메뉴 건너뛰기




Volumn 376, Issue 1, 2008, Pages 120-130

Oxidation-sensitive Residues Mediate the DNA Bending Abilities of the Architectural MC1 Protein

Author keywords

DNA bending; mass spectrometry; oxidative stress; protein oxidation; protein DNA interaction

Indexed keywords

ALANINE; CHROMOSOME PROTEIN; CURVED DNA; MC1 PROTEIN; METHIONINE DERIVATIVE; TRYPTOPHAN DERIVATIVE; UNCLASSIFIED DRUG;

EID: 38049051084     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.11.057     Document Type: Article
Times cited : (4)

References (40)
  • 1
    • 0030841350 scopus 로고    scopus 로고
    • Protein oxidation in aging, disease, and oxidative stress
    • Berlett B.S., and Stadtman E.R. Protein oxidation in aging, disease, and oxidative stress. J. Biol. Chem. 272 (1997) 20313-20316
    • (1997) J. Biol. Chem. , vol.272 , pp. 20313-20316
    • Berlett, B.S.1    Stadtman, E.R.2
  • 2
    • 0036628724 scopus 로고    scopus 로고
    • Role of oxidative stress and protein oxidation in the aging process
    • Sohal R.S. Role of oxidative stress and protein oxidation in the aging process. Free Radic. Biol. Med. 33 (2002) 37-44
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 37-44
    • Sohal, R.S.1
  • 3
    • 12844278044 scopus 로고    scopus 로고
    • The oxidative environment and protein damage
    • Davies M.J. The oxidative environment and protein damage. Biochim. Biophys. Acta 1703 (2005) 93-109
    • (2005) Biochim. Biophys. Acta , vol.1703 , pp. 93-109
    • Davies, M.J.1
  • 5
    • 0002627604 scopus 로고
    • Radiation chemistry of the liquid state: (1) water and homogeneous aqueous solutions
    • Farhataziz R., and A.J. (Eds), VCH Publishers, New York and Weinheim
    • Buxton G.V. Radiation chemistry of the liquid state: (1) water and homogeneous aqueous solutions. In: Farhataziz R., and A.J. (Eds). Radiation Chemistry. Principles and Applications (1987), VCH Publishers, New York and Weinheim
    • (1987) Radiation Chemistry. Principles and Applications
    • Buxton, G.V.1
  • 6
    • 0030988742 scopus 로고    scopus 로고
    • Biochemistry and pathology of radical-mediated protein oxidation
    • Dean R.T., Fu S., Stocker R., and Davies M.J. Biochemistry and pathology of radical-mediated protein oxidation. Biochem. J. 324 (1997) 1-18
    • (1997) Biochem. J. , vol.324 , pp. 1-18
    • Dean, R.T.1    Fu, S.2    Stocker, R.3    Davies, M.J.4
  • 7
    • 0027183423 scopus 로고
    • Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions
    • Stadtman E.R. Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions. Annu. Rev. Biochem. 62 (1993) 797-821
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 797-821
    • Stadtman, E.R.1
  • 9
    • 25144465204 scopus 로고    scopus 로고
    • Radiolytic modification and reactivity of amino acid residues serving as structural probes for protein footprinting
    • Xu G., and Chance M.R. Radiolytic modification and reactivity of amino acid residues serving as structural probes for protein footprinting. Anal. Chem. 77 (2005) 4549-4555
    • (2005) Anal. Chem. , vol.77 , pp. 4549-4555
    • Xu, G.1    Chance, M.R.2
  • 11
    • 25144445202 scopus 로고    scopus 로고
    • Structural proteomics of macromolecular assemblies using oxidative footprinting and mass spectrometry
    • Guan J.Q., and Chance M.R. Structural proteomics of macromolecular assemblies using oxidative footprinting and mass spectrometry. Trends Biochem. Sci. 30 (2005) 583-592
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 583-592
    • Guan, J.Q.1    Chance, M.R.2
  • 13
    • 28044455847 scopus 로고    scopus 로고
