메뉴 건너뛰기




Volumn 64, Issue , 2010, Pages 101-122

Signaling Mechanisms of HAMP domains in chemoreceptors and sensor kinases

Author keywords

conformational coupling; dynamic bundle; phase clash; piston model; transmembrane signaling

Indexed keywords

ADENYLATE CYCLASE; ASPARTIC ACID; BACTERIAL PROTEIN; CHEA KINASE; METHYL ACCEPTING CHEMOTAXIS PROTEIN; PHOSPHATASE; PROTEIN AER; PROTEIN ENVZ; PROTEIN HISTIDINE KINASE; PROTEIN HTR2; PROTEIN NARX; SERINE; UNCLASSIFIED DRUG;

EID: 77957949467     PISSN: 00664227     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.micro.112408.134215     Document Type: Review
Times cited : (157)

References (65)
  • 1
    • 77951643013 scopus 로고    scopus 로고
    • Structure of concatenated HAMP domains provides a mechanism for signal transduction
    • Airola M, Watts KJ, Crane BR. 2010. Structure of concatenated HAMP domains provides a mechanism for signal transduction. Structure 18:436-48
    • Structure , vol.18 , pp. 436-48
    • Airola, M.1    Watts, K.J.2    Crane, B.R.3
  • 2
    • 33847249975 scopus 로고    scopus 로고
    • Evolutionary genomics reveals conserved structural determinants of signaling and adaptation in microbial chemoreceptors
    • Alexander RP, Zhulin IB. 2007. Evolutionary genomics reveals conserved structural determinants of signaling and adaptation in microbial chemoreceptors. Proc. Natl. Acad. Sci. USA 104:2885-90
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 2885-90
    • Alexander, R.P.1    Zhulin, I.B.2
  • 3
    • 53849112614 scopus 로고    scopus 로고
    • Mutational analysis of the connector segment in the HAMP domain of Tsr, the Escherichia coli serine chemoreceptor
    • Ames P, Zhou Q, Parkinson JS. 2008. Mutational analysis of the connector segment in the HAMP domain of Tsr, the Escherichia coli serine chemoreceptor. J. Bacteriol. 190:6676-85
    • (2008) J. Bacteriol. , vol.190 , pp. 6676-85
    • Ames, P.1    Zhou, Q.2    Parkinson, J.S.3
  • 4
    • 34248371291 scopus 로고    scopus 로고
    • The signaling helix: A common functional theme in diverse signaling proteins
    • DOI 10.1186/1745-6150-1-25
    • Anantharaman V, Balaji S, Aravind L. 2006. The signaling helix: a common functional theme in diverse signaling proteins. Biol. Direct. 1:25. doi: 10.1186/1745-6150-1-25 (Pubitemid 46730975)
    • (2006) Biology Direct , vol.1 , pp. 25
    • Anantharaman, V.1    Balaji, S.2    Aravind, L.3
  • 5
    • 0037216619 scopus 로고    scopus 로고
    • Mutational analysis of a conserved signal-transducing element: The HAMP linker of the Escherichia coli nitrate sensor NarX
    • Appleman JA, Stewart V. 2003. Mutational analysis of a conserved signal-transducing element: the HAMP linker of the Escherichia coli nitrate sensor NarX. J. Bacteriol. 185:89-97
    • (2003) J. Bacteriol. , vol.185 , pp. 89-97
    • Appleman, J.A.1    Stewart, V.2
  • 6
    • 0032766134 scopus 로고    scopus 로고
    • The cytoplasmic helical linker domain of receptor histidine ki-nase and methyl-accepting proteins is common to many prokaryotic signaling proteins
    • Aravind L, Ponting CP. 1999. The cytoplasmic helical linker domain of receptor histidine ki-nase and methyl-accepting proteins is common to many prokaryotic signaling proteins. FEMS Microbiol. Lett. 176:111-16
    • (1999) FEMS Microbiol. Lett. , vol.176 , pp. 111-16
    • Aravind, L.1    Ponting, C.P.2
  • 7
    • 0034705035 scopus 로고    scopus 로고
