메뉴 건너뛰기




Volumn 44, Issue 16, 2005, Pages 6144-6152

Linker region of a halobacterial transducer protein interacts directly with its sensor retinal protein

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; DISSOCIATION; MEMBRANES; PH EFFECTS; SENSORS; TITRATION;

EID: 17644401016     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi047573z     Document Type: Article
Times cited : (31)

References (41)
  • 1
    • 14344254083 scopus 로고    scopus 로고
    • Molecular mechanism of protein-protein interaction of pharaonis phoborhodopsin/transducer and photosignal transfer reaction by the complex
    • Sudo, Y., Kandori, H., and Kamo, N. (2004) Molecular mechanism of protein-protein interaction of pharaonis phoborhodopsin/transducer and photosignal transfer reaction by the complex, Recent Res. Dev. Biophys. 3, 1-16.
    • (2004) Recent Res. Dev. Biophys. , vol.3 , pp. 1-16
    • Sudo, Y.1    Kandori, H.2    Kamo, N.3
  • 3
    • 0031455398 scopus 로고    scopus 로고
    • The two-component signaling pathway of bacterial chemotaxis: A molecular view of signal transduction by receptors, kinases, and adaptation enzymes
    • Falke, J. J., Bass, R. B., Butler, S. L., Chervitz, S. A., and Danielson, M. A. (1997) The two-component signaling pathway of bacterial chemotaxis: A molecular view of signal transduction by receptors, kinases, and adaptation enzymes, Annu. Rev. Cell Dev. Biol. 13, 457-512.
    • (1997) Annu. Rev. Cell Dev. Biol. , vol.13 , pp. 457-512
    • Falke, J.J.1    Bass, R.B.2    Butler, S.L.3    Chervitz, S.A.4    Danielson, M.A.5
  • 4
    • 0030906654 scopus 로고    scopus 로고
    • Molecular mechanism of photosignaling by archaeal sensory rhodopsins
    • Hoff, W. D., Jung, K. H., and Spudich, J. L. (1997) Molecular mechanism of photosignaling by archaeal sensory rhodopsins, Annu. Rev. Biophys. Biomol. Struct. 26, 223-258.
    • (1997) Annu. Rev. Biophys. Biomol. Struct. , vol.26 , pp. 223-258
    • Hoff, W.D.1    Jung, K.H.2    Spudich, J.L.3
  • 5
    • 0035312774 scopus 로고    scopus 로고
    • Transmembrane signaling in bacterial chemoreceptors
    • Falke, J. J., and Hazelbauer, G. L. (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
  • 6
    • 0033514438 scopus 로고    scopus 로고
    • The specificity of interaction of archaeal transducers with their cognate sensory rhodopsins is determined by their transmembrane helices
    • Zhang, X. N., Zhu, J., and Spudich, J. L. (1999) The specificity of interaction of archaeal transducers with their cognate sensory rhodopsins is determined by their transmembrane helices, Proc. Natl. Acad. Sci. U.S.A. 96, 857-862.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 857-862
    • Zhang, X.N.1    Zhu, J.2    Spudich, J.L.3
  • 7
    • 0026331216 scopus 로고
    • Identification of signaling states of a sensory receptor by modulation of lifetimes of stimulus-induced conformations: The case of sensory rhodopsin II
    • Yan, B., Takahashi, T., Johnson, R., and Spudich, J. L. (1991) Identification of signaling states of a sensory receptor by modulation of lifetimes of stimulus-induced conformations: The case of sensory rhodopsin II, Biochemistry 30, 10686-10692.
    • (1991) Biochemistry , vol.30 , pp. 10686-10692
    • Yan, B.1    Takahashi, T.2    Johnson, R.3    Spudich, J.L.4
  • 8
    • 1542645230 scopus 로고    scopus 로고
    • Photochemical properties of pharaonis phoborhodopsin (sensory rhodopsin II)
    • Iwamoto, M., Kandori, H., and Kamo N. (2003) Photochemical properties of pharaonis phoborhodopsin (sensory rhodopsin II), Recent Res. Devel. Chem. 1, 15-30.
    • (2003) Recent Res. Devel. Chem. , vol.1 , pp. 15-30
    • Iwamoto, M.1    Kandori, H.2    Kamo, N.3
  • 9
    • 0037285444 scopus 로고    scopus 로고
    • Rhodopsin structure, dynamics, and activation: A perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide cross-linking
