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Volumn 287, Issue 24, 2012, Pages 19973-19984

Site-specific protein dynamics in communication pathway from sensor to signaling domain of oxygen sensor protein, HemAT-Bs: Time-resolved ultraviolet resonance raman study

Author keywords

[No Author keywords available]

Indexed keywords

AMIDE I; COMMUNICATION PATHWAYS; CONFORMATIONAL CHANGE; FULL-LENGTH PROTEINS; INTENSITY CHANGE; LIGAND-FREE STRUCTURES; PEAK INTENSITY; PROTEIN BACKBONE; PROTEIN DYNAMICS; PROTEIN MOIETY; RAMAN BANDS; SENSOR DOMAINS; SIGNAL TRANSDUCER PROTEINS; SITE-SPECIFIC; TIME RANGE; TIME-RESOLVED; ULTRAVIOLET RESONANCE RAMAN; WILD TYPES;

EID: 84862001732     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.357855     Document Type: Article
Times cited : (14)

References (41)
  • 1
    • 0034598826 scopus 로고    scopus 로고
    • Myoglobin-like aerotaxis transducers in Archaea and Bacteria
    • DOI 10.1038/35000570
    • Hou, S., Larsen, R. W., Boudko, D., Riley, C. W., Karatan, E., Zimmer, M., Ordal, G. W., and Alam, M. (2000) Myoglobin-like aerotaxis transducers in archaea and bacteria. Nature 403, 540-544 (Pubitemid 30082198)
    • (2000) Nature , vol.403 , Issue.6769 , pp. 540-544
    • Hou, S.1    Larsen, R.W.2    Boudko, D.3    Riley, C.W.4    Karatan, E.5    Zimmer, M.6    Ordal, G.W.7    Alam, M.8
  • 3
    • 0037134550 scopus 로고    scopus 로고
    • Resonance Raman and ligand binding studies of the oxygen-sensing signal transducer protein HemAT from Bacillus subtilis
    • DOI 10.1074/jbc.M112256200
    • 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 (Pubitemid 34975647)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.16 , pp. 13528-13538
    • Aono, S.1    Kato, T.2    Matsuki, M.3    Nakajima, H.4    Ohta, T.5    Uchida, T.6    Kitagawa, T.7
  • 4
    • 22144452831 scopus 로고    scopus 로고
    • Biophysical and kinetic characterization of HemAT, an aerotaxis receptor from Bacillus subtilis
    • DOI 10.1529/biophysj.104.047936
    • Zhang, W., Olson, J. S., and Phillips, G. N. (2005) Biophysical and kinetic characterization of HemAT, an aerotaxis receptor from Bacillus subtilis. Biophys. J. 88, 2801-2814 (Pubitemid 40976146)
    • (2005) Biophysical Journal , vol.88 , Issue.4 , pp. 2801-2814
    • Zhang, W.1    Olson, J.S.2    Phillips Jr., G.N.3
  • 5
    • 13844256179 scopus 로고    scopus 로고
    • Resonance Raman investigation of the specific sensing mechanism of a target molecule by gas sensory proteins
    • DOI 10.1021/ic0486318
    • Ohta, T., and Kitagawa, T. (2005) Resonance Raman investigation of the specific sensing mechanism of a target molecule by gas sensory proteins. Inorg. Chem. 44, 758-769 (Pubitemid 40255946)
    • (2005) Inorganic Chemistry , vol.44 , Issue.4 , pp. 758-769
    • Ohta, T.1    Kitagawa, T.2
  • 6
    • 45149083640 scopus 로고    scopus 로고
    • Metal-containing sensor proteins sensing diatomic gas molecules
    • Aono, S. (2008) Metal-containing sensor proteins sensing diatomic gas molecules. Dalton Trans. 3137-3146
    • (2008) Dalton Trans. , pp. 3137-3146
    • Aono, S.1
  • 7