    • Domain organization and flavin adenine dinucleotide-binding determinants in the aerotaxis signal transducer Aer of Escherichia coli
    • Bibikov SI, Barnes LA, Gitin Y, Parkinson JS. 2000. Domain organization and flavin adenine dinucleotide-binding determinants in the aerotaxis signal transducer Aer of Escherichia coli. Proc. Natl. Acad. Sci. USA 97:5830-35
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 5830-35
    • Bibikov, S.I.1    Barnes, L.A.2    Gitin, Y.3    Parkinson, J.S.4
  • 9
    • 2942545825 scopus 로고    scopus 로고
    • Methylation-independent aerotaxis mediated by the Escherichia coli Aer protein
    • Bibikov SI, Miller AC, Gosink KK, Parkinson JS. 2004. Methylation-independent aerotaxis mediated by the Escherichia coli Aer protein. J. Bacteriol. 186:3730-37
    • (2004) J. Bacteriol. , vol.186 , pp. 3730-37
    • Bibikov, S.I.1    Miller, A.C.2    Gosink, K.K.3    Parkinson, J.S.4
  • 10
    • 2442720144 scopus 로고    scopus 로고
    • Accessibility of introduced cysteines in chemoreceptor transmembrane helices reveals boundaries interior to bracketing charged residues
    • Boldog T, Hazelbauer GL. 2004. Accessibility of introduced cysteines in chemoreceptor transmembrane helices reveals boundaries interior to bracketing charged residues. Protein Sci. 13:1466-75
    • (2004) Protein Sci. , vol.13 , pp. 1466-75
    • Boldog, T.1    Hazelbauer, G.L.2
  • 11
    • 32044450659 scopus 로고    scopus 로고
    • Structural analysis of a HAMP domain: The linker region of the phototransducer in complex with sensory rhodopsin II
    • Bordignon E, Klare JP, Doebber M, Wegener AA, Martell S, et al. 2005. Structural analysis of a HAMP domain: the linker region of the phototransducer in complex with sensory rhodopsin II. J. Biol. Chem. 280:38767-75
    • (2005) J. Biol. Chem. , vol.280 , pp. 38767-75
    • Bordignon, E.1    Klare, J.P.2    Doebber, M.3    Wegener, A.A.4    Martell, S.5
  • 12
    • 41049095848 scopus 로고    scopus 로고
    • How the "melting" and "freezing" of protein molecules may be used in cell signaling
    • Bray D, Williams D. 2008. How the "melting" and "freezing" of protein molecules may be used in cell signaling. ACS Chem. Biol. 3:89-91
    • (2008) ACS Chem. Biol. , vol.3 , pp. 89-91
    • Bray, D.1    Williams, D.2
  • 13
    • 0029957901 scopus 로고    scopus 로고
    • Heptad breaks in alpha-helical coiled coils: Stutters and stammers
    • Brown JH, Cohen C, Parry DA. 1996. Heptad breaks in alpha-helical coiled coils: stutters and stammers. Proteins 26:134-45
    • (1996) Proteins , vol.26 , pp. 134-45
    • Brown, J.H.1    Cohen, C.2    Parry, D.A.3
  • 14
    • 33646597727 scopus 로고    scopus 로고
    • Loss-and gain-of-function mutations in the F1-HAMP region of the Escherichia coli aerotaxis transducer Aer
    • Buron-Barral MC, Gosink KK, Parkinson JS. 2006. Loss-and gain-of-function mutations in the F1-HAMP region of the Escherichia coli aerotaxis transducer Aer. J. Bacteriol. 188:3477-86
    • (2006) J. Bacteriol. , vol.188 , pp. 3477-86
    • Buron-Barral, M.C.1    Gosink, K.K.2    Parkinson, J.S.3
  • 15
    • 0032575326 scopus 로고    scopus 로고
    • Cysteine and disulfide scanning reveals two amphiphilic helices in the linker region of the aspartate chemoreceptor
    • Butler SL, Falke JJ. 1998. Cysteine and disulfide scanning reveals two amphiphilic helices in the linker region of the aspartate chemoreceptor. Biochemistry 37:10746-56
    • (1998) Biochemistry , vol.37 , pp. 10746-56
