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Volumn 47, Issue 49, 2008, Pages 13046-13055

Methodology to probe subunit interactions in ribonucleotide reductases

Author keywords

[No Author keywords available]

Indexed keywords

AMINES; AMINO ACIDS; BACKPROPAGATION; COLLOIDS; DIFFUSERS (OPTICAL); ELECTROPHORESIS; ELECTROSPRAY IONIZATION; ESCHERICHIA COLI; FLUORESCENCE; GELATION; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; LIGHT EMISSION; LUMINESCENCE; MASS SPECTROMETRY; NUCLEIC ACIDS; ORGANIC ACIDS; POLYMERS; PORT TERMINALS; SODIUM; SODIUM SULFATE; VOLUMETRIC ANALYSIS;

EID: 57449084394     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi8012559     Document Type: Article
Times cited : (14)

References (44)
  • 1
    • 0032023777 scopus 로고    scopus 로고
    • Protein radicals in enzyme catalysis
    • Stubbe, J., and van der Donk, W. A. (1998) Protein radicals in enzyme catalysis. Chem. Rev. 98, 705-762.
    • (1998) Chem. Rev , vol.98 , pp. 705-762
    • Stubbe, J.1    van der Donk, W.A.2
  • 3
    • 35448984575 scopus 로고    scopus 로고
    • Enhanced subunit interactions with gemcitabine-5′-diphosphate inhibit ribonucleotide reductases
    • Wang, J., Lohman, G. J. S., and Stubbe, J. (2007) Enhanced subunit interactions with gemcitabine-5′-diphosphate inhibit ribonucleotide reductases. Proc. Natl. Acad. Sci. U.S.A. 104, 14324-14329.
    • (2007) Proc. Natl. Acad. Sci. U.S.A , vol.104 , pp. 14324-14329
    • Wang, J.1    Lohman, G.J.S.2    Stubbe, J.3
  • 4
    • 0014694233 scopus 로고
    • Ribonucleoside diphosphate reductase: Formation of active and inactive complexes of proteins B1 and B2
    • Brown, N. C., and Reichard, P. (1969) Ribonucleoside diphosphate reductase: Formation of active and inactive complexes of proteins B1 and B2. J. Mol. Biol. 46, 25-38.
    • (1969) J. Mol. Biol , vol.46 , pp. 25-38
    • Brown, N.C.1    Reichard, P.2
  • 5
    • 0015850211 scopus 로고
    • Physicochemical characterization of ribonucleoside diphosphate reductase from Escherichia coli
    • Thelander, L. (1973) Physicochemical characterization of ribonucleoside diphosphate reductase from Escherichia coli. J. Biol. Chem. 248, 4591-4601.
    • (1973) J. Biol. Chem , vol.248 , pp. 4591-4601
    • Thelander, L.1
  • 6
    • 0017615856 scopus 로고
    • Nature of free-radical in ribonucleotide reductase from Escherichia coli
    • Sjöberg, B. M., Reichard, P., Gräslund, A., and Ehrenberg, A. (1977) Nature of free-radical in ribonucleotide reductase from Escherichia coli. J. Biol. Chem. 252, 536-541.
    • (1977) J. Biol. Chem , vol.252 , pp. 536-541
    • Sjöberg, B.M.1    Reichard, P.2    Gräslund, A.3    Ehrenberg, A.4
  • 7
    • 0018135309 scopus 로고
    • Tyrosine free-radical in ribonucleotide reductase from Escherichia coli
    • Sjöberg, B. M., Reichard, P., Gräslund, A., and Ehrenberg, A. (1978) Tyrosine free-radical in ribonucleotide reductase from Escherichia coli. J. Biol. Chem. 253, 6863-6865.
    • (1978) J. Biol. Chem , vol.253 , pp. 6863-6865
    • Sjöberg, B.M.1    Reichard, P.2    Gräslund, A.3    Ehrenberg, A.4
  • 8
    • 0028486194 scopus 로고
    • Structure of ribonucleotide reductase protein R1
    • Uhlin, U., and Eklund, H. (1994) Structure of ribonucleotide reductase protein R1. Nature 370, 533-539.
    • (1994) Nature , vol.370 , pp. 533-539
    • Uhlin, U.1    Eklund, H.2
  • 9
    • 33646176383 scopus 로고    scopus 로고
    • The first holocomplex structure of ribonucleotide reductase gives new insight into its mechanism of action
    • Uppsten, M., Farnegardh, M., Domkin, V., and Uhlin, U. (2006) The first holocomplex structure of ribonucleotide reductase gives new insight into its mechanism of action. J. Mol. Biol. 359, 365-377.
