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Volumn 46, Issue 34, 2007, Pages 9728-9736

Interdomain interactions within the two-component heme-based sensor DevS from Mycobacterium tuberculosis

Author keywords

[No Author keywords available]

Indexed keywords

ANAEROBIOSIS; INTERDOMAIN INTERACTIONS; MYCOBACTERIUM TUBERCULOSIS;

EID: 34548228384     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi7008695     Document Type: Article
Times cited : (31)

References (38)
  • 1
    • 34548241595 scopus 로고    scopus 로고
    • World Health Organization
    • World Health Organization (2007) Fact sheet on TB, http:// www.who.int/3by5/TBfactsheet.pdf.
    • (2007) Fact sheet on TB
  • 2
    • 0035182257 scopus 로고    scopus 로고
    • Dormant tubercle bacilli: The key to more effective TB chemotherapy?
    • Dick, T. (2001) Dormant tubercle bacilli: the key to more effective TB chemotherapy?, J. Antimicrob. Chemother. 47, 117-118.
    • (2001) J. Antimicrob. Chemother , vol.47 , pp. 117-118
    • Dick, T.1
  • 3
    • 0029976980 scopus 로고    scopus 로고
    • An in vitro model for sequential study of shiftdown of Mycobacterium tuberculosis through two stages of nonreplicating persistence
    • Wayne, L. G., and Hayes, L. G. (1996) An in vitro model for sequential study of shiftdown of Mycobacterium tuberculosis through two stages of nonreplicating persistence, Infect. Immun. 64, 2062-2069.
    • (1996) Infect. Immun , vol.64 , pp. 2062-2069
    • Wayne, L.G.1    Hayes, L.G.2
  • 5
    • 0031930142 scopus 로고    scopus 로고
    • Mycobacterial stationary phase induced by low oxygen tension: Cell wall thickening and localization of the 16-kilodalton -crystallin homolog
    • Cunningham, A. F., and Spreadbury, C. L. (1998) Mycobacterial stationary phase induced by low oxygen tension: Cell wall thickening and localization of the 16-kilodalton -crystallin homolog, J. Bacteriol. 180, 801-808.
    • (1998) J. Bacteriol , vol.180 , pp. 801-808
    • Cunningham, A.F.1    Spreadbury, C.L.2
  • 7
    • 0034780485 scopus 로고    scopus 로고
    • Nonreplicating persistence of Mycobacterium tuberculosis
    • Wayne, L. G., and Sohaskey, C. D. (2001) Nonreplicating persistence of Mycobacterium tuberculosis, Annu. Rev. Microbiol. 55, 139-163.
    • (2001) Annu. Rev. Microbiol , vol.55 , pp. 139-163
    • Wayne, L.G.1    Sohaskey, C.D.2
  • 8
    • 0037099165 scopus 로고    scopus 로고
    • Analysis of nitric oxide synthase and nitrotyrosine expression in human pulmonary tuberculosis
    • Choi, H. S., Rai, P. R., Chu, H. W., Cool, C., and Chan, E. D. (2002) Analysis of nitric oxide synthase and nitrotyrosine expression in human pulmonary tuberculosis, Am. J. Respir. Crit. Care Med. 166, 178-186.
    • (2002) Am. J. Respir. Crit. Care Med , vol.166 , pp. 178-186
    • Choi, H.S.1    Rai, P.R.2    Chu, H.W.3    Cool, C.4    Chan, E.D.5
  • 10
    • 2542475060 scopus 로고    scopus 로고
    • Two sensor kinases contribute to the hypoxic response of Mycobacterium tuberculosis
    • Roberts, D. M., Liao, R. P., Wisedchaisri, G., Hoi, W. G., and Sherman, D. R. (2004) Two sensor kinases contribute to the hypoxic response of Mycobacterium tuberculosis, J. Biol. Chem. 279, 23082-23087.