    • Butler, S.L.1    Falke, J.J.2
  • 16
    • 70349795241 scopus 로고    scopus 로고
    • Structural insight into partner specificity and phosphoryl transfer in two-component signal transduction
    • Casino P, Rubio V, Marina A. 2009. Structural insight into partner specificity and phosphoryl transfer in two-component signal transduction. Cell 139:325-36
    • (2009) Cell , vol.139 , pp. 325-36
    • Casino, P.1    Rubio, V.2    Marina, A.3
  • 17
    • 0029865503 scopus 로고    scopus 로고
    • Molecular mechanism of transmembrane signaling by the aspartate receptor: A model
    • Chervitz SA, Falke JJ. 1996. Molecular mechanism of transmembrane signaling by the aspartate receptor: a model. Proc. Natl. Acad. Sci. USA 93:2545-50
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2545-50
    • Chervitz, S.A.1    Falke, J.J.2
  • 18
    • 59649092359 scopus 로고    scopus 로고
    • Structural analysis of ligand stimulation of the histidine kinase NarX
    • Cheung J, Hendrickson WA. 2009. Structural analysis of ligand stimulation of the histidine kinase NarX. Structure 17:190-201
    • (2009) Structure , vol.17 , pp. 190-201
    • Cheung, J.1    Hendrickson, W.A.2
  • 19
    • 19644374667 scopus 로고    scopus 로고
    • Conserved glycine residues in the cytoplasmic domain of the aspartate receptor play essential roles in kinase coupling and on-off switching
    • Coleman MD, Bass RB, Mehan RS, Falke JJ. 2005. Conserved glycine residues in the cytoplasmic domain of the aspartate receptor play essential roles in kinase coupling and on-off switching. Biochemistry 44:7687-95
    • (2005) Biochemistry , vol.44 , pp. 7687-95
    • Coleman, M.D.1    Bass, R.B.2    Mehan, R.S.3    Falke, J.J.4
  • 20
    • 0026747875 scopus 로고
    • Mutational analysis reveals functional similarity between NarX, a nitrate sensor in Escherichia coli K-12, and the methyl-accepting chemotaxis proteins
    • Collins LA, Egan SM, Stewart V. 1992. Mutational analysis reveals functional similarity between NarX, a nitrate sensor in Escherichia coli K-12, and the methyl-accepting chemotaxis proteins.J. Bacteriol. 174:3667-75
    • (1992) J. Bacteriol. , vol.174 , pp. 3667-75
    • Collins, L.A.1    Egan, S.M.2    Stewart, V.3
  • 21
    • 57649118508 scopus 로고    scopus 로고
    • Salt-driven equilibrium between two conformations in the HAMP domain from Natronomonas pharaonis: The language of signal transfer?
    • Doebber M, Bordignon E, Klare JP, Holterhues J, Martell S, et al. 2008. Salt-driven equilibrium between two conformations in the HAMP domain from Natronomonas pharaonis: the language of signal transfer? J. Biol. Chem. 283:28691-701
    • (2008) J. Biol. Chem. , vol.283 , pp. 28691-701
    • Doebber, M.1    Bordignon, E.2    Klare, J.P.3    Holterhues, J.4    Martell, S.5
  • 22
    • 13444283382 scopus 로고    scopus 로고
    • Tryptophan residues flanking the second trans-membrane helix (TM2) set the signaling state of the Tar chemoreceptor
    • Draheim RR, Bormans AF, Lai RZ, Manson MD. 2005. Tryptophan residues flanking the second trans-membrane helix (TM2) set the signaling state of the Tar chemoreceptor. Biochemistry 44:1268-77
    • (2005) Biochemistry , vol.44 , pp. 1268-77
    • Draheim, R.R.1    Bormans, A.F.2    Lai, R.Z.3    Manson, M.D.4
  • 23
    • 33845422855 scopus 로고    scopus 로고
    • Tuning a bacterial chemoreceptor with protein-membrane interactions
    • Draheim RR, Bormans AF, Lai RZ, Manson MD. 2006. Tuning a bacterial chemoreceptor with protein-membrane interactions. Biochemistry 45:14655-64
