메뉴 건너뛰기




Volumn 188, Issue 6, 2006, Pages 2154-2162

Function of the N-terminal cap of the PAS domain in signaling by the aerotaxis receptor Aer

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CYSTEINE; DIMER; OXYGEN; PROTEIN AER; UNCLASSIFIED DRUG;

EID: 33644854244     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.188.6.2154-2162.2006     Document Type: Article
Times cited : (20)

References (62)
  • 1
  • 2
    • 0036774056 scopus 로고    scopus 로고
    • Structure and interactions of PAS kinase N-terminal PAS domain. Model for intramolecular kinase regulation
    • Amezcua, C., S. Harper, J. Rutter, and K. Gardner. 2002. Structure and interactions of PAS kinase N-terminal PAS domain. Model for intramolecular kinase regulation. Structure (Camb) 10:1349-1361.
    • (2002) Structure (Camb) , vol.10 , pp. 1349-1361
    • Amezcua, C.1    Harper, S.2    Rutter, J.3    Gardner, K.4
  • 3
    • 31344454302 scopus 로고    scopus 로고
    • Topology and boundaries of the aerotaxis receptor Aer in the membrane of Escherichia coli
    • Amin, D. N., B. L. Taylor, and M. S. Johnson. 2006. Topology and boundaries of the aerotaxis receptor Aer in the membrane of Escherichia coli. J. Bacteriol. 188:894-901.
    • (2006) J. Bacteriol. , vol.188 , pp. 894-901
    • 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., and C. P. Ponting. 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., L. A. Barnes, Y. Gitin, and J. S. Parkinson. 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
    • 0030925238 scopus 로고    scopus 로고
    • A signal transducer for aerotaxis in Escherichia coli
    • Bibikov, S. I., R. Biran, K. E. Rudd, and J. S. Parkinson. 1997. A signal transducer for aerotaxis in Escherichia coli. J. Bacteriol. 179:4075-4079.
    • (1997) J. Bacteriol. , vol.179 , pp. 4075-4079
    • Bibikov, S.I.1    Biran, R.2    Rudd, K.E.3    Parkinson, J.S.4
  • 7
    • 0029110488 scopus 로고
    • A structure of photoactive yellow protein, a cytosolic photoreceptor: Unusual fold, active site, and chromophore
    • Borgstahl, G. E., D. R. Williams, and E. D. Getzoff. 1995. 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
  • 8
    • 0017807890 scopus 로고
    • Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the P15A cryptic miniplasmid
    • Chang, A. C., and S. N. Cohen. 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
  • 9
    • 0034727659 scopus 로고    scopus 로고
    • Probing the nature of the blue-shifted intermediate of photoactive yellow protein in solution by NMR: Hydrogen-deuterium exchange data and pH studies
    • Craven, C. J., N. M. Derix, J. Hendriks, R. Boelens, K. J. Hellingwerf, and R. Kaptein. 2000. Probing the nature of the blue-shifted intermediate of photoactive yellow protein in solution by NMR: hydrogen-deuterium exchange data and pH studies. Biochemistry 39:14392-14399.
    • (2000) Biochemistry , vol.39 , pp. 14392-14399
    • Craven, C.J.1    Derix, N.M.2    Hendriks, J.3    Boelens, R.4    Hellingwerf, K.J.5    Kaptein, R.6
  • 11
    • 0035853139 scopus 로고    scopus 로고
    • Structure of a flavin-binding plant photoreceptor domain: Insights into light-mediated signal transduction
    • Crosson, S., and K. Moffat. 2001. Structure of a flavin-binding plant photoreceptor domain: insights into light-mediated signal transduction. Proc. Natl. Acad. Sci. USA 98:2995-3000.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2995-3000
    • Crosson, S.1    Moffat, K.2
  • 12
    • 0022459160 scopus 로고
    • Inversion of aerotactic response in Escherichia coli deficient in cheB protein methylesterase
    • Dang, C. V., M. Niwano, J. Ryu, and B. L. Taylor. 1986. Inversion of aerotactic response in Escherichia coli deficient in cheB protein methylesterase. J. Bacteriol. 166:275-280.