    • (2004) J. Biol. Chem , vol.279 , pp. 23082-23087
    • Roberts, D.M.1    Liao, R.P.2    Wisedchaisri, G.3    Hoi, W.G.4    Sherman, D.R.5
  • 11
    • 27144485413 scopus 로고    scopus 로고
    • A GAF domain in the hypoxia/NO-inducible Mycobacterium tuberculosis DosS protein binds haem
    • Sardiwal, S., Kendall, S. L., Movahedzadeh, F., Rison, S. C., Stoker, N. G., and Djordjevic, S. (2005) A GAF domain in the hypoxia/NO-inducible Mycobacterium tuberculosis DosS protein binds haem, J. Mol. Biol. 353, 929-936.
    • (2005) J. Mol. Biol , vol.353 , pp. 929-936
    • Sardiwal, S.1    Kendall, S.L.2    Movahedzadeh, F.3    Rison, S.C.4    Stoker, N.G.5    Djordjevic, S.6
  • 12
    • 34147117736 scopus 로고    scopus 로고
    • DevS, a heme-containing two-component oxygen sensor of Mycobacterium tuberculosis
    • Ioanoviciu, A., Yukl, E. T., Moënne-Loccoz, P., and Ortiz de Montellano, P. R. (2007) DevS, a heme-containing two-component oxygen sensor of Mycobacterium tuberculosis, Biochemistry 46, 4250-4260.
    • (2007) Biochemistry , vol.46 , pp. 4250-4260
    • Ioanoviciu, A.1    Yukl, E.T.2    Moënne-Loccoz, P.3    Ortiz de Montellano, P.R.4
  • 13
    • 34548200606 scopus 로고    scopus 로고
    • Spiro, T. G., and Li, X. Y. (1988) Biological applications of Raman spectroscopy. 3. Resonance Raman spectra of hemes and metalloproteins (Spiro, T. G., Ed.) pp 1-37, John Wiley & Sons, New York.
    • Spiro, T. G., and Li, X. Y. (1988) Biological applications of Raman spectroscopy. Vol. 3. Resonance Raman spectra of hemes and metalloproteins (Spiro, T. G., Ed.) pp 1-37, John Wiley & Sons, New York.
  • 14
    • 0030467166 scopus 로고    scopus 로고
    • Assignment of protoheme resonance Raman spectrum by heme labeling in myoglobin
    • Hu, S., Smith, K. M., and Spiro, T. G. (1996) Assignment of protoheme resonance Raman spectrum by heme labeling in myoglobin, J. Am. Chem. Soc. 118, 12638-12646.
    • (1996) J. Am. Chem. Soc , vol.118 , pp. 12638-12646
    • Hu, S.1    Smith, K.M.2    Spiro, T.G.3
  • 15
    • 0028223077 scopus 로고
    • How far can proteins bend the FeCO unit? Distal polar and steric effects in heme proteins and models
    • Ray, G. B., Li, X.-Y., Ibers, J. A., Sessler, J. L., and Spiro, T. G. (1994) How far can proteins bend the FeCO unit? Distal polar and steric effects in heme proteins and models, J. Am. Chem. Soc. 116, 162-176.
    • (1994) J. Am. Chem. Soc , vol.116 , pp. 162-176
    • Ray, G.B.1    Li, X.-Y.2    Ibers, J.A.3    Sessler, J.L.4    Spiro, T.G.5
  • 16
    • 0028328331 scopus 로고
    • Structural determinants of the stretching frequency of CO bound to myoglobin
    • Li, T., Quillin, M. L., Phillips, G. N., Jr., and Olson, J. S. (1994) Structural determinants of the stretching frequency of CO bound to myoglobin, Biochemistry 33, 1433-1446.