    • (2006) Biochemistry , vol.45 , pp. 14655-64
    • Draheim, R.R.1    Bormans, A.F.2    Lai, R.Z.3    Manson, M.D.4
  • 24
    • 77950492834 scopus 로고    scopus 로고
    • Comprehensive analysis of HAMP domains: Implications for transmembrane signal transduction
    • Dunin-Horkawicz S, Lupas AN. 2010. Comprehensive analysis of HAMP domains: implications for transmembrane signal transduction. J. Mol. Biol. 397:1156-74
    • (2010) J. Mol. Biol. , vol.397 , pp. 1156-74
    • Dunin-Horkawicz, S.1    Lupas, A.N.2
  • 25
    • 49249120898 scopus 로고    scopus 로고
    • Characterization of CetA and CetB, a bipartite energy taxis system in Campy-lobacter jejuni
    • Elliott KT, Dirita VJ. 2008. Characterization of CetA and CetB, a bipartite energy taxis system in Campy-lobacter jejuni. Mol. Microbiol. 69:1091-103
    • (2008) Mol. Microbiol. , vol.69 , pp. 1091-103
    • Elliott, K.T.1    Dirita, V.J.2
  • 26
    • 58149479212 scopus 로고    scopus 로고
    • Conserved residues in the HAMP domain define a new family of proposed bipartite energy taxis receptors
    • Elliott KT, Zhulin IB, Stuckey JA, DiRita VJ. 2009. Conserved residues in the HAMP domain define a new family of proposed bipartite energy taxis receptors. J. Bacteriol. 191:375-87
    • (2009) J. Bacteriol. , vol.191 , pp. 375-87
    • Elliott, K.T.1    Zhulin, I.B.2    Stuckey, J.A.3    Dirita, V.J.4
  • 27
    • 69849086498 scopus 로고    scopus 로고
    • The piston rises again
    • Falke JJ, Erbse AH. 2009. The piston rises again. Structure 17:1149-51
    • (2009) Structure , vol.17 , pp. 1149-51
    • Falke, J.J.1    Erbse, A.H.2
  • 28
    • 0035312774 scopus 로고    scopus 로고
    • Transmembrane signaling in bacterial chemoreceptors
    • Falke JJ, Hazelbauer GL. 2001. Transmembrane signaling in bacterial chemoreceptors. Trends. Biochem. Sci. 26:257-65
    • (2001) Trends. Biochem. Sci. , vol.26 , pp. 257-65
    • Falke, J.J.1    Hazelbauer, G.L.2
  • 29
    • 70349541000 scopus 로고    scopus 로고
    • Biological insights from structures of two-component proteins
    • Gao R, Stock AM. 2009. Biological insights from structures of two-component proteins. Annu. Rev. Microbiol. 63:133-54
    • (2009) Annu. Rev. Microbiol. , vol.63 , pp. 133-54
    • Gao, R.1    Stock, A.M.2
  • 30
    • 0037015619 scopus 로고    scopus 로고
    • Molecular basis of transmembrane signaling by sensory rhodopsin II-transducer complex
    • Gordeliy VI, Labahn J, Moukhametzianov R, Efremov R, Granzin J, et al. 2002. Molecular basis of transmembrane signaling by sensory rhodopsin II-transducer complex. Nature 419:484-87
    • (2002) Nature , vol.419 , pp. 484-87
    • Gordeliy, V.I.1    Labahn, J.2    Moukhametzianov, R.3    Efremov, R.4    Granzin, J.5
  • 31
    • 37249065137 scopus 로고    scopus 로고
    • Structural analysis of the phototactic transducer protein HtrII linker region from Natronomonas pharaonis
    • Hayashi K, Sudo Y, Jee J, Mishima M, Hara H, et al. 2007. Structural analysis of the phototactic transducer protein HtrII linker region from Natronomonas pharaonis. Biochemistry 46:14380-90
    • (2007) Biochemistry , vol.46 , pp. 14380-90
    • Hayashi, K.1    Sudo, Y.2    Jee, J.3    Mishima, M.4    Hara, H.5
  • 32
    • 37749029507 scopus 로고    scopus 로고
    • Bacterial chemoreceptors: High-performance signaling in networked arrays
    • Hazelbauer GL, Falke JJ, Parkinson JS. 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
