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Volumn 77, Issue 3, 2010, Pages 575-586

Gain-of-function mutations cluster in distinct regions associated with the signalling pathway in the PAS domain of the aerotaxis receptor, Aer

Author keywords

[No Author keywords available]

Indexed keywords

AER RECEPTOR; FLAVINE ADENINE NUCLEOTIDE; PAS PROTEIN; PROTEIN; RECEPTOR; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG; AER PROTEIN, E COLI; CARRIER PROTEIN; ESCHERICHIA COLI PROTEIN; PROTEIN BINDING;

EID: 77954839079     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2010.07231.x     Document Type: Article
Times cited : (21)

References (42)
  • 1
    • 0037076332 scopus 로고    scopus 로고
    • Collaborative signaling by mixed chemoreceptor teams in Escherichia coli
    • Ames, P., Studdert, C. A., Reiser, R. H. Parkinson, J. S. (2002) Collaborative signaling by mixed chemoreceptor teams in Escherichia coli. Proc Natl Acad Sci USA 99 : 7060 7065.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 7060-7065
    • Ames, P.1    Studdert, C.A.2    Reiser, R.H.3    Parkinson, J.S.4
  • 2
    • 31344454302 scopus 로고    scopus 로고
    • Topology and boundaries of the aerotaxis receptor Aer in the membrane of Escherichia coli
    • Amin, D. N., Taylor, B. L. Johnson, M. S. (2006) Topology and boundaries of the aerotaxis receptor Aer in the membrane of Escherichia coli. J Bacteriol 186 : 894 901.
    • (2006) J Bacteriol , vol.186 , pp. 894-901
    • Amin, D.N.1    Taylor, B.L.2    Johnson, M.S.3
  • 3
    • 35048857575 scopus 로고    scopus 로고
    • Organization of the aerotaxis receptor Aer in the membrane of Escherichia coli
    • Amin, D. N., Taylor, B. L. Johnson, M. S. (2007) Organization of the aerotaxis receptor Aer in the membrane of Escherichia coli. J Bacteriol 189 : 7206 7212.
    • (2007) J Bacteriol , vol.189 , pp. 7206-7212
    • Amin, D.N.1    Taylor, B.L.2    Johnson, M.S.3
  • 4
    • 0032766134 scopus 로고    scopus 로고
    • The cytoplasmic helical linker domain of receptor histidine kinase and methyl-accepting proteins is common to many prokaryotic signalling proteins
    • Aravind, L. Ponting, C. P. (1999) The cytoplasmic helical linker domain of receptor histidine kinase and methyl-accepting proteins is common to many prokaryotic signalling proteins. FEMS Microbiol Lett 176 : 111 116.
    • (1999) FEMS Microbiol Lett , vol.176 , pp. 111-116
    • Aravind, L.1    Ponting, C.P.2
  • 5
    • 0034705035 scopus 로고    scopus 로고
    • Domain organization and flavin adenine dinucleotide-binding determinants in the aerotaxis signal transducer Aer of Escherichia coli
    • Bibikov, S. I., Barnes, L. A., Gitin, Y. Parkinson, J. S. (2000) Domain organization and flavin adenine dinucleotide-binding determinants in the aerotaxis signal transducer Aer of Escherichia coli. Proc Natl Acad Sci USA 97 : 5830 5835.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 5830-5835
    • Bibikov, S.I.1    Barnes, L.A.2    Gitin, Y.3    Parkinson, J.S.4
  • 6
    • 0029110488 scopus 로고
    • 1.4 A structure of photoactive yellow protein, a cytosolic photoreceptor: Unusual fold, active site, and chromophore
    • Borgstahl, G. E., Williams, D. R. Getzoff, E. D. (1995) 1.4 A structure of photoactive yellow protein, a cytosolic photoreceptor: unusual fold, active site, and chromophore. Biochemistry 34 : 6278 6287.
    • (1995) Biochemistry , vol.34 , pp. 6278-6287
    • Borgstahl, G.E.1    Williams, D.R.2    Getzoff, E.D.3
  • 7
    • 33646597727 scopus 로고    scopus 로고
    • Loss- and gain-of-function mutations in the F1-HAMP region of the Escherichia coli aerotaxis transducer Aer
    • Burón-Barral, M. C., Gosink, K. K. Parkinson, J. S. (2006) Loss- and gain-of-function mutations in the F1-HAMP region of the Escherichia coli aerotaxis transducer Aer. J Bacteriol 188 : 3477 3486.
