메뉴 건너뛰기




Volumn 45, Issue 20, 2006, Pages 6260-6266

Measurement of multisite oxidation kinetics reveals an active site conformational change in Spo0F as a result of protein oxidation

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONS; MASS SPECTROMETRY; OXIDATION; PROTEINS; STOICHIOMETRY;

EID: 33646864750     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi060470r     Document Type: Article
Times cited : (29)

References (27)
  • 1
    • 0002463721 scopus 로고    scopus 로고
    • Oxidative Stress
    • (Strorz, G., and Hengge-Aronis, R., Eds.), ASM Press, Washington, DC
    • Storz, G., and Zheng, M. (2000) Oxidative Stress, in Bacterial Stress Responses (Strorz, G., and Hengge-Aronis, R., Eds.) pp 47-59, ASM Press, Washington, DC.
    • (2000) Bacterial Stress Responses , pp. 47-59
    • Storz, G.1    Zheng, M.2
  • 2
    • 3042775733 scopus 로고    scopus 로고
    • Intracellular reactive oxygen species mediate suppression of sporulation in Bacillus subtilis under shear stress
    • Sahoo, S., Rao, K. K., Suresh, A. K., and Suraishkumar, G. K. (2004) Intracellular reactive oxygen species mediate suppression of sporulation in Bacillus subtilis under shear stress, Biotechnol. Bioeng. 87, 81-9.
    • (2004) Biotechnol. Bioeng. , vol.87 , pp. 81-89
    • Sahoo, S.1    Rao, K.K.2    Suresh, A.K.3    Suraishkumar, G.K.4
  • 3
    • 1842613501 scopus 로고    scopus 로고
    • Regulation of endospore formation in Bacillus subtilis
    • Errington, J. (2003) Regulation of endospore formation in Bacillus subtilis, Nat. Rev. Microbiol. 1, 117-26.
    • (2003) Nat. Rev. Microbiol. , vol.1 , pp. 117-126
    • Errington, J.1
  • 4
    • 0023490127 scopus 로고
    • Relationship among oxidative stress, growth cycle, and sporulation in Bacillus subtilis
    • Dowds, B. C., Murphy, P., McConnell, D. J., and Devine, K. M. (1987) Relationship among oxidative stress, growth cycle, and sporulation in Bacillus subtilis, J. Bacteriol. 169, 5771-5.
    • (1987) J. Bacteriol. , vol.169 , pp. 5771-5775
    • Dowds, B.C.1    Murphy, P.2    McConnell, D.J.3    Devine, K.M.4
  • 5
    • 0002868568 scopus 로고
    • DNA repair systems
    • (Sonenshein, A. L., Hoch, J. A., and Losick, R., Eds.), ASM Press, Washington, DC
    • Yasbin, R. E., Cheo, D., and Bol, D. (1993) DNA Repair Systems, in Bacillus subtilis and Other Gram-Positive Bacteria (Sonenshein, A. L., Hoch, J. A., and Losick, R., Eds.) pp 529-37, ASM Press, Washington, DC.
    • (1993) Bacillus Subtilis and Other Gram-Positive Bacteria , pp. 529-537
    • Yasbin, R.E.1    Cheo, D.2    Bol, D.3
  • 6
    • 0025964291 scopus 로고
    • Initiation of sporulation in B. subtilis is controlled by a multicomponent phosphorelay
    • Burbulys, D., Trach, K. A., and Hoch, J. A. (1991) Initiation of sporulation in B. subtilis is controlled by a multicomponent phosphorelay, Cell 64, 545-52.
    • (1991) Cell , vol.64 , pp. 545-552
    • Burbulys, D.1    Trach, K.A.2    Hoch, J.A.3
  • 7
    • 0003030824 scopus 로고    scopus 로고
    • Bacterial sporulation: A response to environmental signals
    • (Storz, G., and Hengge-Aronis, R., Eds.), ASM Press, Washington, DC
    • Sonenshein, A. L. (2000) Bacterial Sporulation: A Response to Environmental Signals, in Bacterial Stress Responses (Storz, G., and Hengge-Aronis, R., Eds.) pp 199-215, ASM Press, Washington, DC.
    • (2000) Bacterial Stress Responses , pp. 199-215
    • Sonenshein, A.L.1
  • 8
    • 0033566242 scopus 로고    scopus 로고
    • Millisecond-timescale motions contribute to the function of the bacterial response regulator protein Spo0F
    • Feher, V. A., and Cavanagh, J. (1999) Millisecond-timescale motions contribute to the function of the bacterial response regulator protein Spo0F, Nature 400, 289-93.
    • (1999) Nature , vol.400 , pp. 289-293
    • Feher, V.A.1    Cavanagh, J.2
  • 9
    • 0028982719 scopus 로고
    • 13C backbone chemical shift assignments, secondary structure, and magnesium-binding characteristics of the Bacillus subtilis response regulator, Spo0F, determined by heteronuclear high-resolution NMR
    • 13C backbone chemical shift assignments, secondary structure, and magnesium-binding characteristics of the Bacillus subtilis response regulator, Spo0F, determined by heteronuclear high-resolution NMR, Protein Sci. 4, 1801-14.