  • 33
    • 0031929447 scopus 로고    scopus 로고
    • Sensory rhodopsin II transducer HtrII is also responsible for serine chemotaxis in the archaeon Halobacterium salinarum
    • Hou S, Brooun A, Yu HS, Freitas T, Alam M. 1998. Sensory rhodopsin II transducer HtrII is also responsible for serine chemotaxis in the archaeon Halobacterium salinarum. J. Bacteriol. 180:1600-2
    • (1998) J. Bacteriol. , vol.180 , pp. 1600-2
    • Hou, S.1    Brooun, A.2    Yu, H.S.3    Freitas, T.4    Alam, M.5
  • 34
    • 33748183257 scopus 로고    scopus 로고
    • The HAMP domain structure implies helix rotation in transmembrane signaling
    • Hulko M, Berndt F, Gruber M, Linder JU, Truffault V, et al. 2006. The HAMP domain structure implies helix rotation in transmembrane signaling. Cell 126:929-40
    • (2006) Cell , vol.126 , pp. 929-40
    • Hulko, M.1    Berndt, F.2    Gruber, M.3    Linder, J.U.4    Truffault, V.5
  • 35
    • 39049147453 scopus 로고    scopus 로고
    • Signal transmission through the HtrII transducer alters the interaction of two alpha-helices in the HAMP domain
    • Inoue K, Sasaki J, Spudich JL, Terazima M. 2008. Signal transmission through the HtrII transducer alters the interaction of two alpha-helices in the HAMP domain. J. Mol. Biol. 376:963-70
    • (2008) J. Mol. Biol. , vol.376 , pp. 963-70
    • Inoue, K.1    Sasaki, J.2    Spudich, J.L.3    Terazima, M.4
  • 36
    • 0028061352 scopus 로고
    • Transmembrane signaling Mutational analysis of the cytoplasmic linker region of Taz1-1, a Tar-EnvZ chimeric receptor in Escherichia coli
    • Jin T, Inouye M. 1994. Transmembrane signaling. Mutational analysis of the cytoplasmic linker region of Taz1-1, a Tar-EnvZ chimeric receptor in Escherichia coli. J. Mol. Biol. 244:477-81
    • (1994) J. Mol. Biol. , vol.244 , pp. 477-81
    • Jin, T.1    Inouye, M.2
  • 37
    • 0020770030 scopus 로고
    • Enzymatic deamidation of methyl-accepting chemotaxis proteins in Escherichia coli catalyzed by the cheB gene product
    • Kehry MR, Bond MW, Hunkapiller MW, Dahlquist FW. 1983. Enzymatic deamidation of methyl-accepting chemotaxis proteins in Escherichia coli catalyzed by the cheB gene product. Proc. Natl. Acad. Sci. USA 80:3599-603
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 3599-603
    • Kehry, M.R.1    Bond, M.W.2    Hunkapiller, M.W.3    Dahlquist, F.W.4
  • 38
    • 34548819024 scopus 로고    scopus 로고
    • Structural and functional studies of the HAMP domain of EnvZ, an osmosensing transmembrane histidine kinase in Escherichia coli
    • Kishii R, Falzon L, Yoshida T, Kobayashi H, Inouye M. 2007. Structural and functional studies of the HAMP domain of EnvZ, an osmosensing transmembrane histidine kinase in Escherichia coli. J. Biol. Chem. 282:26401-8
    • (2007) J. Biol. Chem. , vol.282 , pp. 26401-8
    • Kishii, R.1    Falzon, L.2    Yoshida, T.3    Kobayashi, H.4    Inouye, M.5
  • 39
    • 0030271515 scopus 로고    scopus 로고
    • Coiled coils: New structures and new functions
    • Lupas A. 1996. Coiled coils: new structures and new functions. Trends Biochem. Sci. 21:375-82
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 375-82
    • Lupas, A.1
  • 40
    • 1242352964 scopus 로고    scopus 로고
    • Side chains at the membrane-water interface modulate the signaling state of a transmembrane receptor
    • Miller AS, Falke JJ. 2004. Side chains at the membrane-water interface modulate the signaling state of a transmembrane receptor. Biochemistry 43:1763-70