    • (2006) J. Mol. Biol , vol.359 , pp. 365-377
    • Uppsten, M.1    Farnegardh, M.2    Domkin, V.3    Uhlin, U.4
  • 11
    • 0027283896 scopus 로고
    • Structure and function of the Escherichia coli ribonucleotide reductase protein R2
    • Nordlund, P., and Eklund, H. (1993) Structure and function of the Escherichia coli ribonucleotide reductase protein R2. J. Mol. Biol. 232, 123-164.
    • (1993) J. Mol. Biol , vol.232 , pp. 123-164
    • Nordlund, P.1    Eklund, H.2
  • 12
    • 0025293287 scopus 로고
    • Three-dimensional structure of the free radical protein of ribonucleotide reductase
    • Nordlund, P., Sjöberg, B. M., and Eklund, H. (1990) Three-dimensional structure of the free radical protein of ribonucleotide reductase. Nature 345, 593-598.
    • (1990) Nature , vol.345 , pp. 593-598
    • Nordlund, P.1    Sjöberg, B.M.2    Eklund, H.3
  • 13
    • 0031571616 scopus 로고    scopus 로고
    • Binding of allosteric effectors to ribonucleotide reductase protein R1: Reduction of active-site cysteines promotes substrate binding
    • Eriksson, M., Uhlin, U., Ramaswamy, S., Ekberg, M., Regnstrom, K., Sjöberg, B. M., and Eklund, H. (1997) Binding of allosteric effectors to ribonucleotide reductase protein R1: reduction of active-site cysteines promotes substrate binding. Structure 5, 1077-1092.
    • (1997) Structure , vol.5 , pp. 1077-1092
    • Eriksson, M.1    Uhlin, U.2    Ramaswamy, S.3    Ekberg, M.4    Regnstrom, K.5    Sjöberg, B.M.6    Eklund, H.7
  • 14
    • 27544491667 scopus 로고    scopus 로고
    • EPR distance measurements support a model for long-range radical initiation in Escherichia coli ribonucleotide reductase
    • Bennati, M., Robblee, J. H., Mugnaini, V., Stubbe, J., Freed, J. H., and Borbat, P. (2005) EPR distance measurements support a model for long-range radical initiation in Escherichia coli ribonucleotide reductase. J. Am. Chem. Soc. 127, 15014-15015.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 15014-15015
    • Bennati, M.1    Robblee, J.H.2    Mugnaini, V.3    Stubbe, J.4    Freed, J.H.5    Borbat, P.6
  • 15
    • 37549042071 scopus 로고    scopus 로고
    • PELDOR spectroscopy with DOPA-β2 and NH2Y-α2s: Distance measurements between residues involved in the radical propagation pathway of Escherichia coli ribonucleotide reductase
    • Seyedsayamdost, M. R., Chan, C. T. Y., Mugnaini, V., Stubbe, J., and Bennati, M. (2007) PELDOR spectroscopy with DOPA-β2 and NH2Y-α2s: Distance measurements between residues involved in the radical propagation pathway of Escherichia coli ribonucleotide reductase. J. Am. Chem. Soc. 129, 15748-15749.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 15748-15749
    • Seyedsayamdost, M.R.1    Chan, C.T.Y.2    Mugnaini, V.3    Stubbe, J.4    Bennati, M.5
  • 16
    • 0022455333 scopus 로고
    • Specific-inhibition of herpesvirus ribonucleotide reductase by a nonapeptide derived from the carboxy terminus of subunit-2
    • Cohen, E. A., Gaudreau, P., Brazeau, P., and Langelier, Y. (1986) Specific-inhibition of herpesvirus ribonucleotide reductase by a nonapeptide derived from the carboxy terminus of subunit-2. Nature 321, 441-443.
    • (1986) Nature , vol.321 , pp. 441-443
    • Cohen, E.A.1    Gaudreau, P.2    Brazeau, P.3    Langelier, Y.4
  • 17
    • 0038796547 scopus 로고    scopus 로고
    • Oligopeptide inhibition of class I ribonucleotide reductases
    • Cooperman, B. S. (2003) Oligopeptide inhibition of class I ribonucleotide reductases. Biopolymers 71, 117-131.
    • (2003) Biopolymers , vol.71 , pp. 117-131
    • Cooperman, B.S.1
  • 18
    • 0025851264 scopus 로고
    • Carboxyl-terminal peptides as probes for Escherichia coli ribonucleotide reductase subunit interaction - kinetic-analysis of inhibition studies
    • Climent, I., Sjöberg, B. M., and Huang, C. Y. (1991) Carboxyl-terminal peptides as probes for Escherichia coli ribonucleotide reductase subunit interaction - kinetic-analysis of inhibition studies. Biochemistry 30, 5164-5171.