    • (2006) J Bacteriol , vol.188 , pp. 3477-3486
    • Burón-Barral, M.C.1    Gosink, K.K.2    Parkinson, J.S.3
  • 9
    • 0017807890 scopus 로고
    • Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the P15A cryptic miniplasmid
    • Chang, A. C. Cohen, S. N. (1978) Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the P15A cryptic miniplasmid. J Bacteriol 134 : 1141 1156.
    • (1978) J Bacteriol , vol.134 , pp. 1141-1156
    • Chang, A.C.1    Cohen, S.N.2
  • 10
    • 33750009613 scopus 로고    scopus 로고
    • Differentiation between electron transport sensing and proton motive force sensing by the Aer and Tsr receptors for aerotaxis
    • Edwards, J. C., Johnson, M. S. Taylor, B. L. (2006) Differentiation between electron transport sensing and proton motive force sensing by the Aer and Tsr receptors for aerotaxis. Mol Microbiol 62 : 823 837.
    • (2006) Mol Microbiol , vol.62 , pp. 823-837
    • Edwards, J.C.1    Johnson, M.S.2    Taylor, B.L.3
  • 11
    • 53549125239 scopus 로고    scopus 로고
    • Plasticity of the PAS domain and a potential role for signal transduction in the histidine kinase DcuS
    • Etzkorn, M., Kneuper, H., Dunnwald, P., Vijayan, V., Kramer, J., Griesinger, C., et al. (2008) Plasticity of the PAS domain and a potential role for signal transduction in the histidine kinase DcuS. Nat Struct Mol Biol 15 : 1031 1039.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 1031-1039
    • Etzkorn, M.1    Kneuper, H.2    Dunnwald, P.3    Vijayan, V.4    Kramer, J.5    Griesinger, C.6
  • 12
    • 0032438105 scopus 로고    scopus 로고
    • Structure of a biological oxygen sensor: A new mechanism for heme-driven signal transduction
    • Gong, W., Hao, B., Mansy, S. S., Gonzalez, G., Gilles-Gonzalez, M. A. Chan, M. K. (1998) Structure of a biological oxygen sensor: a new mechanism for heme-driven signal transduction. Proc Natl Acad Sci USA 95 : 15177 15182.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 15177-15182
    • Gong, W.1    Hao, B.2    Mansy, S.S.3    Gonzalez, G.4    Gilles-Gonzalez, M.A.5    Chan, M.K.6
  • 13
    • 33646544356 scopus 로고    scopus 로고
    • Signaling interactions between the aerotaxis transducer Aer and heterologous chemoreceptors in Escherichia coli
    • Gosink, K. K., Burón-Barral, M. C. Parkinson, J. S. (2006) Signaling interactions between the aerotaxis transducer Aer and heterologous chemoreceptors in Escherichia coli. J Bacteriol 188 : 3487 3493.
    • (2006) J Bacteriol , vol.188 , pp. 3487-3493
    • Gosink, K.K.1    Burón-Barral, M.C.2    Parkinson, J.S.3
  • 14
    • 0345707600 scopus 로고    scopus 로고
    • Role of an N-terminal loop in the secondary structural change of photoactive yellow protein
    • Harigai, M., Imamoto, Y., Kamikubo, H., Yamazaki, Y. Kataoka, M. (2003) Role of an N-terminal loop in the secondary structural change of photoactive yellow protein. Biochemistry 42 : 13893 13900.
    • (2003) Biochemistry , vol.42 , pp. 13893-13900
    • Harigai, M.1    Imamoto, Y.2    Kamikubo, H.3    Yamazaki, Y.4    Kataoka, M.5
  • 15
    • 37749029507 scopus 로고    scopus 로고
    • Bacterial chemoreceptors: High-performance signaling in networked arrays
    • Hazelbauer, G. L., Falke, J. J. Parkinson, J. S. (2008) Bacterial chemoreceptors: high-performance signaling in networked arrays. Trends Biochem Sci 33 : 9 19.