    • 10444268892 scopus 로고    scopus 로고
    • Heme-based sensors: Defining characteristics, recent developments, and regulatory hypotheses
    • Gilles-Gonzalez, M. A., and Gonzalez, G. J. (2005) Heme-based sensors: defining characteristics, recent developments, and regulatory hypotheses. J. Inorg. Biochem. 99, 1-22
    • (2005) J. Inorg. Biochem. , vol.99 , pp. 1-22
    • Gilles-Gonzalez, M.A.1    Gonzalez, G.J.2
  • 8
    • 24344498616 scopus 로고    scopus 로고
    • Mechanism for transduction of the ligand-binding signal in heme-based gas sensory proteins revealed by resonance Raman spectroscopy
    • DOI 10.1021/ar030267d
    • Uchida, T., and Kitagawa, T. (2005) Mechanism for transduction of the ligand-binding signal in heme-based gas sensory proteins revealed by resonance Raman spectroscopy. Acc. Chem. Res. 38, 662-670 (Pubitemid 41260520)
    • (2005) Accounts of Chemical Research , vol.38 , Issue.8 , pp. 662-670
    • Uchida, T.1    Kitagawa, T.2
  • 9
    • 2942584862 scopus 로고    scopus 로고
    • Diversity in chemotaxis mechanisms among the bacteria and archaea
    • DOI 10.1128/MMBR.68.2.301-319.2004
    • Szurmant, H., and Ordal, G. W. (2004) Diversity in chemotaxis mechanisms among the bacteria and archaea. Microbiol. Mol. Biol. Rev. 68, 301-319 (Pubitemid 38756867)
    • (2004) Microbiology and Molecular Biology Reviews , vol.68 , Issue.2 , pp. 301-319
    • Szurmant, H.1    Ordal, G.W.2
  • 10
    • 0026502186 scopus 로고
    • Bacillus subtilis chemotaxis: A deviation from the Escherichia coli paradigm
    • Bischoff, D. S., and Ordal, G. W. (1992) Bacillus subtilis chemotaxis: a deviation from the Escherichia coli paradigm. Mol. Microbiol. 6, 23-28
    • (1992) Mol. Microbiol. , vol.6 , pp. 23-28
    • Bischoff, D.S.1    Ordal, G.W.2
  • 11
    • 0028882853 scopus 로고
    • Chemotaxis in Bacillus subtilis: How bacteria monitor environmental signals
    • Garrity, L. F., and Ordal, G. W. (1995) Chemotaxis in Bacillus subtilis: how bacteria monitor environmental signals. Pharmacol. Ther. 68, 87-104
    • (1995) Pharmacol. Ther. , vol.68 , pp. 87-104
    • Garrity, L.F.1    Ordal, G.W.2
  • 12
    • 0042334880 scopus 로고    scopus 로고
    • Structure of the oxygen sensor in Bacillus subtilis: Signal transduction of chemotaxis by control of symmetry
    • DOI 10.1016/S0969-2126(03)00169-2
    • Zhang, W., and Phillips, G. N. (2003) Structure of the oxygen sensor in Bacillus subtilis: signal transduction of chemotaxis by control of symmetry. Structure 11, 1097-1110 (Pubitemid 37103071)
    • (2003) Structure , vol.11 , Issue.9 , pp. 1097-1110
    • Zhang, W.1    Phillips Jr., G.N.2
  • 13
    • 9444278384 scopus 로고    scopus 로고
    • Oxygen-sensing mechanism of HemAT from Bacillus subtilis: A resonance Raman spectroscopic study
    • DOI 10.1021/ja046896f
    • 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 (Pubitemid 39561730)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.46 , pp. 15000-15001
    • Ohta, T.1    Yoshimura, H.2    Yoshioka, S.3    Aono, S.4    Kitagawa, T.5
  • 15
    • 33746912769 scopus 로고    scopus 로고