    • (1991) Biochemistry , vol.30 , pp. 5164-5171
    • Climent, I.1    Sjöberg, B.M.2    Huang, C.Y.3
  • 19
    • 0029896950 scopus 로고    scopus 로고
    • A kinetic study on the influence of nucleoside triphosphate effectors on subunit interaction in mouse ribonucleotide reductase
    • Ingemarson, R., and Thelander, L. (1996) A kinetic study on the influence of nucleoside triphosphate effectors on subunit interaction in mouse ribonucleotide reductase. Biochemistry 35, 8603-8609.
    • (1996) Biochemistry , vol.35 , pp. 8603-8609
    • Ingemarson, R.1    Thelander, L.2
  • 20
    • 3843050352 scopus 로고    scopus 로고
    • Enhancement by effectors and substrate nucleotides of R1-R2 interactions in Escherichia coli class Ia ribonucleotide reductase
    • Kasrayan, A., Birgander, P. L., Pappalardo, L., Regnstrom, K., Westman, M., Slaby, A., Gordon, E., and Sjöberg, B. M. (2004) Enhancement by effectors and substrate nucleotides of R1-R2 interactions in Escherichia coli class Ia ribonucleotide reductase. J. Biol. Chem. 279, 31050-31057.
    • (2004) J. Biol. Chem , vol.279 , pp. 31050-31057
    • Kasrayan, A.1    Birgander, P.L.2    Pappalardo, L.3    Regnstrom, K.4    Westman, M.5    Slaby, A.6    Gordon, E.7    Sjöberg, B.M.8
  • 21
    • 0026652152 scopus 로고
    • Site-directed mutagenesis and deletion of the carboxyl terminus of Escherichia coli ribonucleotide reductase protein R2 - effects on catalytic activity and subunit interaction
    • Climent, I., Sjöberg, B. M., and Huang, C. Y. (1992) Site-directed mutagenesis and deletion of the carboxyl terminus of Escherichia coli ribonucleotide reductase protein R2 - effects on catalytic activity and subunit interaction. Biochemistry 31, 4801-4807.
    • (1992) Biochemistry , vol.31 , pp. 4801-4807
    • Climent, I.1    Sjöberg, B.M.2    Huang, C.Y.3
  • 22
    • 0021811719 scopus 로고
    • Direct cloning of the trxB gene that encodes thioredoxin reductase
    • Russel, M., and Model, P. (1985) Direct cloning of the trxB gene that encodes thioredoxin reductase. J. Bacteriol. 163, 238-242.
    • (1985) J. Bacteriol , vol.163 , pp. 238-242
    • Russel, M.1    Model, P.2
  • 23
    • 0021256117 scopus 로고
    • Amplification and purification of plasmid-encoded thioredoxin from Escherichia coli K12
    • Lunn, C. A., Kathju, S., Wallace, B. J., Kushner, S. R., and Pigiet, V. (1984) Amplification and purification of plasmid-encoded thioredoxin from Escherichia coli K12. J. Biol. Chem. 259, 10469-10474.
    • (1984) J. Biol. Chem , vol.259 , pp. 10469-10474
    • Lunn, C.A.1    Kathju, S.2    Wallace, B.J.3    Kushner, S.R.4    Pigiet, V.5
  • 24
    • 0348111211 scopus 로고    scopus 로고
    • Generation of the β2 subunit of ribonucleotide reductase by intein chemistry: Insertion of 3-nitrotyrosine at residue 356 as a probe of the radical initiation process
    • Yee, C. S., Seyedsayamdost, M. R., Chang, M. C. Y., Nocera, D. G., and Stubbe, J. (2003) Generation of the β2 subunit of ribonucleotide reductase by intein chemistry: Insertion of 3-nitrotyrosine at residue 356 as a probe of the radical initiation process. Biochemistry 42, 14541-14552.
    • (2003) Biochemistry , vol.42 , pp. 14541-14552
    • Yee, C.S.1    Seyedsayamdost, M.R.2    Chang, M.C.Y.3    Nocera, D.G.4    Stubbe, J.5
  • 25
    • 0034645606 scopus 로고    scopus 로고
    • Mechanism of rapid electron transfer during oxygen activation in the R2 subunit of Escherichia coli ribonucleotide reductase. 1. Evidence for a transient tryptophan radical
    • Baldwin, J., Krebs, C., Ley, B. A., Edmondson, D. E., Huynh, B. H., and Bollinger, J. M. J. (2000) Mechanism of rapid electron transfer during oxygen activation in the R2 subunit of Escherichia coli ribonucleotide reductase. 1. Evidence for a transient tryptophan radical. J. Am. Chem. Soc. 122, 12195-12206.