    • (2008) Trends Biochem Sci , vol.33 , pp. 9-19
    • Hazelbauer, G.L.1    Falke, J.J.2    Parkinson, J.S.3
  • 16
    • 4944243738 scopus 로고    scopus 로고
    • PAS domain of the Aer redox sensor requires C-terminal residues for native-fold formation and flavin adenine dinucleotide binding
    • Herrmann, S., Ma, Q., Johnson, M. S., Repik, A. V. Taylor, B. L. (2004) PAS domain of the Aer redox sensor requires C-terminal residues for native-fold formation and flavin adenine dinucleotide binding. J Bacteriol 186 : 6782 6791.
    • (2004) J Bacteriol , vol.186 , pp. 6782-6791
    • Herrmann, S.1    Ma, Q.2    Johnson, M.S.3    Repik, A.V.4    Taylor, B.L.5
  • 17
    • 0027184569 scopus 로고
    • PAS is a dimerization domain common to Drosophila period and several transcription factors
    • Huang, Z. J., Edery, I. Rosbash, M. (1993) PAS is a dimerization domain common to Drosophila period and several transcription factors. Nature 364 : 259 262.
    • (1993) Nature , vol.364 , pp. 259-262
    • Huang, Z.J.1    Edery, I.2    Rosbash, M.3
  • 18
    • 33748183257 scopus 로고    scopus 로고
    • The HAMP domain structure implies helix rotation in transmembrane signaling
    • Hulko, M., Berndt, F., Gruber, M., Linder, J. U., Truffault, V., Schultz, A., et al. (2006) The HAMP domain structure implies helix rotation in transmembrane signaling. Cell 126 : 929 940.
    • (2006) Cell , vol.126 , pp. 929-940
    • Hulko, M.1    Berndt, F.2    Gruber, M.3    Linder, J.U.4    Truffault, V.5    Schultz, A.6
  • 19
    • 0031922353 scopus 로고    scopus 로고
    • Suppressor mutation analysis of the sensory rhodopsin I-transducer complex: Insights into the color-sensing mechanism
    • Jung, K. H. Spudich, J. L. (1998) Suppressor mutation analysis of the sensory rhodopsin I-transducer complex: insights into the color-sensing mechanism. J Bacteriol 180 : 2033 2042.
    • (1998) J Bacteriol , vol.180 , pp. 2033-2042
    • Jung, K.H.1    Spudich, J.L.2
  • 20
    • 0030916198 scopus 로고    scopus 로고
    • PAS, present, and future: Clues to the origins of circadian clocks
    • Kay, S. A. (1997) PAS, present, and future: clues to the origins of circadian clocks. Science 276 : 753 754.
    • (1997) Science , vol.276 , pp. 753-754
    • Kay, S.A.1
  • 21
    • 0345708353 scopus 로고    scopus 로고
    • The mammalian basic helix-loop-helix/PAS family of transcriptional regulators
    • Kewley, R. J., Whitelaw, M. L. Chapman-Smith, A. (2004) The mammalian basic helix-loop-helix/PAS family of transcriptional regulators. Int J Biochem Cell Biol 36 : 189 204.
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 189-204
    • Kewley, R.J.1    Whitelaw, M.L.2    Chapman-Smith, A.3
  • 22
    • 15444362702 scopus 로고    scopus 로고
    • Crystal structures of deoxy and CO-bound bjFixLH reveal details of ligand recognition and signaling
    • Key, J. Moffat, K. (2005) Crystal structures of deoxy and CO-bound bjFixLH reveal details of ligand recognition and signaling. Biochemistry 44 : 4627 4635.
    • (2005) Biochemistry , vol.44 , pp. 4627-4635
    • Key, J.1    Moffat, K.2
  • 23
    • 33947412138 scopus 로고    scopus 로고
    • Structure of the redox sensor domain of Azotobacter vinelandii NifL at atomic resolution: Signaling, dimerization, and mechanism
    • Key, J., Hefti, M., Purcell, E. B. Moffat, K. (2007) Structure of the redox sensor domain of Azotobacter vinelandii NifL at atomic resolution: signaling, dimerization, and mechanism. Biochemistry 46 : 3614 3623.