    • (1994) Biochemistry , vol.33 , pp. 1433-1446
    • Li, T.1    Quillin, M.L.2    Phillips Jr., G.N.3    Olson, J.S.4
  • 17
    • 0031018221 scopus 로고    scopus 로고
    • A chemometric analysis of the resonance Raman spectra of mutant carbonmonoxy-myoglobins reveals the effects of polarity
    • Anderton, C. L., Hester, R. E., and Moore, J. N. (1997) A chemometric analysis of the resonance Raman spectra of mutant carbonmonoxy-myoglobins reveals the effects of polarity, Biochim. Biophys. Acta 1338, 107-120.
    • (1997) Biochim. Biophys. Acta , vol.1338 , pp. 107-120
    • Anderton, C.L.1    Hester, R.E.2    Moore, J.N.3
  • 18
    • 0028568019 scopus 로고
    • Identification of the iron-carbonyl stretch in distal histidine mutants of carbon- monoxymyoglobin
    • Ling, J., Li, T., Olson, J. S., and Bocian, D. F. (1994) Identification of the iron-carbonyl stretch in distal histidine mutants of carbon- monoxymyoglobin, Biochim. Biophys. Acta 1188, 417-421.
    • (1994) Biochim. Biophys. Acta , vol.1188 , pp. 417-421
    • Ling, J.1    Li, T.2    Olson, J.S.3    Bocian, D.F.4
  • 19
    • 0001652725 scopus 로고    scopus 로고
    • Resonance Raman investigation of Fe-N-O structure of nitrosylheme in myoglobin and its mutants
    • Tomita, T., Hirota, S., Ogura, T., Olson, J. S., and Kitagawa, T. (1999) Resonance Raman investigation of Fe-N-O structure of nitrosylheme in myoglobin and its mutants, J. Phys. Chem. B 103, 7044-7054.
    • (1999) J. Phys. Chem. B , vol.103 , pp. 7044-7054
    • Tomita, T.1    Hirota, S.2    Ogura, T.3    Olson, J.S.4    Kitagawa, T.5
  • 21
    • 0000506287 scopus 로고
    • Resonance Raman spectra of the nitric oxide adducts of ferrous cytochrome P450cam in the presence of various substrates
    • Hu, S., and Kincaid, J. R. (1991) Resonance Raman spectra of the nitric oxide adducts of ferrous cytochrome P450cam in the presence of various substrates, J. Am. Chem. Soc. 113, 9760-9766.
    • (1991) J. Am. Chem. Soc , vol.113 , pp. 9760-9766
    • Hu, S.1    Kincaid, J.R.2
  • 22
    • 0033520701 scopus 로고    scopus 로고
    • Determinants of the FeXO (X = C, N, O) vibrational frequencies in heme adducts from experiment and density functional theory
    • Vogel, K. M., Kozlowski, P. M., Zgierski, M. Z., and Spiro, T. G. (1999) Determinants of the FeXO (X = C, N, O) vibrational frequencies in heme adducts from experiment and density functional theory, J. Am. Chem. Soc. 121, 9915-9921.
    • (1999) J. Am. Chem. Soc , vol.121 , pp. 9915-9921
    • Vogel, K.M.1    Kozlowski, P.M.2    Zgierski, M.Z.3    Spiro, T.G.4
  • 23
    • 0000582319 scopus 로고
    • Oxygen-bound heme-heme oxygenase complex - Evidence for a highly bent structure of the coordinated oxygen
    • Takahashi, S., Ishikawa, K., Takeuchi, N., Ikeda-Saito, M., Yoshida, T., and Rousseau, D. L. (1995) Oxygen-bound heme-heme oxygenase complex - Evidence for a highly bent structure of the coordinated oxygen, J. Am. Chem. Soc. 117, 6002-6006.