    • Recognition and discrimination of gases by the oxygen-sensing signal transducer protein HemAT as revealed by FTIR spectroscopy
    • DOI 10.1021/bi0604072
    • Pinakoulaki, E., Yoshimura, H., Yoshioka, S., Aono, S., and Varotsis, C. (2006) Recognition and discrimination of gases by the oxygen-sensing signal transducer protein HemAT As revealed by FTIR spectroscopy. Biochemistry 45, 7763-7766 (Pubitemid 44185492)
    • (2006) Biochemistry , vol.45 , Issue.25 , pp. 7763-7766
    • Pinakoulaki, E.1    Yoshimura, H.2    Yoshioka, S.3    Aono, S.4    Varotsis, C.5
  • 16
    • 0001291195 scopus 로고
    • Spectroscopy of Biological Systems
    • Clark, R. J. H., and Hester, R. E., eds John Wiley & Sons, Chichester, UK
    • Harada, I., and Takeuchi, H. (1986) in Spectroscopy of Biological Systems (Clark, R. J. H., and Hester, R. E., eds) pp. 113-175, Advances in Spectroscopy, vol. 13, John Wiley & Sons, Chichester, UK
    • (1986) Advances in Spectroscopy , vol.13 , pp. 113-175
    • Harada, I.1    Takeuchi, H.2
  • 17
    • 0002058203 scopus 로고
    • Biomolecular Spectroscopy, Part A
    • Clark, R. J. H., and Hester, R. E., eds John Wiley & Sons, Chichester, UK
    • Austin, J. C., Jordan, T., and Spiro, T. G. (1993) in Biomolecular Spectroscopy, Part A (Clark, R. J. H., and Hester, R. E., eds) pp. 55-127, Advances in Spectroscopy, vol. 20, John Wiley & Sons, Chichester, UK
    • (1993) Advances in Spectroscopy , vol.20 , pp. 55-127
    • Austin, J.C.1    Jordan, T.2    Spiro, T.G.3
  • 18
    • 0000967751 scopus 로고
    • Hemoglobin R3T structural dynamics from simultaneous monitoring of tyrosine and tryptophan time-resolved UV resonance Raman signals
    • Rodgers, K. R., Su, C., Subramaniam, S., and Spiro, T. G. (1992) Hemoglobin R3T structural dynamics from simultaneous monitoring of tyrosine and tryptophan time-resolved UV resonance Raman signals. J. Am. Chem. Soc. 114, 3697-3709
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 3697-3709
    • Rodgers, K.R.1    Su, C.2    Subramaniam, S.3    Spiro, T.G.4
  • 19
    • 33947665446 scopus 로고    scopus 로고
    • Ultraviolet resonance Raman evidence for utilization of the heme 6-propionate hydrogen-bond network in signal transmission from heme to protein in Ec DOS protein
    • DOI 10.1021/ja0669777
    • El-Mashtoly, S. F., Takahashi, H., Shimizu, T., and Kitagawa, T. (2007) Ultraviolet resonance Raman evidence for utilization of the heme 6-propionate hydrogen-bond network in signal transmission from heme to protein in Ec DOS protein. J. Am. Chem. Soc. 129, 3556-3563 (Pubitemid 46502717)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.12 , pp. 3556-3563
    • El-Mashtoly, S.F.1    Takahashi, H.2    Shimizu, T.3    Kitagawa, T.4
  • 20
    • 33748312196 scopus 로고    scopus 로고
    • Pathway of information transmission from heme to protein upon ligand binding/dissociation in myoglobin revealed by UV resonance raman spectroscopy
    • DOI 10.1074/jbc.M603198200
    • Gao, Y., El-Mashtoly, S. F., Pal, B., Hayashi, T., Harada, K., and Kitagawa, T. (2006) Pathway of information transmission from heme to protein upon ligand binding/dissociation in myoglobin revealed by UV resonance Raman spectroscopy. J. Biol. Chem. 281, 24637-24646 (Pubitemid 44321472)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.34 , pp. 24637-24646