    • (2007) Biochemistry , vol.46 , pp. 3614-3623
    • Key, J.1    Hefti, M.2    Purcell, E.B.3    Moffat, K.4
  • 25
    • 0026314893 scopus 로고
    • The Drosophila single-minded gene encodes a helix-loop-helix protein that acts as a master regulator of CNS midline development
    • Nambu, J. R., Lewis, J. O., Wharton, K. A., Jr. Crews, S. T. (1991) The Drosophila single-minded gene encodes a helix-loop-helix protein that acts as a master regulator of CNS midline development. Cell 67 : 1157 1167.
    • (1991) Cell , vol.67 , pp. 1157-1167
    • Nambu, J.R.1    Lewis, J.O.2    Wharton Jr., K.A.3    Crews, S.T.4
  • 27
    • 0018189924 scopus 로고
    • Complementation analysis and deletion mapping of Escherichia coli mutants defective in chemotaxis
    • Parkinson, J. S. (1978) Complementation analysis and deletion mapping of Escherichia coli mutants defective in chemotaxis. J Bacteriol 135 : 45 53.
    • (1978) J Bacteriol , vol.135 , pp. 45-53
    • Parkinson, J.S.1
  • 28
    • 0032568630 scopus 로고    scopus 로고
    • Photoactive yellow protein: A structural prototype for the three-dimensional fold of the PAS domain superfamily
    • Pellequer, J. L., Wager-Smith, K. A., Kay, S. A. Getzoff, E. D. (1998) Photoactive yellow protein: a structural prototype for the three-dimensional fold of the PAS domain superfamily. Proc Natl Acad Sci USA 95 : 5884 5890.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 5884-5890
    • Pellequer, J.L.1    Wager-Smith, K.A.2    Kay, S.A.3    Getzoff, E.D.4
  • 29
    • 0030883388 scopus 로고    scopus 로고
    • The Aer protein and the serine chemoreceptor Tsr independently sense intracellular energy levels and transduce oxygen, redox, and energy signals for Escherichia coli behavior
    • Rebbapragada, A., Johnson, M. S., Harding, G. P., Zuccarelli, A. J., Fletcher, H. M., Zhulin, I. B. Taylor, B. L. (1997) The Aer protein and the serine chemoreceptor Tsr independently sense intracellular energy levels and transduce oxygen, redox, and energy signals for Escherichia coli behavior. Proc Natl Acad Sci USA 94 : 10541 10546.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10541-10546
    • Rebbapragada, A.1    Johnson, M.S.2    Harding, G.P.3    Zuccarelli, A.J.4    Fletcher, H.M.5    Zhulin, I.B.6    Taylor, B.L.7
  • 30
    • 0034029031 scopus 로고    scopus 로고
    • PAS domain residues involved in signal transduction by the Aer redox sensor of Escherichia coli
    • Repik, A., Rebbapragada, A., Johnson, M. S., Haznedar, J. O., Zhulin, I. B. Taylor, B. L. (2000) PAS domain residues involved in signal transduction by the Aer redox sensor of Escherichia coli. Mol Microbiol 36 : 806 816.
    • (2000) Mol Microbiol , vol.36 , pp. 806-816
    • Repik, A.1    Rebbapragada, A.2    Johnson, M.S.3    Haznedar, J.O.4    Zhulin, I.B.5    Taylor, B.L.6
  • 31
    • 34548356914 scopus 로고    scopus 로고
    • Aer on the inside looking out: Paradigm for a PAS-HAMP role in sensing oxygen, redox and energy
    • Taylor, B. L. (2007) Aer on the inside looking out: paradigm for a PAS-HAMP role in sensing oxygen, redox and energy. Mol Microbiol 65 : 1415 1424.
    • (2007) Mol Microbiol , vol.65 , pp. 1415-1424
    • Taylor, B.L.1
  • 32
    • 0032990441 scopus 로고    scopus 로고
    • PAS domains: Internal sensors of oxygen, redox potential, and light
    • Taylor, B. L. Zhulin, I. B. (1999) PAS domains: internal sensors of oxygen, redox potential, and light. Microbiol Mol Biol Rev 63 : 479 506.
    • (1999) Microbiol Mol Biol Rev , vol.63 , pp. 479-506
    • Taylor, B.L.1    Zhulin, I.B.2
  • 33
    • 0032694979 scopus 로고    scopus 로고
    • Aerotaxis and other energy-sensing behavior in bacteria
    • Taylor, B. L., Zhulin, I. B. Johnson, M. S. (1999) Aerotaxis and other energy-sensing behavior in bacteria. Annu Rev Microbiol 53 : 103 128.