    • High-LET irradiation of a DNA-binding protein: protein-protein and DNA-protein crosslinks
    • Culard F., Bouffard S., and Charlier M. High-LET irradiation of a DNA-binding protein: protein-protein and DNA-protein crosslinks. Radiat. Res. 164 (2005) 774-780
    • (2005) Radiat. Res. , vol.164 , pp. 774-780
    • Culard, F.1    Bouffard, S.2    Charlier, M.3
  • 14
    • 9744245199 scopus 로고    scopus 로고
    • NMR solution structure of the archaebacterial chromosomal protein MC1 reveals a new protein fold
    • Paquet F., Culard F., Barbault F., Maurizot J.C., and Lancelot G. NMR solution structure of the archaebacterial chromosomal protein MC1 reveals a new protein fold. Biochemistry 43 (2004) 14971-14978
    • (2004) Biochemistry , vol.43 , pp. 14971-14978
    • Paquet, F.1    Culard, F.2    Barbault, F.3    Maurizot, J.C.4    Lancelot, G.5
  • 15
    • 0013550357 scopus 로고    scopus 로고
    • DNA bending induced by the archaebacterial histone-like protein MC1
    • Cam E.L., Culard F., Larquet E., Delain E., and Cognet J.A. DNA bending induced by the archaebacterial histone-like protein MC1. J. Mol. Biol. 285 (1999) 1011-1021
    • (1999) J. Mol. Biol. , vol.285 , pp. 1011-1021
    • Cam, E.L.1    Culard, F.2    Larquet, E.3    Delain, E.4    Cognet, J.A.5
  • 16
    • 23044456676 scopus 로고    scopus 로고
    • Atypical recognition of particular DNA sequences by the archaeal chromosomal MC1 protein
    • De Vuyst G., Aci S., Genest D., and Culard F. Atypical recognition of particular DNA sequences by the archaeal chromosomal MC1 protein. Biochemistry 44 (2005) 10369-10377
    • (2005) Biochemistry , vol.44 , pp. 10369-10377
    • De Vuyst, G.1    Aci, S.2    Genest, D.3    Culard, F.4
  • 18
    • 0026692124 scopus 로고
    • Mass spectrometry of peptides and proteins
    • Biemann K. Mass spectrometry of peptides and proteins. Annu. Rev. Biochem. 61 (1992) 977-1010
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 977-1010
    • Biemann, K.1
  • 19
    • 0026490544 scopus 로고
    • Use of gel retardation to analyze protein-nucleic acid interactions
    • Lane D., Prentki P., and Chandler M. Use of gel retardation to analyze protein-nucleic acid interactions. Microbiol. Rev. 56 (1992) 509-528
    • (1992) Microbiol. Rev. , vol.56 , pp. 509-528
    • Lane, D.1    Prentki, P.2    Chandler, M.3
  • 21
    • 0028905146 scopus 로고
    • Conformational changes of DNA minicircles upon the binding of the archaebacterial histone-like protein MC1
    • Toulme F., Le Cam E., Teyssier C., Delain E., Sautiere P., Maurizot J.C., and Culard F. Conformational changes of DNA minicircles upon the binding of the archaebacterial histone-like protein MC1. J. Biol. Chem. 270 (1995) 6286-6291
    • (1995) J. Biol. Chem. , vol.270 , pp. 6286-6291
    • Toulme, F.1    Le Cam, E.2    Teyssier, C.3    Delain, E.4    Sautiere, P.5    Maurizot, J.C.6    Culard, F.7
  • 22
    • 0029934873 scopus 로고    scopus 로고
    • Complementarity of microscopies in the structural analysis of DNA minicircles associated to protein MC1
    • Larquet E., Le Cam E., Fourcade A., Culard F., Furrer P., and Delain E. Complementarity of microscopies in the structural analysis of DNA minicircles associated to protein MC1. C.R. Acad. Sci. III 319 (1996) 461-471
    • (1996) C.R. Acad. Sci. III , vol.319 , pp. 461-471
    • Larquet, E.1    Le Cam, E.2    Fourcade, A.3    Culard, F.4    Furrer, P.5    Delain, E.6
  • 23
    • 0032540302 scopus 로고    scopus 로고
    • Direct versus indirect readout in the interaction of the trp repressor with non-canonical binding sites