    • (1995) J. Am. Chem. Soc , vol.117 , pp. 6002-6006
    • Takahashi, S.1    Ishikawa, K.2    Takeuchi, N.3    Ikeda-Saito, M.4    Yoshida, T.5    Rousseau, D.L.6
  • 24
    • 2442645409 scopus 로고    scopus 로고
    • Crystal structure of the dioxygen-bound heme oxygenase from Corynebacterium diphtheriae: Implications for heme oxygenase function
    • Unno, M., Matsui, T., Chu, G. C., Couture, M., Yoshida, T., Rousseau, D. L., Olson, J. S., and Ikeda-Saito, M. (2004) Crystal structure of the dioxygen-bound heme oxygenase from Corynebacterium diphtheriae: implications for heme oxygenase function, J. Biol. Chem. 279, 21055-21061.
    • (2004) J. Biol. Chem , vol.279 , pp. 21055-21061
    • Unno, M.1    Matsui, T.2    Chu, G.C.3    Couture, M.4    Yoshida, T.5    Rousseau, D.L.6    Olson, J.S.7    Ikeda-Saito, M.8
  • 27
    • 0030942247 scopus 로고    scopus 로고
    • Characterization of ferrous FixL-nitric oxide adducts by resonance Raman spectroscopy
    • Lukat-Rodgers, G. S., and Rodgers, K. R. (1997) Characterization of ferrous FixL-nitric oxide adducts by resonance Raman spectroscopy, Biochemistry 36, 4178-4187.
    • (1997) Biochemistry , vol.36 , pp. 4178-4187
    • Lukat-Rodgers, G.S.1    Rodgers, K.R.2
  • 28
    • 0033551768 scopus 로고    scopus 로고
    • Iron coordination structures of oxygen sensor FixL characterized by Fe K-edge extended x-ray absorption fine structure and resonance Raman spectroscopy
    • Miyatake, H., Mukai, M., Adachi, S., Nakamura, H., Tamura, K., Iizuka, T., Shiro, Y., Strange, R. W., and Hasnain, S. S. (1999) Iron coordination structures of oxygen sensor FixL characterized by Fe K-edge extended x-ray absorption fine structure and resonance Raman spectroscopy, J. Biol. Chem. 274, 23176-23184.
    • (1999) J. Biol. Chem , vol.274 , pp. 23176-23184
    • Miyatake, H.1    Mukai, M.2    Adachi, S.3    Nakamura, H.4    Tamura, K.5    Iizuka, T.6    Shiro, Y.7    Strange, R.W.8    Hasnain, S.S.9
  • 29
    • 0037134550 scopus 로고    scopus 로고
    • Resonance Raman and ligand binding studies of the oxygen-sensing signal transducer protein HemAT from Bacillus subtilis
    • Aono, S., Kato, T., Matsuki, M., Nakajima, H., Ohta, T., Uchida, T., and Kitagawa, T. (2002) Resonance Raman and ligand binding studies of the oxygen-sensing signal transducer protein HemAT from Bacillus subtilis, J. Biol. Chem. 277, 13528-13538.
    • (2002) J. Biol. Chem , vol.277 , pp. 13528-13538
    • Aono, S.1    Kato, T.2    Matsuki, M.3    Nakajima, H.4    Ohta, T.5    Uchida, T.6    Kitagawa, T.7
  • 30
    • 0037117726 scopus 로고    scopus 로고
    • A comparative resonance Raman analysis of heme-binding PAS domains: Heme iron coordination structures of the BjFixL, AxPDEA1, EcDos, and MtDos proteins
    • Tomita, T., Gonzalez, G., Chang, A. L., Ikeda-Saito, M., and Gilles-Gonzalez, M. A. (2002) A comparative resonance Raman analysis of heme-binding PAS domains: heme iron coordination structures of the BjFixL, AxPDEA1, EcDos, and MtDos proteins, Biochemistry 41, 4819-4826.