    • (2004) Biochemistry , vol.43 , pp. 1763-70
    • Miller, A.S.1    Falke, J.J.2
  • 41
    • 0030811371 scopus 로고    scopus 로고
    • Mutational analysis of the linker region of EnvZ, an osmosensor in Escherichia coli
    • Park H, Inouye M. 1997. Mutational analysis of the linker region of EnvZ, an osmosensor in Escherichia coli. J. Bacteriol. 179:4382-90
    • (1997) J. Bacteriol. , vol.179 , pp. 4382-90
    • Park, H.1    Inouye, M.2
  • 42
    • 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 MS, Harding GP, Zuccarelli AJ, Fletcher HM, et al. 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 94:10541-46
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10541-46
    • Rebbapragada, A.1    Johnson, M.S.2    Harding, G.P.3    Zuccarelli, A.J.4    Fletcher, H.M.5
  • 44
    • 0025883204 scopus 로고
    • Sites of deamidation and methylation inTsr,a bacterial chemotaxis sensory transducer
    • Rice MS, Dahlquist FW. 1991. Sites of deamidation and methylation inTsr,a bacterial chemotaxis sensory transducer. J. Biol. Chem. 266:9746-53
    • (1991) J. Biol. Chem. , vol.266 , pp. 9746-53
    • Rice, M.S.1    Dahlquist, F.W.2
  • 45
    • 49749116145 scopus 로고    scopus 로고
    • Signal transfer in haloarchaeal sensory rhodopsin-transducer complexes
    • Sasaki J, Spudich JL. 2008. Signal transfer in haloarchaeal sensory rhodopsin-transducer complexes. Pho-tochem. Photobiol. 84:863-68
    • (2008) Pho-tochem. Photobiol. , vol.84 , pp. 863-68
    • Sasaki, J.1    Spudich, J.L.2
  • 46
    • 13444301196 scopus 로고    scopus 로고
    • Adaptation mechanism of the aspartate receptor: Electrostatics of the adaptation subdomain play a key role in modulating kinase activity
    • Starrett DJ, Falke JJ. 2005. Adaptation mechanism of the aspartate receptor: electrostatics of the adaptation subdomain play a key role in modulating kinase activity. Biochemistry 44:1550-60
    • (2005) Biochemistry , vol.44 , pp. 1550-60
    • Starrett, D.J.1    Falke, J.J.2
  • 47
    • 0037326468 scopus 로고    scopus 로고
    • Biochemical Society Special Lecture. Nitrate-and nitrite-responsive sensors NarX and NarQ of proteobacteria
    • Stewart V. 2003. Biochemical Society Special Lecture. Nitrate-and nitrite-responsive sensors NarX and NarQ of proteobacteria. Biochem. Soc. Trans. 31:1-10
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 1-10
    • Stewart, V.1
  • 48
    • 75149162101 scopus 로고    scopus 로고
    • The S-helix mediates signal transmission as a HAMP domain coiled-coil extension in the NarX nitrate sensor from Escherichia coli K-12
    • Stewart V, Chen LL. 2010. The S-helix mediates signal transmission as a HAMP domain coiled-coil extension in the NarX nitrate sensor from Escherichia coli K-12. J. Bacteriol. 192:734-45
    • (2010) J. Bacteriol. , vol.192 , pp. 734-45
    • Stewart, V.1    Chen, L.L.2
  • 49
    • 36848998769 scopus 로고    scopus 로고
    • Structure of the conserved HAMP domain in an intact, membrane-bound chemoreceptor: A disulfide mapping study
    • Swain KE, Falke JJ. 2007. Structure of the conserved HAMP domain in an intact, membrane-bound chemoreceptor: a disulfide mapping study. Biochemistry 46:13684-95
    • (2007) Biochemistry , vol.46 , pp. 13684-95
    • Swain, K.E.1    Falke, J.J.2
  • 50
    • 70349611544 scopus 로고    scopus 로고