    • Bareket-Samish A., Cohen I., and Haran T.E. Direct versus indirect readout in the interaction of the trp repressor with non-canonical binding sites. J. Mol. Biol. 277 (1998) 1071-1080
    • (1998) J. Mol. Biol. , vol.277 , pp. 1071-1080
    • Bareket-Samish, A.1    Cohen, I.2    Haran, T.E.3
  • 24
    • 0031791713 scopus 로고    scopus 로고
    • Identification of tryptophan oxidation products in bovine alpha-crystallin
    • Finley E.L., Dillon J., Crouch R.K., and Schey K.L. Identification of tryptophan oxidation products in bovine alpha-crystallin. Protein Sci. 7 (1998) 2391-2397
    • (1998) Protein Sci. , vol.7 , pp. 2391-2397
    • Finley, E.L.1    Dillon, J.2    Crouch, R.K.3    Schey, K.L.4
  • 25
    • 17644406754 scopus 로고    scopus 로고
    • Radiolytic modification of sulfur-containing amino acid residues in model peptides: fundamental studies for protein footprinting
    • Xu G., and Chance M.R. Radiolytic modification of sulfur-containing amino acid residues in model peptides: fundamental studies for protein footprinting. Anal. Chem. 77 (2005) 2437-2449
    • (2005) Anal. Chem. , vol.77 , pp. 2437-2449
    • Xu, G.1    Chance, M.R.2
  • 27
    • 0026787523 scopus 로고
    • Global features of DNA structure by comparative gel electrophoresis
    • Crothers D.M., and Drak J. Global features of DNA structure by comparative gel electrophoresis. Methods Enzymol. 212 (1992) 46-71
    • (1992) Methods Enzymol. , vol.212 , pp. 46-71
    • Crothers, D.M.1    Drak, J.2
  • 28
    • 0029954441 scopus 로고    scopus 로고
    • Preferential binding of the archaebacterial histone-like MC1 protein to negatively supercoiled DNA minicircles
    • Teyssier C., Toulme F., Touzel J.P., Gervais A., Maurizot J.C., and Culard F. Preferential binding of the archaebacterial histone-like MC1 protein to negatively supercoiled DNA minicircles. Biochemistry 35 (1996) 7954-7958
    • (1996) Biochemistry , vol.35 , pp. 7954-7958
    • Teyssier, C.1    Toulme, F.2    Touzel, J.P.3    Gervais, A.4    Maurizot, J.C.5    Culard, F.6
  • 29
    • 3042621005 scopus 로고    scopus 로고
    • Nucleosome conformational flexibility and implications for chromatin dynamics
    • Sivolob A., and Prunell A. Nucleosome conformational flexibility and implications for chromatin dynamics. Phil. Trans. A: Math. Phys. Eng. Sci. 362 (2004) 1519-1547
    • (2004) Phil. Trans. A: Math. Phys. Eng. Sci. , vol.362 , pp. 1519-1547
    • Sivolob, A.1    Prunell, A.2
  • 31
    • 0032539630 scopus 로고    scopus 로고
    • DNA-binding domains of Fos and Jun do not induce DNA curvature: an investigation with solution and gel methods
    • Sitlani A., and Crothers D.M. DNA-binding domains of Fos and Jun do not induce DNA curvature: an investigation with solution and gel methods. Proc. Natl Acad. Sci. USA 95 (1998) 1404-1409
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 1404-1409
    • Sitlani, A.1    Crothers, D.M.2
  • 32
    • 0030610119 scopus 로고    scopus 로고
    • Oxidation of a critical methionine modulates DNA binding of the Drosophila melanogaster high mobility group protein, HMG-D
    • Dow L.K., Changela A., Hefner H.E., and Churchill M.E. Oxidation of a critical methionine modulates DNA binding of the Drosophila melanogaster high mobility group protein, HMG-D. FEBS Letters 414 (1997) 514-520
    • (1997) FEBS Letters , vol.414 , pp. 514-520
    • Dow, L.K.1    Changela, A.2    Hefner, H.E.3    Churchill, M.E.4
  • 33
    • 0037592865 scopus 로고    scopus 로고
    • The role of intercalating residues in chromosomal high-mobility-group protein DNA binding, bending and specificity