    • (2002) Biochemistry , vol.41 , pp. 4819-4826
    • Tomita, T.1    Gonzalez, G.2    Chang, A.L.3    Ikeda-Saito, M.4    Gilles-Gonzalez, M.A.5
  • 31
    • 1542327658 scopus 로고    scopus 로고
    • Insights into signal transduction involving PAS domain oxygen-sensing heme proteins from the X-ray crystal structure of Escherichia coli Dos heme domain (Ec DosH)
    • Park, H., Suquet, C., Satterlee, J. D., and Kang, C. (2004) Insights into signal transduction involving PAS domain oxygen-sensing heme proteins from the X-ray crystal structure of Escherichia coli Dos heme domain (Ec DosH), Biochemistry 43, 2738-2746.
    • (2004) Biochemistry , vol.43 , pp. 2738-2746
    • Park, H.1    Suquet, C.2    Satterlee, J.D.3    Kang, C.4
  • 32
    • 9444278384 scopus 로고    scopus 로고
    • Oxygen-sensing mechanism of HemAT from Bacillus subtilis: A resonance Raman spectroscopic study
    • Ohta, T., Yoshimura, H., Yoshioka, S., Aono, S., and Kitagawa, T. (2004) Oxygen-sensing mechanism of HemAT from Bacillus subtilis: a resonance Raman spectroscopic study, J. Am. Chem. Soc. 126, 15000-15001.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 15000-15001
    • Ohta, T.1    Yoshimura, H.2    Yoshioka, S.3    Aono, S.4    Kitagawa, T.5
  • 33
    • 33745814412 scopus 로고    scopus 로고
    • Specific hydrogen-bonding networks responsible for selective O2 sensing of the oxygen sensor protein HemAT from Bacillus subtilis
    • Yoshimura, H., Yoshioka, S., Kobayashi, K., Ohta, T., Uchida, T., Kubo, M., Kitagawa, T., and Aono, S. (2006) Specific hydrogen-bonding networks responsible for selective O2 sensing of the oxygen sensor protein HemAT from Bacillus subtilis, Biochemistry 45, 8301-8307.
    • (2006) Biochemistry , vol.45 , pp. 8301-8307
    • Yoshimura, H.1    Yoshioka, S.2    Kobayashi, K.3    Ohta, T.4    Uchida, T.5    Kubo, M.6    Kitagawa, T.7    Aono, S.8
  • 35
    • 0020484765 scopus 로고
    • Resonance Raman investigation of carbon monoxide bonding in (carbon monoxy)hemoglobin and -myoglobin: Detection of Fe-CO stretching and Fe-C-O bending vibrations and influence of the quaternary structure change
    • Tsubaki, M., Srivastava, R. B., and Yu, N. T. (1982) Resonance Raman investigation of carbon monoxide bonding in (carbon monoxy)hemoglobin and -myoglobin: detection of Fe-CO stretching and Fe-C-O bending vibrations and influence of the quaternary structure change, Biochemistry 21, 1132-1140.
    • (1982) Biochemistry , vol.21 , pp. 1132-1140
    • Tsubaki, M.1    Srivastava, R.B.2    Yu, N.T.3
  • 36
    • 0022252945 scopus 로고
    • Resonance Raman evidence for the activation of dioxygen in horseradish oxyperoxidase
    • Van Wart, H. E., and Zimmer, J. (1985) Resonance Raman evidence for the activation of dioxygen in horseradish oxyperoxidase, J. Biol. Chem. 260, 8372-8377.
    • (1985) J. Biol. Chem , vol.260 , pp. 8372-8377
    • Van Wart, H.E.1    Zimmer, J.2
  • 38
    • 34547568747 scopus 로고    scopus 로고
    • DosT and DevS are oxygen-switched kinases in Mycobacterium tuberculosis
    • in press
    • Sousa, E. H. S., Tuckerman, J. R., Gonzalez, G., and Gilles-Gonzalez, M.-A. (2007) DosT and DevS are oxygen-switched kinases in Mycobacterium tuberculosis, Protein Sci. 16, in press.
    • (2007) Protein Sci , vol.16
    • Sousa, E.H.S.1    Tuckerman, J.R.2    Gonzalez, G.3    Gilles-Gonzalez, M.-A.4


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