    • (1986) J. Bacteriol. , vol.166 , pp. 275-280
    • Dang, C.V.1    Niwano, M.2    Ryu, J.3    Taylor, B.L.4
  • 14
    • 0034938152 scopus 로고    scopus 로고
    • Competence repression under oxygen limitation through the two-component MicAB signal-transducing system in Streptococcus pneumoniae and involvement of the PAS domain of MicB
    • Echenique, J. R., and M. C. Trombe. 2001. Competence repression under oxygen limitation through the two-component MicAB signal-transducing system in Streptococcus pneumoniae and involvement of the PAS domain of MicB. J. Bacteriol. 183:4599-4608.
    • (2001) J. Bacteriol. , vol.183 , pp. 4599-4608
    • Echenique, J.R.1    Trombe, M.C.2
  • 15
    • 0346734132 scopus 로고    scopus 로고
    • Structural basis for PAS domain heterodimerization in the basic helix-loop-helix-PAS transcription factor hypoxia-inducible factor
    • Erbel, P. J., P. B. Card, O. Karakuzu, R. K. Bruick, and K. H. Gardner. 2003. Structural basis for PAS domain heterodimerization in the basic helix-loop-helix-PAS transcription factor hypoxia-inducible factor. Proc. Natl. Acad. Sci. USA 100:15504-15509.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 15504-15509
    • Erbel, P.J.1    Card, P.B.2    Karakuzu, O.3    Bruick, R.K.4    Gardner, K.H.5
  • 16
    • 0035312774 scopus 로고    scopus 로고
    • Transmembrane signaling in bacterial chemoreceptors
    • Falke, J. J., and G. L. Hazelbauer. 2001. Transmembrane signaling in bacterial chemoreceptors. Trends Biochem. Sci. 26:257-265.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 257-265
    • Falke, J.J.1    Hazelbauer, G.L.2
  • 17
    • 0030660403 scopus 로고    scopus 로고
    • High- and low-abundance chemoreceptors in Escherichia coli: Differential activities associated with closely related cytoplasmic domains
    • Feng, X., J. W. Baumgartner, and G. L. Hazelbauer. 1997. High- and low-abundance chemoreceptors in Escherichia coli: differential activities associated with closely related cytoplasmic domains. J. Bacteriol. 179:6714-6720.
    • (1997) J. Bacteriol. , vol.179 , pp. 6714-6720
    • Feng, X.1    Baumgartner, J.W.2    Hazelbauer, G.L.3
  • 19
    • 0034636144 scopus 로고    scopus 로고
    • New mechanistic insights from structural studies of the oxygen-sensing domain of Bradyrhizobium japonicum FixL
    • Gong, W., B. Hao, and M. K. Chan. 2000. New mechanistic insights from structural studies of the oxygen-sensing domain of Bradyrhizobium japonicum FixL. Biochemistry 39:3955-3962.
    • (2000) Biochemistry , vol.39 , pp. 3955-3962
    • Gong, W.1    Hao, B.2    Chan, M.K.3
  • 21
    • 0037195260 scopus 로고    scopus 로고
    • Structure-based mechanism of O2 sensing and ligand discrimination by the FixL heme domain of Bradyrhizobium japonicum
    • Hao, B., C. Isaza, J. Arndt, M. Soltis, and M. K. Chan. 2002. Structure-based mechanism of O2 sensing and ligand discrimination by the FixL heme domain of Bradyrhizobium japonicum. Biochemistry 41:12952-12958.
    • (2002) Biochemistry , vol.41 , pp. 12952-12958
    • Hao, B.1    Isaza, C.2    Arndt, J.3    Soltis, M.4    Chan, M.K.5
  • 22
    • 0345707600 scopus 로고    scopus 로고
    • Role of an N-terminal loop in the secondary structural change of photoactive yellow protein
    • Harigai, M., Y. Imamoto, H. Kamikubo, Y. Yamazaki, and M. Kataoka. 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
  • 23
    • 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., Q. Ma, M. S. Johnson, A. V. Repik, and B. L. Taylor. 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
  • 24
    • 0029875231 scopus 로고    scopus 로고
    • Azotobacter vinelandii NIFL is a flavoprotein that modulates transcriptional activation of nitrogen-fixation genes via redox-sensitive switch
    • Hill, S., S. Austin, T. Eydmann, T. Jones, and R. Dixon. 1996. Azotobacter vinelandii NIFL is a flavoprotein that modulates transcriptional activation of nitrogen-fixation genes via redox-sensitive switch. Proc. Natl. Acad. Sci. USA 93:2143-2148.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2143-2148
    • Hill, S.1    Austin, S.2    Eydmann, T.3    Jones, T.4    Dixon, R.5
  • 25
    • 0020792024 scopus 로고
    • Luminometric determination of FAD in subpicomole quantities
    • Hinkkanen, A., and K. Decker. 1983. Luminometric determination of FAD in subpicomole quantities. Anal. Biochem. 132:202-208.