    • Gao, Y.1    El-Mashtoly, S.F.2    Pal, B.3    Hayashi, T.4    Harada, K.5    Kitagawa, T.6
  • 21
    • 30544439249 scopus 로고    scopus 로고
    • Structural changes during the photocycle of photoactive yellow protein monitored by ultraviolet resonance Raman spectra of tyrosine and tryptophan
    • DOI 10.1021/jp054772z
    • El-Mashtoly, S. F., Yamauchi, S., Kumauchi, M., Hamada, N., Tokunaga, F., and Unno, M. (2005) Structural changes during the photocycle of photoactive yellow protein monitored by ultraviolet resonance Raman spectra of tyrosine and tryptophan. J. Phys. Chem. B 109, 23666-23673 (Pubitemid 43081542)
    • (2005) Journal of Physical Chemistry B , vol.109 , Issue.49 , pp. 23666-23673
    • El-Mashtoly, S.F.1    Yamauchi, S.2    Kumauchi, M.3    Hamada, N.4    Tokunaga, F.5    Unno, M.6
  • 22
    • 77952259197 scopus 로고    scopus 로고
    • Structural refinement of a key tryptophan residue in the BLUF photoreceptor AppA by ultraviolet resonance Raman spectroscopy
    • Unno, M., Kikuchi, S., and Masuda, S. (2010) Structural refinement of a key tryptophan residue in the BLUF photoreceptor AppA by ultraviolet resonance Raman spectroscopy. Biophys. J. 98, 1949-1956
    • (2010) Biophys. J. , vol.98 , pp. 1949-1956
    • Unno, M.1    Kikuchi, S.2    Masuda, S.3
  • 23
    • 33744956072 scopus 로고    scopus 로고
    • Evidence for displacements of the C-helix by CO ligation and DNA binding to CooA revealed by UV resonance raman spectroscopy
    • DOI 10.1074/jbc.M513261200
    • Kubo, M., Inagaki, S., Yoshioka, S., Uchida, T., Mizutani, Y., Aono, S., and Kitagawa, T. (2006) Evidence for displacements of the C-helix by CO ligation and DNA binding to CooA revealed by UV resonance Raman spectroscopy. J. Biol. Chem. 281, 11271-11278 (Pubitemid 43855552)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.16 , pp. 11271-11278
    • Kubo, M.1    Inagaki, S.2    Yoshioka, S.3    Uchida, T.4    Mizutani, Y.5    Aono, S.6    Kitagawa, T.7
  • 25
    • 0027993426 scopus 로고
    • Nanosecond dynamics of the R3T transition in hemoglobin: Ultraviolet Raman studies
    • Rodgers, K. R., and Spiro, T. G. (1994) Nanosecond dynamics of the R3T transition in hemoglobin: ultraviolet Raman studies. Science 265, 1697-1699
    • (1994) Science , vol.265 , pp. 1697-1699
    • Rodgers, K.R.1    Spiro, T.G.2
  • 26
    • 6444222269 scopus 로고    scopus 로고
    • Time-resolved resonance Raman study of HbA with 220 nm excitation: Probing phenylalanine
    • Kneipp, J., Balakrishnan, G., and Spiro, T. G. (2004) Time-resolved resonance Raman study of HbA with 220 nm excitation: probing phenylalanine. J. Phys. Chem. B 108, 15919-15927
    • (2004) J. Phys. Chem. B , vol.108 , pp. 15919-15927
    • Kneipp, J.1    Balakrishnan, G.2    Spiro, T.G.3
  • 28
    • 43749094347 scopus 로고    scopus 로고
    • Protein conformation changes of HemAT-Bs upon ligand binding probed by ultraviolet resonance Raman spectroscopy