    • Klass J., Murphy F.V.t., Fouts S., Serenil M., Changela A., Siple J., and Churchill M.E. The role of intercalating residues in chromosomal high-mobility-group protein DNA binding, bending and specificity. Nucl. Acids Res. 31 (2003) 2852-2864
    • (2003) Nucl. Acids Res. , vol.31 , pp. 2852-2864
    • Klass, J.1    Murphy, F.V.t.2    Fouts, S.3    Serenil, M.4    Changela, A.5    Siple, J.6    Churchill, M.E.7
  • 34
    • 0031830815 scopus 로고    scopus 로고
    • Minor groove-binding architectural proteins: structure, function, and DNA recognition
    • Bewley C.A., Gronenborn A.M., and Clore G.M. Minor groove-binding architectural proteins: structure, function, and DNA recognition. Annu. Rev. Biophys. Biomol. Struct. 27 (1998) 105-131
    • (1998) Annu. Rev. Biophys. Biomol. Struct. , vol.27 , pp. 105-131
    • Bewley, C.A.1    Gronenborn, A.M.2    Clore, G.M.3
  • 35
    • 12344293866 scopus 로고    scopus 로고
    • Structures of the hyperthermophilic chromosomal protein Sac7d in complex with DNA decamers
    • Ko T.P., Chu H.M., Chen C.Y., Chou C.C., and Wang A.H. Structures of the hyperthermophilic chromosomal protein Sac7d in complex with DNA decamers. Acta Crystallog. sect. D 60 (2004) 1381-1387
    • (2004) Acta Crystallog. sect. D , vol.60 , pp. 1381-1387
    • Ko, T.P.1    Chu, H.M.2    Chen, C.Y.3    Chou, C.C.4    Wang, A.H.5
  • 36
    • 15444375819 scopus 로고    scopus 로고
    • Effect of mutation of the Sac7d intercalating residues on the temperature dependence of DNA distortion and binding thermodynamics
    • Peters W.B., Edmondson S.P., and Shriver J.W. Effect of mutation of the Sac7d intercalating residues on the temperature dependence of DNA distortion and binding thermodynamics. Biochemistry 44 (2005) 4794-4804
    • (2005) Biochemistry , vol.44 , pp. 4794-4804
    • Peters, W.B.1    Edmondson, S.P.2    Shriver, J.W.3
  • 37
    • 12344302072 scopus 로고    scopus 로고
    • Role of a surface tryptophan in defining the structure, stability, and DNA binding of the hyperthermophile protein Sac7d
    • Bedell J.L., Edmondson S.P., and Shriver J.W. Role of a surface tryptophan in defining the structure, stability, and DNA binding of the hyperthermophile protein Sac7d. Biochemistry 44 (2005) 915-925
    • (2005) Biochemistry , vol.44 , pp. 915-925
    • Bedell, J.L.1    Edmondson, S.P.2    Shriver, J.W.3
  • 38
    • 0035281548 scopus 로고    scopus 로고
    • HMG1 and 2, and related 'architectural' DNA-binding proteins
    • Thomas J.O., and Travers A.A. HMG1 and 2, and related 'architectural' DNA-binding proteins. Trends Biochem. Sci. 26 (2001) 167-174
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 167-174
    • Thomas, J.O.1    Travers, A.A.2
  • 39
    • 33745242847 scopus 로고    scopus 로고
    • Structure of a complex of tandem HMG boxes and DNA
    • Stott K., Tang G.S., Lee K.B., and Thomas J.O. Structure of a complex of tandem HMG boxes and DNA. J. Mol. Biol. 360 (2006) 90-104
    • (2006) J. Mol. Biol. , vol.360 , pp. 90-104
    • Stott, K.1    Tang, G.S.2    Lee, K.B.3    Thomas, J.O.4
  • 40
    • 0034669677 scopus 로고    scopus 로고
    • A robust, detergent-friendly method for mass spectrometric analysis of integral membrane proteins
    • Cadene M., and Chait B.T. A robust, detergent-friendly method for mass spectrometric analysis of integral membrane proteins. Anal. Chem. 72 (2000) 5655-5658
    • (2000) Anal. Chem. , vol.72 , pp. 5655-5658
    • Cadene, M.1    Chait, B.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.