    • (1983) Anal. Biochem. , vol.132 , pp. 202-208
    • Hinkkanen, A.1    Decker, K.2
  • 26
    • 0029910912 scopus 로고    scopus 로고
    • Detecting the conformational change of transmembrane signaling in a bacterial chemoreceptor by measuring effects on disulfide cross-linking in vivo
    • Hughson, A. G., and G. L. Hazelbauer. 1996. Detecting the conformational change of transmembrane signaling in a bacterial chemoreceptor by measuring effects on disulfide cross-linking in vivo. Proc. Natl. Acad. Sci. USA 93:11546-11551.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 11546-11551
    • Hughson, A.G.1    Hazelbauer, G.L.2
  • 27
    • 0037137227 scopus 로고    scopus 로고
    • Light-induced global conformational change of photoactive yellow protein in solution
    • Imamoto, Y., H. Kamikubo, M. Harigai, N. Shimizu, and M. Kataoka. 2002. Light-induced global conformational change of photoactive yellow protein in solution. Biochemistry 41:13595-13601.
    • (2002) Biochemistry , vol.41 , pp. 13595-13601
    • Imamoto, Y.1    Kamikubo, H.2    Harigai, M.3    Shimizu, N.4    Kataoka, M.5
  • 28
    • 0031922353 scopus 로고    scopus 로고
    • Suppressor mutation analysis of the sensory rhodopsin I-transducer complex: Insights into the color-sensing mechanism
    • Jung, K. H., and J. L. Spudich. 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
  • 29
    • 0014871777 scopus 로고
    • Enzymic determination of uracil nucleotides in tissues
    • Keppler, D., J. Rudigler, and K. Decker. 1970. Enzymic determination of uracil nucleotides in tissues. Anal. Biochem. 38:105-114.
    • (1970) Anal. Biochem. , vol.38 , pp. 105-114
    • Keppler, D.1    Rudigler, J.2    Decker, K.3
  • 30
    • 0019395341 scopus 로고
    • Cytoplasmic pH mediates pH taxis and weak-acid repellent taxis of bacteria
    • Kihara, M., and R. M. Macnab. 1981. Cytoplasmic pH mediates pH taxis and weak-acid repellent taxis of bacteria. J. Bacteriol. 145:1209-1221.
    • (1981) J. Bacteriol. , vol.145 , pp. 1209-1221
    • Kihara, M.1    Macnab, R.M.2
  • 31
    • 0001690764 scopus 로고    scopus 로고
    • Four-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor
    • Kim, K. K., H. Yokota, and S. H. Kim. 1999. Four-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor. Nature 400:787-792.
    • (1999) Nature , vol.400 , pp. 787-792
    • Kim, K.K.1    Yokota, H.2    Kim, S.H.3
  • 32
    • 0037015003 scopus 로고    scopus 로고
    • Dynamic and clustering model of bacterial chemotaxis receptors: Structural basis for signaling and high sensitivity
    • Kim, S. H., W. Wang, and K. K. Kim. 2002. Dynamic and clustering model of bacterial chemotaxis receptors: structural basis for signaling and high sensitivity. Proc. Natl. Acad. Sci. USA 99:11611-11615.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11611-11615
    • Kim, S.H.1    Wang, W.2    Kim, K.K.3
  • 33
    • 2442624510 scopus 로고    scopus 로고
    • A redox-controlled molecular switch revealed by the crystal structure of a bacterial heme PAS sensor
    • Kurokawa, H., D. S. Lee, M. Watanabe, I. Sagami, B. Mikami, C. S. Raman, and T. Shimizu. 2004. A redox-controlled molecular switch revealed by the crystal structure of a bacterial heme PAS sensor. J. Biol. Chem. 279:20186-20193.
