pol3-13, a mutated allele of DNA polymerase delta in Saccharomyces cerevisiae. Curr Genet 43, 337-350.
    • (2003) Curr Genet , vol.43 , pp. 337-350
    • Chanet, R.1    Heude, M.2
  • 2
    • 43049146539 scopus 로고    scopus 로고
    • Toward a comprehensive temperature-sensitive mutant repository of the essential genes of Saccharomyces cerevisiae
    • Ben-Aroya S, Coombes C, Kwok T, O'Donnell KA, Boeke JD, &, Hieter P, (2008) Toward a comprehensive temperature-sensitive mutant repository of the essential genes of Saccharomyces cerevisiae. Mol Cell 30, 248-258.
    • (2008) Mol Cell , vol.30 , pp. 248-258
    • Ben-Aroya, S.1    Coombes, C.2    Kwok, T.3    O'Donnell, K.A.4    Boeke, J.D.5    Hieter, P.6
  • 4
    • 84887212507 scopus 로고    scopus 로고
    • A newly identified essential complex, Dre2-Tah18, controls mitochondria integrity and cell death after oxidative stress in yeast
    • Vernis L, Facca C, Delagoutte E, Soler N, Chanet R, Guiard B, Faye G, &, Baldacci G, (2009) A newly identified essential complex, Dre2-Tah18, controls mitochondria integrity and cell death after oxidative stress in yeast. PLoS One 4, e4376.
    • (2009) PLoS One , vol.4
    • Vernis, L.1    Facca, C.2    Delagoutte, E.3    Soler, N.4    Chanet, R.5    Guiard, B.6    Faye, G.7    Baldacci, G.8
  • 6
    • 0033613167 scopus 로고    scopus 로고
    • CDC45 and DPB11 are required for processive DNA replication and resistance to DNA topoisomerase I-mediated DNA damage
    • Reid RJ, Fiorani P, Sugawara M, &, Bjornsti MA, (1999) CDC45 and DPB11 are required for processive DNA replication and resistance to DNA topoisomerase I-mediated DNA damage. Proc Natl Acad Sci USA 96, 11440-11445.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 11440-11445
    • Reid, R.J.1    Fiorani, P.2    Sugawara, M.3    Bjornsti, M.A.4
  • 9
    • 1242321069 scopus 로고    scopus 로고
    • Identification of a cytokine-induced antiapoptotic molecule anamorsin essential for definitive hematopoiesis
    • Shibayama H, Takai E, Matsumura I, Kouno M, Morii E, Kitamura Y, Takeda J, &, Kanakura Y, (2004) Identification of a cytokine-induced antiapoptotic molecule anamorsin essential for definitive hematopoiesis. J Exp Med 199, 581-592.
    • (2004) J Exp Med , vol.199 , pp. 581-592
    • Shibayama, H.1    Takai, E.2    Matsumura, I.3    Kouno, M.4    Morii, E.5    Kitamura, Y.6    Takeda, J.7    Kanakura, Y.8
  • 10
  • 11
    • 0036917889 scopus 로고    scopus 로고
    • SAM (dependent) I AM: The S-adenosylmethionine-dependent methyltransferase fold
    • Martin JL, &, McMillan FM, (2002) SAM (dependent) I AM: the S-adenosylmethionine-dependent methyltransferase fold. Curr Opin Struct Biol 12, 783-793.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 783-793
    • Martin, J.L.1    McMillan, F.M.2
  • 13
    • 0034694686 scopus 로고    scopus 로고
    • Conversion of 3Fe-4S to 4Fe-4s clusters in native pyruvate formate-lyase activating enzyme: Mössbauer characterization and implications for mechanism
    • Krebs C, Henshaw TF, Cheek J, Huynh BH, &, Broderick JB, (2000) Conversion of 3Fe-4S to 4Fe-4s clusters in native pyruvate formate-lyase activating enzyme: mössbauer characterization and implications for mechanism. J Am Chem Soc 122, 12497-12506.