    • (2000) J. Am. Chem. Soc , vol.122 , pp. 12195-12206
    • Baldwin, J.1    Krebs, C.2    Ley, B.A.3    Edmondson, D.E.4    Huynh, B.H.5    Bollinger, J.M.J.6
  • 26
    • 0029157059 scopus 로고    scopus 로고
    • Bollinger, J. M., Tong, W. H., Ravi, N., Huynh, B. H., Edmondson, D. E., and Stubbe, J. (1995) Use of rapid kinetics methods to study the assembly of the diferric-tyrosyl radical cofactor of Escherichia coli ribonucleotide reductase, in. Methods Enzymol. 258, 278-303.
    • Bollinger, J. M., Tong, W. H., Ravi, N., Huynh, B. H., Edmondson, D. E., and Stubbe, J. (1995) Use of rapid kinetics methods to study the assembly of the diferric-tyrosyl radical cofactor of Escherichia coli ribonucleotide reductase, in. Methods Enzymol. 258, 278-303.
  • 27
    • 0026801085 scopus 로고
    • A model for the role of multiple cysteine residues involved in ribonucleotide reduction - amazing and still confusing
    • Mao, S. S., Holler, T. P., Yu, G. X., Bollinger, J. M., Booker, S., Johnston, M. I., and Stubbe, J. (1992) A model for the role of multiple cysteine residues involved in ribonucleotide reduction - amazing and still confusing. Biochemistry 31, 9733-9743.
    • (1992) Biochemistry , vol.31 , pp. 9733-9743
    • Mao, S.S.1    Holler, T.P.2    Yu, G.X.3    Bollinger, J.M.4    Booker, S.5    Johnston, M.I.6    Stubbe, J.7
  • 28
    • 0014759788 scopus 로고
    • A rapid assay for CDP reductase activity in mammalian cell extracts
    • Steeper, J. R., and Steuart, C. D. (1970) A rapid assay for CDP reductase activity in mammalian cell extracts. Anal. Biochem. 34, 123-130.
    • (1970) Anal. Biochem , vol.34 , pp. 123-130
    • Steeper, J.R.1    Steuart, C.D.2
  • 30
    • 0030023342 scopus 로고    scopus 로고
    • Spectral properties of environmentally sensitive probes associated with horseradish peroxidase
    • Lasagna, M., Vargas, V., Jameson, D. M., and Brunet, J. E. (1996) Spectral properties of environmentally sensitive probes associated with horseradish peroxidase. Biochemistry 35, 973-979.
    • (1996) Biochemistry , vol.35 , pp. 973-979
    • Lasagna, M.1    Vargas, V.2    Jameson, D.M.3    Brunet, J.E.4
  • 31
    • 0023918636 scopus 로고
    • An exact correction to the Cheng-Prusoff correction
    • Munson, P. J., and Rodbard, D. (1988) An exact correction to the Cheng-Prusoff correction. J. Recept. Res. 8, 533-546.
    • (1988) J. Recept. Res , vol.8 , pp. 533-546
    • Munson, P.J.1    Rodbard, D.2
  • 32
    • 0015861774 scopus 로고
    • Relationship between inhibition constant (KI) and concentration of inhibitor which causes 50% inhibition (I50) of an enzymatic-reaction
    • Cheng, Y., and Prusoff, W. H. (1973) Relationship between inhibition constant (KI) and concentration of inhibitor which causes 50% inhibition (I50) of an enzymatic-reaction. Biochem. Pharmacol. 22, 3099-3108.
    • (1973) Biochem. Pharmacol , vol.22 , pp. 3099-3108
    • Cheng, Y.1    Prusoff, W.H.2
  • 34
    • 0028235205 scopus 로고
    • Benzophenone photophores in biochemistry
    • Dorman, G., and Prestwich, G. D. (1994) Benzophenone photophores in biochemistry. Biochemistry 33, 5661-5673.
    • (1994) Biochemistry , vol.33 , pp. 5661-5673
    • Dorman, G.1    Prestwich, G.D.2
  • 35
    • 0000736085 scopus 로고
    • Preparation, crystalline-structure, and spectral properties of fluorescent-probe 4,4-bis-1-phenylamino-8-naphthalenesulfonate
    • Farris, F. J., Weber, G., Chiang, C. C., and Paul, I. C. (1978) Preparation, crystalline-structure, and spectral properties of fluorescent-probe 4,4-bis-1-phenylamino-8-naphthalenesulfonate. J. Am. Chem. Soc. 100, 4469-4474.