    • (1999) Annu Rev Microbiol , vol.53 , pp. 103-128
    • Taylor, B.L.1    Zhulin, I.B.2    Johnson, M.S.3
  • 34
    • 34250804328 scopus 로고    scopus 로고
    • Oxygen and redox sensing by two-component systems that regulate behavioral responses: Behavioral assays and structural studies of aer using in vivo disulfide cross-linking
    • Taylor, B. L., Watts, K. J. Johnson, M. S. (2007) Oxygen and redox sensing by two-component systems that regulate behavioral responses: behavioral assays and structural studies of aer using in vivo disulfide cross-linking. Methods Enzymol 422 : 190 232.
    • (2007) Methods Enzymol , vol.422 , pp. 190-232
    • Taylor, B.L.1    Watts, K.J.2    Johnson, M.S.3
  • 35
    • 64349123371 scopus 로고    scopus 로고
    • Structure of the Redox Sensor Domain of Methylococcus capsulatus (Bath) MmoS
    • Ukaegbu, U. E. Rosenzweig, A. C. (2009) Structure of the Redox Sensor Domain of Methylococcus capsulatus (Bath) MmoS. Biochemistry 48 : 2207 2215.
    • (2009) Biochemistry , vol.48 , pp. 2207-2215
    • Ukaegbu, U.E.1    Rosenzweig, A.C.2
  • 36
    • 14844325781 scopus 로고    scopus 로고
    • Reducing mutational bias in random protein libraries
    • Vanhercke, T., Ampe, C., Tirry, L. Denolf, P. (2005) Reducing mutational bias in random protein libraries. Anal Biochem 339 : 9 14.
    • (2005) Anal Biochem , vol.339 , pp. 9-14
    • Vanhercke, T.1    Ampe, C.2    Tirry, L.3    Denolf, P.4
  • 37
    • 6044254952 scopus 로고    scopus 로고
    • Interactions between the PAS and HAMP domains of the Escherichia coli aerotaxis receptor Aer
    • Watts, K. J., Ma, Q., Johnson, M. S. Taylor, B. L. (2004) Interactions between the PAS and HAMP domains of the Escherichia coli aerotaxis receptor Aer. J Bacteriol 186 : 7440 7449.
    • (2004) J Bacteriol , vol.186 , pp. 7440-7449
    • Watts, K.J.1    Ma, Q.2    Johnson, M.S.3    Taylor, B.L.4
  • 38
    • 33644854244 scopus 로고    scopus 로고
    • Function of the N-terminal cap of the PAS domain in signaling by the aerotaxis receptor Aer
    • Watts, K. J., Sommer, K., Fry, S. L., Johnson, M. S. Taylor, B. L. (2006) Function of the N-terminal cap of the PAS domain in signaling by the aerotaxis receptor Aer. J Bacteriol 188 : 2154 2162.
    • (2006) J Bacteriol , vol.188 , pp. 2154-2162
    • Watts, K.J.1    Sommer, K.2    Fry, S.L.3    Johnson, M.S.4    Taylor, B.L.5
  • 39
    • 76649086069 scopus 로고    scopus 로고
    • PAS domain containing chemoreceptor couples dynamic changes in metabolism with chemotaxis
    • Xie, Z., Ulrich, L. E., Zhulin, I. B. Alexandre, G. (2010) PAS domain containing chemoreceptor couples dynamic changes in metabolism with chemotaxis. Proc Natl Acad Sci USA 107 : 2235 2240.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 2235-2240
    • Xie, Z.1    Ulrich, L.E.2    Zhulin, I.B.3    Alexandre, G.4
  • 41
    • 0030695117 scopus 로고    scopus 로고
    • How do bacteria avoid high oxygen concentrations?
    • Zhulin, I. B., Johnson, M. S. Taylor, B. L. (1997) How do bacteria avoid high oxygen concentrations? Biosci Rep 17 : 335 342.
    • (1997) Biosci Rep , vol.17 , pp. 335-342
    • Zhulin, I.B.1    Johnson, M.S.2    Taylor, B.L.3


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