    • Engineered socket study of signaling through a four-helix bundle: Evidence for a yin-yang mechanism in the kinase control module of the aspartate receptor
    • Swain KE, Gonzalez MA, Falke JJ. 2009. Engineered socket study of signaling through a four-helix bundle: evidence for a yin-yang mechanism in the kinase control module of the aspartate receptor. Biochemistry 48:9266-77
    • (2009) Biochemistry , vol.48 , pp. 9266-77
    • Swain, K.E.1    Ma, G.2    Falke, J.J.3
  • 51
    • 36549003158 scopus 로고    scopus 로고
    • Sensor complexes regulating two-component signal transduction
    • Szurmant H, White RA, Hoch JA. 2007. Sensor complexes regulating two-component signal transduction. Curr. Opin. Struct. Biol. 17:706-15
    • (2007) Curr. Opin. Struct. Biol. , vol.17 , pp. 706-15
    • Szurmant, H.1    White, R.A.2    Hoch, J.A.3
  • 52
    • 34548356914 scopus 로고    scopus 로고
    • Aer on the inside looking out: Paradigm for a PAS-HAMP role in sensing oxygen, redox and energy
    • Taylor BL. 2007. Aer on the inside looking out: paradigm for a PAS-HAMP role in sensing oxygen, redox and energy. Mol. Microbiol. 65:1415-24
    • (2007) Mol. Microbiol. , vol.65 , pp. 1415-24
    • Taylor, B.L.1
  • 53
    • 0024462539 scopus 로고
    • Activation of bacterial porin gene expression by a chimeric signal transducer in response to aspartate
    • Utsumi R, Brissette RE, Rampersaud A, Forst SA, Oosawa K, Inouye M. 1989. Activation of bacterial porin gene expression by a chimeric signal transducer in response to aspartate. Science 245:1246-49
    • (1989) Science , vol.245 , pp. 1246-49
    • Utsumi, R.1    Brissette, R.E.2    Rampersaud, A.3    Forst, S.A.4    Oosawa, K.5    Inouye, M.6
  • 54
    • 33744718485 scopus 로고    scopus 로고
    • Mutationally altered signal output in the Nart (NarX-Tar) hybrid chemoreceptor
    • Ward SM, Bormans AF, Manson MD. 2006. Mutationally altered signal output in the Nart (NarX-Tar) hybrid chemoreceptor. J. Bacteriol. 188:3944-51
    • (2006) J. Bacteriol. , vol.188 , pp. 3944-51
    • Ward, S.M.1    Bormans, A.F.2    Manson, M.D.3
  • 55
    • 0036091152 scopus 로고    scopus 로고
    • A NarX-Tar chimera mediates repellent chemo-taxis to nitrate and nitrite
    • Ward SM, Delgado A, Gunsalus RP, Manson MD. 2002. A NarX-Tar chimera mediates repellent chemo-taxis to nitrate and nitrite. Mol. Microbiol. 44:709-19
    • (2002) Mol. Microbiol. , vol.44 , pp. 709-19
    • Ward, S.M.1    Delgado, A.2    Gunsalus, R.P.3    Manson, M.D.4
  • 56
    • 40449120005 scopus 로고    scopus 로고
    • Structure-function relationships in the HAMP and proximal signaling domains of the aerotaxis receptor Aer
    • Watts KJ, Johnson MS, Taylor BL. 2008. Structure-function relationships in the HAMP and proximal signaling domains of the aerotaxis receptor Aer. J. Bacteriol. 190:2118-27
    • (2008) J. Bacteriol. , vol.190 , pp. 2118-27
    • 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 KJ, Ma Q, Johnson MS, Taylor BL. 2004. Interactions between the PAS and HAMP domains of the Escherichia coli aerotaxis receptor Aer. J. Bacteriol. 186:7440-49
    • (2004) J. Bacteriol. , vol.186 , pp. 7440-49
    • Watts, K.J.1    Ma, Q.2    Johnson, M.S.3    Taylor, B.L.4
  • 58
    • 0035477798 scopus 로고    scopus 로고
    • Structural insights into the early steps of receptor-transducer signal transfer in archaeal phototaxis
    • Wegener AA, Klare JP, Engelhard M, Steinhoff HJ. 2001. Structural insights into the early steps of receptor-transducer signal transfer in archaeal phototaxis. EMBO J. 20:5312-19