    • (1995) Protein Sci. , vol.4 , pp. 1801-1814
    • Feher, V.A.1    Zapf, J.W.2    Hoch, J.A.3    Dahlquist, F.W.4    Whiteley, J.M.5    Cavanagh, J.6
  • 10
    • 0030850026 scopus 로고    scopus 로고
    • High-resolution NMR structure and backbone dynamics of the Bacillus subtilis response regulator, Spo0F: Implications for phosphorylation and molecular recognition
    • Feher, V. A., Zapf, J. W., Hoch, J. A., Whiteley, J. M., McIntosh, L. P., Ranee, M., Skelton, N. J., Dahlquist, F. W., and Cavanagh, J. (1997) High-resolution NMR structure and backbone dynamics of the Bacillus subtilis response regulator, Spo0F: Implications for phosphorylation and molecular recognition, Biochemistry 36, 10015-25.
    • (1997) Biochemistry , vol.36 , pp. 10015-10025
    • Feher, V.A.1    Zapf, J.W.2    Hoch, J.A.3    Whiteley, J.M.4    McIntosh, L.P.5    Ranee, M.6    Skelton, N.J.7    Dahlquist, F.W.8    Cavanagh, J.9
  • 11
    • 0030813090 scopus 로고    scopus 로고
    • Molecular recognition in signal transduction: The interaction surfaces of the Spo0F response regulator with its cognate phosphorelay proteins revealed by alanine scanning mutagenesis
    • Tzeng, Y. L., and Hoch, J. A. (1997) Molecular recognition in signal transduction: The interaction surfaces of the Spo0F response regulator with its cognate phosphorelay proteins revealed by alanine scanning mutagenesis, J. Mol. Biol. 272, 200-12.
    • (1997) J. Mol. Biol. , vol.272 , pp. 200-212
    • Tzeng, Y.L.1    Hoch, J.A.2
  • 12
    • 0032564389 scopus 로고    scopus 로고
    • Characterization of interactions between a two-component response regulator, Spo0F, and its phosphatase, RapB
    • Tzeng, Y. L., Feher, V. A., Cavanagh, J., Perego, M., and Hoch, J. A. (1998) Characterization of interactions between a two-component response regulator, Spo0F, and its phosphatase, RapB, Biochemistry 37, 16538-45.
    • (1998) Biochemistry , vol.37 , pp. 16538-16545
    • Tzeng, Y.L.1    Feher, V.A.2    Cavanagh, J.3    Perego, M.4    Hoch, J.A.5
  • 13
    • 0034879819 scopus 로고    scopus 로고
    • Keeping signals straight in phosphorelay signal transduction
    • Hoch, J. A., and Varughese, K. I. (2001) Keeping signals straight in phosphorelay signal transduction, J. Bacteriol. 183, 4941-9.
    • (2001) J. Bacteriol. , vol.183 , pp. 4941-4949
    • Hoch, J.A.1    Varughese, K.I.2
  • 14
    • 0035964867 scopus 로고    scopus 로고
    • Unfolding of apomyoglobin examined by synchrotron footprinting
    • Chance, M. R. (2001) Unfolding of apomyoglobin examined by synchrotron footprinting, Biochem. Biophys. Res. Commun. 287, 614-21.
    • (2001) Biochem. Biophys. Res. Commun. , vol.287 , pp. 614-621
    • Chance, M.R.1
  • 15
    • 0842283944 scopus 로고    scopus 로고
    • Analysis of protein solvent accessible surfaces by photochemical oxidation and mass spectrometry
    • Sharp, J. S., Becker, J. M., and Hettich, R. L. (2004) Analysis of protein solvent accessible surfaces by photochemical oxidation and mass spectrometry, Anal. Chem. 76, 672-83.
    • (2004) Anal. Chem. , vol.76 , pp. 672-683
    • Sharp, J.S.1    Becker, J.M.2    Hettich, R.L.3
  • 16
    • 0037442729 scopus 로고    scopus 로고
    • Protein surface mapping by chemical oxidation: Structural analysis by mass spectrometry
    • Sharp, J. S., Becker, J. M., and Hettich, R. L. (2003) Protein surface mapping by chemical oxidation: Structural analysis by mass spectrometry, Anal. Biochem. 313, 216-25.
    • (2003) Anal. Biochem. , vol.313 , pp. 216-225
    • Sharp, J.S.1    Becker, J.M.2    Hettich, R.L.3
  • 17
    • 27844593258 scopus 로고    scopus 로고
    • Laser flash photolysis of hydrogen peroxide to oxidize protein solvent-accessible residues on the microsecond time scale
    • Hambly, D. M., and Gross, M. L. (2005) Laser flash photolysis of hydrogen peroxide to oxidize protein solvent-accessible residues on the microsecond time scale, J. Am. Soc. Mass Spectrom. 16, 2057-63.
    • (2005) J. Am. Soc. Mass Spectrom. , vol.16 , pp. 2057-2063
    • Hambly, D.M.1    Gross, M.L.2
  • 18
    • 0035702274 scopus 로고    scopus 로고
    • Synchrotron protein footprinting: A technique to investigate protein-protein interactions