    • (2000) J Am Chem Soc , vol.122 , pp. 12497-12506
    • Krebs, C.1    Henshaw, T.F.2    Cheek, J.3    Huynh, B.H.4    Broderick, J.B.5
  • 14
    • 0034595376 scopus 로고    scopus 로고
    • Iron-sulfur cluster interconversions in biotin synthase: Dissociation and reassociation of iron during conversion of [2Fe-2S] to [4Fe-4S] clusters
    • Ugulava NB, Gibney BR, &, Jarrett JT, (2000) Iron-sulfur cluster interconversions in biotin synthase: dissociation and reassociation of iron during conversion of [2Fe-2S] to [4Fe-4S] clusters. Biochemistry 39, 5206-5214.
    • (2000) Biochemistry , vol.39 , pp. 5206-5214
    • Ugulava, N.B.1    Gibney, B.R.2    Jarrett, J.T.3
  • 15
  • 17
    • 33847804116 scopus 로고
    • Conformation in the excited state of two tryptophanyl diketopiperazines
    • Donzel B, Gaudchon P, &, Wahl P, (1974) Conformation in the excited state of two tryptophanyl diketopiperazines. J Am Chem Soc 96, 801-808.
    • (1974) J Am Chem Soc , vol.96 , pp. 801-808
    • Donzel, B.1    Gaudchon, P.2    Wahl, P.3
  • 18
    • 33750927821 scopus 로고
    • Fluorescence decay of tryptophan conformers in aqueous solution
    • Szabo AG, &, Rayner DM, (1980) Fluorescence decay of tryptophan conformers in aqueous solution. J Am Chem Soc 102, 554-563.
    • (1980) J Am Chem Soc , vol.102 , pp. 554-563
    • Szabo, A.G.1    Rayner, D.M.2
  • 19
    • 0032516433 scopus 로고    scopus 로고
    • Toward understanding tryptophan fluorescence in proteins
    • Chen Y, &, Barkley MD, (1998) Toward understanding tryptophan fluorescence in proteins. Biochemistry 37, 9976-9982.
    • (1998) Biochemistry , vol.37 , pp. 9976-9982
    • Chen, Y.1    Barkley, M.D.2
  • 21
    • 36549044982 scopus 로고    scopus 로고
    • Successful expression and purification of human CIAPIN1 in baculovirus-insect cell system and application of this system to investigation of its potential methyltransferase activity
    • Hao Z, Li X, Qiao T, &, Fan D, (2008) Successful expression and purification of human CIAPIN1 in baculovirus-insect cell system and application of this system to investigation of its potential methyltransferase activity. Int J Biol Macromol 42, 27-32.
    • (2008) Int J Biol Macromol , vol.42 , pp. 27-32
    • Hao, Z.1    Li, X.2    Qiao, T.3    Fan, D.4
  • 22
    • 33847635732 scopus 로고    scopus 로고
    • S-adenosylmethionine as an oxidant: The radical SAM superfamily
    • Wang SC, &, Frey PA, (2007) S-adenosylmethionine as an oxidant: the radical SAM superfamily. Trends Biochem Sci 32, 101-110.
    • (2007) Trends Biochem Sci , vol.32 , pp. 101-110
    • Wang, S.C.1    Frey, P.A.2
  • 24
    • 0037432317 scopus 로고    scopus 로고
    • Control of adenosylmethionine-dependent radical generation in biotin synthase: A kinetic and thermodynamic analysis of substrate binding to active and inactive forms of BioB
    • Ugulava NB, Frederick KK, &, Jarrett JT, (2003) Control of adenosylmethionine-dependent radical generation in biotin synthase: a kinetic and thermodynamic analysis of substrate binding to active and inactive forms of BioB. Biochemistry 42, 2708-2719.
    • (2003) Biochemistry , vol.42 , pp. 2708-2719
    • Ugulava, N.B.1    Frederick, K.K.2    Jarrett, J.T.3
  • 25
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: Multiple sequence alignment with high accuracy and high throughput
    • Edgar RC, (2004) MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res 32, 1792-1797.
    • (2004) Nucleic Acids Res , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 28
    • 0242578620 scopus 로고    scopus 로고
    • A simple, fast, and accurate algorithm to estimate large phylogenies by maximum likelihood
    • Guindon S, &, Gascuel O, (2003) A simple, fast, and accurate algorithm to estimate large phylogenies by maximum likelihood. Syst Biol 52, 696-704.