    • (2001) EMBO J. , vol.20 , pp. 5312-19
    • Wegener, A.A.1    Klare, J.P.2    Engelhard, M.3    Steinhoff, H.J.4
  • 59
    • 0032826834 scopus 로고    scopus 로고
    • Functional similarities among two-component sensors and methyl-accepting chemotaxis proteins suggest a role for linker region amphipathic helices in transmem-brane signal transduction
    • Williams SB, Stewart V. 1999. Functional similarities among two-component sensors and methyl-accepting chemotaxis proteins suggest a role for linker region amphipathic helices in transmem-brane signal transduction. Mol. Microbiol. 33:1093-102
    • (1999) Mol. Microbiol. , vol.33 , pp. 1093-102
    • Williams, S.B.1    Stewart, V.2
  • 60
    • 25444437722 scopus 로고    scopus 로고
    • Evidence that the adaptation region of the aspartate receptor is a dynamic four-helix bundle: Cysteine and disulfide scanning studies
    • Winston SE, Mehan R, Falke JJ. 2005. Evidence that the adaptation region of the aspartate receptor is a dynamic four-helix bundle: cysteine and disulfide scanning studies. Biochemistry 44:12655-66
    • (2005) Biochemistry , vol.44 , pp. 12655-66
    • Winston, S.E.1    Mehan, R.2    Falke, J.J.3
  • 61
    • 0027295668 scopus 로고
    • Ligand binding induces an asymmetrical transmembrane signal through a receptor dimer
    • Yang Y, Park H, Inouye M. 1993. Ligand binding induces an asymmetrical transmembrane signal through a receptor dimer. J. Mol. Biol. 232:493-98
    • (1993) J. Mol. Biol. , vol.232 , pp. 493-98
    • Yang, Y.1    Park, H.2    Inouye, M.3
  • 62
    • 0033514438 scopus 로고    scopus 로고
    • The specificity of interaction of archaeal transducers with their cognate sensory rhodopsins is determined by their transmembrane helices
    • Zhang XN, Zhu J, Spudich JL. 1999. The specificity of interaction of archaeal transducers with their cognate sensory rhodopsins is determined by their transmembrane helices. Proc. Natl. Acad. Sci. USA 96:857-62
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 857-62
    • Zhang, X.N.1    Zhu, J.2    Spudich, J.L.3
  • 63
    • 70350163201 scopus 로고    scopus 로고
    • Mutational analyses of HAMP helices suggest a dynamic bundle model of input-output signaling in chemoreceptors
    • Zhou Q, Ames P, Parkinson JS. 2009. Mutational analyses of HAMP helices suggest a dynamic bundle model of input-output signaling in chemoreceptors. Mol. Microbiol. 73:801-14
    • (2009) Mol. Microbiol. , vol.73 , pp. 801-14
    • Zhou, Q.1    Ames, P.2    Parkinson, J.S.3
  • 64
    • 0037589946 scopus 로고    scopus 로고
    • Analysis of the role of the EnvZ linker region in signal transduction using a chimeric Tar/EnvZ receptor protein, Tez1
    • Zhu Y, Inouye M. 2003. Analysis of the role of the EnvZ linker region in signal transduction using a chimeric Tar/EnvZ receptor protein, Tez1. J. Biol. Chem. 278:22812-19
    • (2003) J. Biol. Chem. , vol.278 , pp. 22812-19
    • Zhu, Y.1    Inouye, M.2
  • 65
    • 9144234840 scopus 로고    scopus 로고
    • The HAMP linker in histidine kinase dimeric receptors is critical for symmetric transmembrane signal transduction
    • Zhu Y, Inouye M. 2004. The HAMP linker in histidine kinase dimeric receptors is critical for symmetric transmembrane signal transduction. J. Biol. Chem. 279:48152-58
    • (2004) J. Biol. Chem. , vol.279 , pp. 48152-58
    • Zhu, Y.1    Inouye, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.