    • El-Mashtoly, S. F., Gu, Y., Yoshimura, H., Yoshioka, S., Aono, S., and Kitagawa, T. (2008) Protein conformation changes of HemAT-Bs upon ligand binding probed by ultraviolet resonance Raman spectroscopy. J. Biol. Chem. 283, 6942-6949
    • (2008) J. Biol. Chem. , vol.283 , pp. 6942-6949
    • El-Mashtoly, S.F.1    Gu, Y.2    Yoshimura, H.3    Yoshioka, S.4    Aono, S.5    Kitagawa, T.6
  • 29
    • 34247877483 scopus 로고    scopus 로고
    • The formation of hydrogen bond in the proximal heme pocket of HemAT-Bs upon ligand binding
    • DOI 10.1016/j.bbrc.2007.04.041, PII S0006291X07007693
    • Yoshimura, H., Yoshioka, S., Mizutani, Y., and Aono, S. (2007) The formation of hydrogen bond in the proximal heme pocket of HemAT-Bs upon ligand binding. Biochem. Biophys. Res. Commun. 357, 1053-1057 (Pubitemid 46693678)
    • (2007) Biochemical and Biophysical Research Communications , vol.357 , Issue.4 , pp. 1053-1057
    • Yoshimura, H.1    Yoshioka, S.2    Mizutani, Y.3    Aono, S.4
  • 30
    • 34548417989 scopus 로고    scopus 로고
    • Evidence for fast conformational change upon ligand dissociation in the HemAT class of bacterial oxygen sensors
    • DOI 10.1016/j.febslet.2007.08.031, PII S0014579307009076
    • Mokdad, A., Nissen, M., Satterlee, J. D., and Larsen, R. W. (2007) Evidence for fast conformational changes upon ligand dissociation in the HemeAT class of bacterial oxygen sensors. FEBS Lett. 581, 4512-4518 (Pubitemid 47368211)
    • (2007) FEBS Letters , vol.581 , Issue.23 , pp. 4512-4518
    • Mokdad, A.1    Nissen, M.2    Satterlee, J.D.3    Larsen, R.W.4
  • 31
    • 39649122396 scopus 로고    scopus 로고
    • Construction of a subnanosecond time-resolved, high-resolution ultraviolet resonance raman measurement system and its application to reveal the dynamic structures of proteins
    • DOI 10.1366/000370208783412573
    • Kubo, M., Uchida, T., Nakashima, S., and Kitagawa, T. (2008) Construction of a subnanosecond time-resolved, high-resolution ultraviolet resonance Raman measurement system and its application to reveal the dynamic structures of proteins. Appl. Spectrosc. 62, 30-37 (Pubitemid 351321605)
    • (2008) Applied Spectroscopy , vol.62 , Issue.1 , pp. 30-37
    • Kubo, M.1    Uchida, T.2    Nakashima, S.3    Kitagawa, T.4
  • 32
    • 80052380624 scopus 로고    scopus 로고
    • Structural dynamics of EcDOS heme domain revealed by time-resolved ultraviolet resonance Raman spectroscopy
    • El-Mashtoly, S. F., Kubo, M., Nakashima, S., Shimizu, T., and Kitagawa, T. (2011) Structural dynamics of EcDOS heme domain revealed by time-resolved ultraviolet resonance Raman spectroscopy. J. Phys. Chem. Lett. 2, 2212-2217
    • (2011) J. Phys. Chem. Lett. , vol.2 , pp. 2212-2217
    • El-Mashtoly, S.F.1    Kubo, M.2    Nakashima, S.3    Shimizu, T.4    Kitagawa, T.5
  • 33
    • 0027429642 scopus 로고
    • A model-independent approach to assigning bacteriorhodopsin's intramolecular reactions to photocycle intermediates
    • Hessling, B., Souvignier, G., and Gerwert, K. (1993) A model-independent approach to assigning bacteriorhodopsin's intramolecular reactions to photocycle intermediates. Biophys. J. 65, 1929-1941 (Pubitemid 23334860)