    • (2003) Syst Biol , vol.52 , pp. 696-704
    • Guindon, S.1    Gascuel, O.2
  • 29
    • 33744809773 scopus 로고    scopus 로고
    • Macromolecular size-and-shape distributions by sedimentation velocity analytical ultracentrifugation
    • Brown PH, &, Schuck P, (2006) Macromolecular size-and-shape distributions by sedimentation velocity analytical ultracentrifugation. Biophys J 90, 4651-4661.
    • (2006) Biophys J , vol.90 , pp. 4651-4661
    • Brown, P.H.1    Schuck, P.2
  • 30
    • 0001229341 scopus 로고    scopus 로고
    • Calculation of hydrodynamic properties of globular proteins from their atomic-level structure
    • Garcia De La Torre J, Huertas ML, &, Carrasco B, (2000) Calculation of hydrodynamic properties of globular proteins from their atomic-level structure. Biophys J 78, 719-730.
    • (2000) Biophys J , vol.78 , pp. 719-730
    • Garcia De La Torre, J.1    Huertas, M.L.2    Carrasco, B.3
  • 31
    • 77950552976 scopus 로고    scopus 로고
    • The implementation of SOMO (SOlution MOdeller) in the UltraScan analytical ultracentrifugation data analysis suite: Enhanced capabilities allow the reliable hydrodynamic modeling of virtually any kind of biomacromolecule
    • Brookes E, Demeler B, Rosano C, &, Rocco M, (2010) The implementation of SOMO (SOlution MOdeller) in the UltraScan analytical ultracentrifugation data analysis suite: enhanced capabilities allow the reliable hydrodynamic modeling of virtually any kind of biomacromolecule. Eur Biophys J 39, 423-435.
    • (2010) Eur Biophys J , vol.39 , pp. 423-435
    • Brookes, E.1    Demeler, B.2    Rosano, C.3    Rocco, M.4
  • 32
    • 0001464493 scopus 로고
    • Analyzing the distribution of decay constants in pulse-fluorimetry using the maximum entropy method
    • Livesey AK, &, Brochon JC, (1987) Analyzing the distribution of decay constants in pulse-fluorimetry using the maximum entropy method. Biophys J 52, 693-706.
    • (1987) Biophys J , vol.52 , pp. 693-706
    • Livesey, A.K.1    Brochon, J.C.2
  • 33
    • 0024299704 scopus 로고
    • Nanosecond dynamics of horse heart apocytochrome c in aqueous solution as studied by time-resolved fluorescence of the single tryptophan residue (Trp-59)
    • Vincent M, Brochon JC, Merola F, Jordi W, &, Gallay J, (1988) Nanosecond dynamics of horse heart apocytochrome c in aqueous solution as studied by time-resolved fluorescence of the single tryptophan residue (Trp-59). Biochemistry 27, 8752-8761.
    • (1988) Biochemistry , vol.27 , pp. 8752-8761
    • Vincent, M.1    Brochon, J.C.2    Merola, F.3    Jordi, W.4    Gallay, J.5
  • 34
    • 0025771172 scopus 로고
    • The interactions of horse heart apocytochrome c with phospholipid vesicles and surfactant micelles: Time-resolved fluorescence study of the single tryptophan residue (Trp-59)
    • Vincent M, &, Gallay J, (1991) The interactions of horse heart apocytochrome c with phospholipid vesicles and surfactant micelles: time-resolved fluorescence study of the single tryptophan residue (Trp-59). Eur Biophys J 20, 183-191.
    • (1991) Eur Biophys J , vol.20 , pp. 183-191
    • Vincent, M.1    Gallay, J.2
  • 35
    • 0028672799 scopus 로고
    • Maximum entropy method of data analysis in time-resolved spectroscopy
    • Brochon JC, (1994) Maximum entropy method of data analysis in time-resolved spectroscopy. Methods Enzymol 240, 262-311.
    • (1994) Methods Enzymol , vol.240 , pp. 262-311
    • Brochon, J.C.1
  • 36
    • 0017729574 scopus 로고
    • A theory of fluorescence polarization decay in membranes
    • Kinosita K Jr, Kawato S, &, Ikegami A, (1977) A theory of fluorescence polarization decay in membranes. Biophys J 20, 289-305.
    • (1977) Biophys J , vol.20 , pp. 289-305
    • Kinosita Jr., K.1    Kawato, S.2    Ikegami, A.3


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