    • (2004) J. Biol. Chem. , vol.279 , pp. 20186-20193
    • Kurokawa, H.1    Lee, D.S.2    Watanabe, M.3    Sagami, I.4    Mikami, B.5    Raman, C.S.6    Shimizu, T.7
  • 34
    • 20344372661 scopus 로고    scopus 로고
    • Adaptational assistance in clusters of bacterial chemoreceptors
    • Li, M., and G. L. Hazelbauer. 2005. Adaptational assistance in clusters of bacterial chemoreceptors. Mol. Microbiol. 56:1617-1626.
    • (2005) Mol. Microbiol. , vol.56 , pp. 1617-1626
    • Li, M.1    Hazelbauer, G.L.2
  • 35
    • 2942610579 scopus 로고    scopus 로고
    • Cellular stoichiometry of the components of the chemotaxis signaling complex
    • Li, M., and G. L. Hazelbauer. 2004. Cellular stoichiometry of the components of the chemotaxis signaling complex. J. Bacteriol. 186:3687-3694.
    • (2004) J. Bacteriol. , vol.186 , pp. 3687-3694
    • Li, M.1    Hazelbauer, G.L.2
  • 36
    • 0034608895 scopus 로고    scopus 로고
    • Differences in the polar clustering of the high- and low-abundance chemoreceptors of Escherichia coli
    • Lybarger, S. R., and J. R. Maddock. 2000. Differences in the polar clustering of the high- and low-abundance chemoreceptors of Escherichia coli. Proc. Natl. Acad. Sci. USA 97:8057-8062.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8057-8062
    • Lybarger, S.R.1    Maddock, J.R.2
  • 37
    • 11144338821 scopus 로고    scopus 로고
    • Genetic analysis of the HAMP domain of the Aer aerotaxis sensor localizes flavin adenine dinucleotide-binding determinants to the AS-2 helix
    • Ma, Q., M. S. Johnson, and B. L. Taylor. 2005. Genetic analysis of the HAMP domain of the Aer aerotaxis sensor localizes flavin adenine dinucleotide-binding determinants to the AS-2 helix. J. Bacteriol. 187:193-201.
    • (2005) J. Bacteriol. , vol.187 , pp. 193-201
    • Ma, Q.1    Johnson, M.S.2    Taylor, B.L.3
  • 38
    • 6044247517 scopus 로고    scopus 로고
    • The Aer protein of Escherichia coli forms a homodimer independent of the signaling domain and FAD binding
    • Ma, Q., F. Roy, S. Herrmann, B. L. Taylor, and M. S. Johnson. 2004. The Aer protein of Escherichia coli forms a homodimer independent of the signaling domain and FAD binding. J. Bacteriol. 186:7456-7459.
    • (2004) J. Bacteriol. , vol.186 , pp. 7456-7459
    • Ma, Q.1    Roy, F.2    Herrmann, S.3    Taylor, B.L.4    Johnson, M.S.5
  • 39
    • 0009481832 scopus 로고
    • Bacterial flagella rotating in bundles: A study in helical geometry
    • Macnab, R. M. 1977. Bacterial flagella rotating in bundles: a study in helical geometry. Proc. Natl. Acad. Sci. USA 74:221-225.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 221-225
    • Macnab, R.M.1
  • 40
    • 0034636982 scopus 로고    scopus 로고
    • Sensory mechanism of oxygen sensor FixL from Rhizobium meliloti: Crystallographic, mutagenesis and resonance Raman spectroscopic studies
    • Miyatake, H., M. Mukai, S. Y. Park, S. Adachi, K. Tamura, H. Nakamura, K. Nakamura, T. Tsuchiya, T. Iizuka, and Y. Shiro. 2000. Sensory mechanism of oxygen sensor FixL from Rhizobium meliloti: crystallographic, mutagenesis and resonance Raman spectroscopic studies. J. Mol. Biol. 301:415-431.