    • Goldsmith, S. C., Guan, J. Q., Almo, S., and Chance, M. (2001) Synchrotron protein footprinting: A technique to investigate protein-protein interactions, J. Biomol. Struct. Dyn. 19, 405-18.
    • (2001) J. Biomol. Struct. Dyn. , vol.19 , pp. 405-418
    • Goldsmith, S.C.1    Guan, J.Q.2    Almo, S.3    Chance, M.4
  • 19
    • 0035865266 scopus 로고    scopus 로고
    • Determination of macromolecular folding and structure by synchrotron X-ray radiolysis techniques
    • Maleknia, S. D., Ralston, C. Y., Brenowitz, M. D., Downard, K. M., and Chance, M. R. (2001) Determination of macromolecular folding and structure by synchrotron X-ray radiolysis techniques, Anal. Biochem. 289, 103-15.
    • (2001) Anal. Biochem. , vol.289 , pp. 103-115
    • Maleknia, S.D.1    Ralston, C.Y.2    Brenowitz, M.D.3    Downard, K.M.4    Chance, M.R.5
  • 21
    • 0000302143 scopus 로고
    • Reaction mechanisms in the radiolysis of peptides, polypeptides, and proteins
    • Garrison, W. M. (1987) Reaction Mechanisms in the Radiolysis of Peptides, Polypeptides, and Proteins, Chem. Rev. 87, 381-98.
    • (1987) Chem. Rev. , vol.87 , pp. 381-398
    • Garrison, W.M.1
  • 22
    • 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. (2005) Radiolytic modification and reactivity of amino acid residues serving as structural probes for protein footprinting, Anal. Chem. 77, 4549-55.
    • (2005) Anal. Chem. , vol.77 , pp. 4549-4555
    • Xu, G.1    Chance, M.R.2
  • 23
    • 0029883898 scopus 로고    scopus 로고
    • A phosphotransferase activity of the Bacillus subtilis sporulation protein Spo0F that employs phosphoramidate substrates
    • Zapf, J. W., Hoch, J. A., and Whiteley, J. M. (1996) A phosphotransferase activity of the Bacillus subtilis sporulation protein Spo0F that employs phosphoramidate substrates, Biochemistry 35, 2926-33.
    • (1996) Biochemistry , vol.35 , pp. 2926-2933
    • Zapf, J.W.1    Hoch, J.A.2    Whiteley, J.M.3
  • 24
    • 18844415551 scopus 로고    scopus 로고
    • Secondary reactions and strategies to improve quantitative protein footprinting
    • Xu, G., Kiselar, J., He, Q., and Chance, M. R. (2005) Secondary reactions and strategies to improve quantitative protein footprinting, Anal. Chem. 77, 3029-37.
    • (2005) Anal. Chem. , vol.77 , pp. 3029-3037
    • Xu, G.1    Kiselar, J.2    He, Q.3    Chance, M.R.4
  • 25
    • 0030585421 scopus 로고    scopus 로고
    • Crystal structure of a phosphatase-resistant mutant of sporulation response regulator Spo0F from Bacillus subtilis
    • Madhusudan, Zapf, J., Whiteley, J. M., Hoch, J. A., Xuong, N. H., and Varughese, K. I. (1996) Crystal structure of a phosphatase-resistant mutant of sporulation response regulator Spo0F from Bacillus subtilis, Structure 4, 679-90.
    • (1996) Structure , vol.4 , pp. 679-690
    • Madhusudan1    Zapf, J.2    Whiteley, J.M.3    Hoch, J.A.4    Xuong, N.H.5    Varughese, K.I.6
  • 26
    • 0041573371 scopus 로고    scopus 로고
    • Selective solid-phase isolation of methionine-containing peptides and subsequent matrix-assisted laser desorption/ionisation mass spectrometric detection of methionine- and of methionine-sulfoxide-containing peptides
    • Grunert, T., Pock, K., Buchacher, A., and Allmaier, G. (2003) Selective solid-phase isolation of methionine-containing peptides and subsequent matrix-assisted laser desorption/ionisation mass spectrometric detection of methionine- and of methionine-sulfoxide-containing peptides, Rapid Commun. Mass Spectrom. 17, 1815-24.
    • (2003) Rapid Commun. Mass Spectrom. , vol.17 , pp. 1815-1824
    • Grunert, T.1    Pock, K.2    Buchacher, A.3    Allmaier, G.4
  • 27
    • 0032993415 scopus 로고    scopus 로고
    • Alanine mutants of the Spo0F response regulator modifying specificity for sensor kinases in sporulation initiation
    • Jiang, M., Tzeng, Y. L., Feher, V. A., Perego, M., and Hoch, J. A. (1999) Alanine mutants of the Spo0F response regulator modifying specificity for sensor kinases in sporulation initiation, Mol. Microbiol. 33, 389-95.
    • (1999) Mol. Microbiol. , vol.33 , pp. 389-395
    • Jiang, M.1    Tzeng, Y.L.2    Feher, V.A.3    Perego, M.4    Hoch, J.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.