    • (1978) J. Am. Chem. Soc , vol.100 , pp. 4469-4474
    • Farris, F.J.1    Weber, G.2    Chiang, C.C.3    Paul, I.C.4
  • 36
    • 57449092546 scopus 로고    scopus 로고
    • Ph.D. Thesis, MIT, Cambridge, MA
    • Yee, C. S. (2004) Ph.D. Thesis, MIT, Cambridge, MA.
    • (2004)
    • Yee, C.S.1
  • 37
    • 0028176923 scopus 로고
    • 1H-NMR studies of mouse ribonucleotide reductase - the R2 protein carboxyl-terminal tail, essential for subunit interaction, is highly flexible but becomes rigid in the presence of protein R1
    • Lycksell, P. O., Ingemarson, R., Davis, R., Gräslund, A., and Thelander, L. (1994) 1H-NMR studies of mouse ribonucleotide reductase - the R2 protein carboxyl-terminal tail, essential for subunit interaction, is highly flexible but becomes rigid in the presence of protein R1. Biochemistry 33, 2838-2842.
    • (1994) Biochemistry , vol.33 , pp. 2838-2842
    • Lycksell, P.O.1    Ingemarson, R.2    Davis, R.3    Gräslund, A.4    Thelander, L.5
  • 38
    • 0029126928 scopus 로고
    • Demonstration of segmental mobility in the functionally essential carboxyl-terminal part of ribonucleotide reductase protein R2 from Escherichia coli
    • Lycksell, P. O., and Sahlin, M. (1995) Demonstration of segmental mobility in the functionally essential carboxyl-terminal part of ribonucleotide reductase protein R2 from Escherichia coli. FEBS Lett. 368, 441-444.
    • (1995) FEBS Lett , vol.368 , pp. 441-444
    • Lycksell, P.O.1    Sahlin, M.2
  • 39
    • 33847666363 scopus 로고    scopus 로고
    • Forward and reverse electron transfer with the Y(356)DOPA-β2 heterodimer of Escherichia coli ribonucleotide reductase
    • Seyedsayamdost, M. R., and Stubbe, J. (2007) Forward and reverse electron transfer with the Y(356)DOPA-β2 heterodimer of Escherichia coli ribonucleotide reductase. J. Am. Chem. Soc. 129, 2226-2227.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 2226-2227
    • Seyedsayamdost, M.R.1    Stubbe, J.2
  • 40
    • 0023655427 scopus 로고
    • Half-site reactivity of the tyrosyl radical of ribonucleotide reductase from Escherichia coli
    • Sjöberg, B. M., Karlsson, M., and Jornvall, H. (1987) Half-site reactivity of the tyrosyl radical of ribonucleotide reductase from Escherichia coli. J. Biol. Chem. 262, 9736-9743.
    • (1987) J. Biol. Chem , vol.262 , pp. 9736-9743
    • Sjöberg, B.M.1    Karlsson, M.2    Jornvall, H.3
  • 41
    • 55249116734 scopus 로고    scopus 로고
    • Mapping the subunit interface of ribonucleotide reductase (RNR) using photo-cross-linking
    • in press
    • Hassan, A. Q., and Stubbe, J. (2008) Mapping the subunit interface of ribonucleotide reductase (RNR) using photo-cross-linking. Bioorg. Med. Chem. Lett., in press.
    • (2008) Bioorg. Med. Chem. Lett
    • Hassan, A.Q.1    Stubbe, J.2
  • 42
    • 0018786922 scopus 로고
    • Synthesis and spectral properties of a hydrophobic fluorescent-probe - 6-propionyl-2-(dimethylamino)Naphthalene
    • Weber, G., and Farris, F. J. (1979) Synthesis and spectral properties of a hydrophobic fluorescent-probe - 6-propionyl-2-(dimethylamino)Naphthalene. Biochemistry 18, 3075-3078.
    • (1979) Biochemistry , vol.18 , pp. 3075-3078
    • Weber, G.1    Farris, F.J.2
  • 44
    • 57449118316 scopus 로고    scopus 로고
    • New peptide inhibitors of mammalian ribonucleotide reductase. Mechanisms of action
    • Gao, Y., Tan, C., Kashlan, O. B., Kaur, J., and Cooperman, B. S. (2004) New peptide inhibitors of mammalian ribonucleotide reductase. Mechanisms of action. Regul. Pept. 122, 14-14.
    • (2004) Regul. Pept , vol.122 , pp. 14-14
    • Gao, Y.1    Tan, C.2    Kashlan, O.B.3    Kaur, J.4    Cooperman, B.S.5


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