    • (2000) J. Mol. Biol. , vol.301 , pp. 415-431
    • Miyatake, H.1    Mukai, M.2    Park, S.Y.3    Adachi, S.4    Tamura, K.5    Nakamura, H.6    Nakamura, K.7    Tsuchiya, T.8    Iizuka, T.9    Shiro, Y.10
  • 41
    • 0032567106 scopus 로고    scopus 로고
    • Crystal structure and functional analysis of the HERG potassium channel N terminus: A eukaryotic PAS domain
    • Morais Cabral, J. H., A. Lee, S. L. Cohen, B. T. Chait, M. Li, and R. Mackinnon. 1998. Crystal structure and functional analysis of the HERG potassium channel N terminus: a eukaryotic PAS domain. Cell 95:649-655.
    • (1998) Cell , vol.95 , pp. 649-655
    • Morais Cabral, J.H.1    Lee, A.2    Cohen, S.L.3    Chait, B.T.4    Li, M.5    Mackinnon, R.6
  • 42
    • 0017821654 scopus 로고
    • Attraction by repellents: An error in sensory information processing by bacterial mutants
    • Muskavitch, M. A., E. N. Kort, M. S. Springer, M. F. Goy, and J. Adler. 1978. Attraction by repellents: an error in sensory information processing by bacterial mutants. Science 201:63-65.
    • (1978) Science , vol.201 , pp. 63-65
    • Muskavitch, M.A.1    Kort, E.N.2    Springer, M.S.3    Goy, M.F.4    Adler, J.5
  • 43
    • 0030696872 scopus 로고    scopus 로고
    • Thermosensing properties of mutant aspartate chemoreceptors with methyl-accepting sites replaced singly or multiply by alanine
    • Nishiyama, S., T. Nara, M. Homma, Y. Imae, and I. Kawagishi. 1997. Thermosensing properties of mutant aspartate chemoreceptors with methyl-accepting sites replaced singly or multiply by alanine. J. Bacteriol. 179:6573-6580.
    • (1997) J. Bacteriol. , vol.179 , pp. 6573-6580
    • Nishiyama, S.1    Nara, T.2    Homma, M.3    Imae, Y.4    Kawagishi, I.5
  • 45
    • 0019979301 scopus 로고
    • Isolation and behavior of Escherichia coli deletion mutants lacking chemotaxis functions
    • Parkinson, J. S., and S. E. Houts. 1982. Isolation and behavior of Escherichia coli deletion mutants lacking chemotaxis functions. J. Bacteriol. 151:106-113.
    • (1982) J. Bacteriol. , vol.151 , pp. 106-113
    • Parkinson, J.S.1    Houts, S.E.2
  • 46
    • 0032568630 scopus 로고    scopus 로고
    • Photoactive yellow protein: A structural prototype for the three-dimensional fold of the PAS domain superfamily
    • Pellequer, J. L., K. A. Wager-Smith, S. A. Kay, and E. D. Getzoff. 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
  • 47
    • 0037452676 scopus 로고    scopus 로고
    • Crystal structure of a photoactive yellow protein from a sensor histidine kinase: Conformational variability and signal transduction
    • Rajagopal, S., and K. Moffat. 2003. Crystal structure of a photoactive yellow protein from a sensor histidine kinase: conformational variability and signal transduction. Proc. Natl. Acad. Sci. USA 100:1649-1654.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 1649-1654
    • Rajagopal, S.1    Moffat, K.2
  • 48
    • 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., M. S. Johnson, G. P. Harding, A. J. Zuccarelli, H. M. Fletcher, I. B. Zhulin, and B. L. Taylor. 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
  • 49
    • 0034029031 scopus 로고    scopus 로고
    • PAS domain residues involved in signal transduction by the Aer redox sensor of Escherichia coli
    • Repik, A., A. Rebbapragada, M. S. Johnson, J. O. Haznedar, I. B. Zhulin, and B. L. Taylor. 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
  • 50
    • 0031573763 scopus 로고    scopus 로고
    • NifL of Klebsiella pneumoniae carries an N-terminally bound FAD cofactor, which is not directly required for the inhibitory function of NifL
    • Schmitz, R. A. 1997. NifL of Klebsiella pneumoniae carries an N-terminally bound FAD cofactor, which is not directly required for the inhibitory function of NifL. FEMS Microbiol. Lett. 157:313-318.