    • (1993) Biophysical Journal , vol.65 , Issue.5 , pp. 1929-1941
    • Hessling, B.1    Souvignier, G.2    Gerwert, K.3
  • 34
    • 0000281676 scopus 로고    scopus 로고
    • UV Raman determination of the environment and solvent exposure of Tyr and Trp residues
    • Chi, Z., and Asher, S. A. (1998) UV Raman determination of the environment and solvent exposure of Tyr and Trp residues. J. Phys. Chem. B 102, 9595-9602 (Pubitemid 128611879)
    • (1998) Journal of Physical Chemistry B , vol.102 , Issue.47 , pp. 9595-9602
    • Chi, Z.1    Asher, S.A.2
  • 35
    • 0000749062 scopus 로고    scopus 로고
    • Effects of Hydrogen Bonding and Hydrophobic Interactions on the Ultraviolet Resonance Raman Intensities of Indole Ring Vibrations
    • Matsuno, M., and Takeuchi, H. (1998) Effects of hydrogen bonding and hydrophobic interactions on the ultraviolet resonance Raman intensities of indole ring vibrations. Bull. Chem. Soc. Jpn. 71, 851-857 (Pubitemid 128499846)
    • (1998) Bulletin of the Chemical Society of Japan , vol.71 , Issue.4 , pp. 851-857
    • Matsuno, M.1    Takeuchi, H.2
  • 36
    • 84988158723 scopus 로고
    • Saturation effects on ultraviolet resonance Raman intensities: Excimer/YAG laser comparison and aromatic amino acid cross-sections
    • Su, C., Wang, Y., and Spiro, T. G. (1990) Saturation effects on ultraviolet resonance Raman intensities: excimer/YAG laser comparison and aromatic amino acid cross-sections. J. Raman Spectrosc. 21, 435-440
    • (1990) J. Raman Spectrosc. , vol.21 , pp. 435-440
    • Su, C.1    Wang, Y.2    Spiro, T.G.3
  • 37
    • 0000361659 scopus 로고
    • Tryptophan UV resonance Raman excitation profiles
    • Sweeney, J. A., and Asher, S. A. (1990) Tryptophan UV resonance Raman excitation profiles. J. Phys. Chem. 94, 4784-4791
    • (1990) J. Phys. Chem. , vol.94 , pp. 4784-4791
    • Sweeney, J.A.1    Asher, S.A.2
  • 39
    • 0033543590 scopus 로고    scopus 로고
    • A piston model for transmembrane signaling of the aspartate receptor
    • DOI 10.1126/science.285.5434.1751
    • Ottemann, K. M., Xiao, W., Shin, Y. K., and Koshland, D. E., Jr. (1999) A piston model for transmembrane signaling of the aspartate receptor. Science 285, 1751-1754 (Pubitemid 29428878)
    • (1999) Science , vol.285 , Issue.5434 , pp. 1751-1754
    • Ottemann, K.M.1    Xiao, W.2    Shin, Y.-K.3    Koshland Jr., D.E.4
  • 40
    • 8544279966 scopus 로고    scopus 로고
    • Ligand-induced conformational changes in the Bacillus subtilis chemoreceptor McpB determined by disulfide crosslinking in vivo
    • DOI 10.1016/j.jmb.2004.09.093, PII S0022283604012641
    • Szurmant, H., Bunn, M. W., Cho, S. H., and Ordal, G. W. (2004) Ligand-induced conformational changes in the Bacillus subtilis chemoreceptor McpBdetermined by disulfide cross-linking in vivo. J. Mol. Biol. 344, 919-928 (Pubitemid 39491239)
    • (2004) Journal of Molecular Biology , vol.344 , Issue.4 , pp. 919-928
    • Szurmant, H.1    Bunn, M.W.2    Cho, S.H.3    Ordal, G.W.4


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