    • (1997) FEMS Microbiol. Lett. , vol.157 , pp. 313-318
    • Schmitz, R.A.1
  • 51
    • 0023279515 scopus 로고
    • Oxygen as attractant and repellent in bacterial chemotaxis
    • Shioi, J., C. V. Dang, and B. L. Taylor. 1987. Oxygen as attractant and repellent in bacterial chemotaxis. J. Bacteriol. 169:3118-3123.
    • (1987) J. Bacteriol. , vol.169 , pp. 3118-3123
    • Shioi, J.1    Dang, C.V.2    Taylor, B.L.3
  • 52
    • 0032478673 scopus 로고    scopus 로고
    • Rewiring a receptor: Negative output from positive input
    • Taylor, B. L., and M. S. Johnson. 1998. Rewiring a receptor: negative output from positive input. FEBS Lett. 425:377-381.
    • (1998) FEBS Lett. , vol.425 , pp. 377-381
    • Taylor, B.L.1    Johnson, M.S.2
  • 53
    • 0032990441 scopus 로고    scopus 로고
    • PAS domains: Internal sensors of oxygen, redox potential, and light
    • Taylor, B. L., and I. B. Zhulin. 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
  • 54
    • 0035906913 scopus 로고    scopus 로고
    • The role of the N-terminal domain of photoactive yellow protein in the transient partial unfolding during signalling state formation
    • van der Horst, M. A., I. H. van Stokkum, W. Crielaard, and K. J. Hellingwerf. 2001. The role of the N-terminal domain of photoactive yellow protein in the transient partial unfolding during signalling state formation. FEBS Lett. 497:26-30.
    • (2001) FEBS Lett. , vol.497 , pp. 26-30
    • Van Der Horst, M.A.1    Van Stokkum, I.H.2    Crielaard, W.3    Hellingwerf, K.J.4
  • 56
    • 33644849608 scopus 로고    scopus 로고
    • Minimal requirements for oxygen sensing by the aerotaxis receptor Aer
    • Watts, K. J., M. S. Johnson, and B. L. Taylor. 2006. Minimal requirements for oxygen sensing by the aerotaxis receptor Aer. Mol. Microbiol. 59:1317-1326.
    • (2006) Mol. Microbiol. , vol.59 , pp. 1317-1326
    • Watts, K.J.1    Johnson, M.S.2    Taylor, B.L.3
  • 57
    • 6044254952 scopus 로고    scopus 로고
    • Interactions between the PAS and HAMP domains of the Escherichia coli aerotaxis receptor Aer
    • Watts, K. J., Q. Ma, M. S. Johnson, and B. L. Taylor. 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
  • 60
    • 6044272040 scopus 로고    scopus 로고
    • Structure of the PAS fold and signal transduction mechanisms
    • S. T. Crews (ed.). Kluwer Academic Publishers, Boston, Mass.
    • Zhong, X., B. Hao, and M. K. Chan. 2003. Structure of the PAS fold and signal transduction mechanisms, p. 1-16. In S. T. Crews (ed.), PAS proteins: regulators and sensors of development and physiology. Kluwer Academic Publishers, Boston, Mass.
    • (2003) PAS Proteins: Regulators and Sensors of Development and Physiology , pp. 1-16
    • Zhong, X.1    Hao, B.2    Chan, M.K.3
  • 61
    • 0030972243 scopus 로고    scopus 로고
    • Glycerol elicits energy taxis of Escherichia coli and Salmonella typhimurium
    • Zhulin, I. B., E. H. Rowsell, M. S. Johnson, and B. L.Taylor. 1997. Glycerol elicits energy taxis of Escherichia coli and Salmonella typhimurium. J. Bacteriol. 179:3196-3201.
    • (1997) J. Bacteriol. , vol.179 , pp. 3196-3201
    • Zhulin, I.B.1    Rowsell, E.H.2    Johnson, M.S.3    Taylor, B.L.4
  • 62
    • 0030884102 scopus 로고    scopus 로고
    • PAS domain S-boxes in archaea, bacteria and sensors for oxygen and redox
    • Zhulin, I. B., B. L. Taylor, and R. Dixon. 1997. PAS domain S-boxes in archaea, bacteria and sensors for oxygen and redox. Trends Biochem. Sci. 22:331-333.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 331-333
    • Zhulin, I.B.1    Taylor, B.L.2    Dixon, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.