    • Hubbell, W. L., Altenbach, C., Hubbell, C. M., and Khorana, H. G. (2003) Rhodopsin structure, dynamics, and activation: A perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide cross-linking, Adv. Protein Chem. 243-290.
    • (2003) Adv. Protein Chem. , pp. 243-290
    • Hubbell, W.L.1    Altenbach, C.2    Hubbell, C.M.3    Khorana, H.G.4
  • 11
    • 0033529279 scopus 로고    scopus 로고
    • The nop-1 gene of neurospora crassa encodes a seven transmembrane helix retinal-binding protein homologous to archaeal rhodopsins
    • Bieszke, J. A., Braun, E. L., Bean, L. E., Kang, S., Natvig, D. O., and Borkovich, K. A. (1999) The nop-1 gene of neurospora crassa encodes a seven transmembrane helix retinal-binding protein homologous to archaeal rhodopsins, Proc. Natl. Acad. Sci. U.S.A. 96, 8034-8039.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 8034-8039
    • Bieszke, J.A.1    Braun, E.L.2    Bean, L.E.3    Kang, S.4    Natvig, D.O.5    Borkovich, K.A.6
  • 13
    • 0242365582 scopus 로고    scopus 로고
    • Arg-72 of pharaonis phoborhodopsin (sensory rhodopsin II) is important for the maintenance of the protein structure in the solubilized state
    • Ikeura, Y., Shimono, K., Iwamoto, M., Sudo, Y., and Kamo, N. (2003) Arg-72 of pharaonis phoborhodopsin (sensory rhodopsin II) is important for the maintenance of the protein structure in the solubilized state, Photochem. Photobiol. 77, 96-100.
    • (2003) Photochem. Photobiol. , vol.77 , pp. 96-100
    • Ikeura, Y.1    Shimono, K.2    Iwamoto, M.3    Sudo, Y.4    Kamo, N.5
  • 14
    • 0344413602 scopus 로고    scopus 로고
    • Interaction of Natronobacterium pharaonis phoborhodopsin (sensory rhodopsin II) with its cognate transducer probed by increase in the thermal stability
    • Sudo, Y., Yamabi, M., Iwamoto, M., Shimono, K., and Kamo, N. (2003) Interaction of Natronobacterium pharaonis phoborhodopsin (sensory rhodopsin II) with its cognate transducer probed by increase in the thermal stability, Photochem. Photobiol. 78, 511-516.
    • (2003) Photochem. Photobiol. , vol.78 , pp. 511-516
    • Sudo, Y.1    Yamabi, M.2    Iwamoto, M.3    Shimono, K.4    Kamo, N.5
  • 15
    • 0031583910 scopus 로고    scopus 로고
    • Functional expression of pharaonis phoborhodopsin in Escherichia coli
    • Shimono, K., Iwamoto, M., Sumi, M., and Kamo, N. (1997) Functional expression of pharaonis phoborhodopsin in Escherichia coli, FEBS Lett. 420, 54-56.
    • (1997) FEBS Lett. , vol.420 , pp. 54-56
    • Shimono, K.1    Iwamoto, M.2    Sumi, M.3    Kamo, N.4
  • 16
    • 0036829632 scopus 로고    scopus 로고
    • Spotlight on receptor/transducer interaction
    • Spudich, J. L. (2002) Spotlight on receptor/transducer interaction, Nat. Struct. Biol. 9, 797-799.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 797-799
    • Spudich, J.L.1
  • 17
    • 1942436349 scopus 로고    scopus 로고
    • The archaeal sensory rhodopsin II/transducer complex: A model for transmembrane signal transfer
    • Klare, J. P., Gordeliy, V. I., Labahn, J., Büldt, G., Steinhoff, H. J., and Engelhard, M. (2004) The archaeal sensory rhodopsin II/transducer complex: A model for transmembrane signal transfer, FEBS Lett. 564, 219-224.
    • (2004) FEBS Lett. , vol.564 , pp. 219-224
    • Klare, J.P.1    Gordeliy, V.I.2    Labahn, J.3    Büldt, G.4    Steinhoff, H.J.5    Engelhard, M.6
  • 18
    • 0035470682 scopus 로고    scopus 로고
    • pharaonis phoborhodopsin binds to its cognate truncated transducer even in the presence of a detergent with a 1:1 stoichiometry
    • Sudo, Y., Iwamoto, M., Shimono, K., and Kamo, N. (2001) pharaonis phoborhodopsin binds to its cognate truncated transducer even in the presence of a detergent with a 1:1 stoichiometry, Photochem. Photobiol. 74, 489-494.
    • (2001) Photochem. Photobiol. , vol.74 , pp. 489-494
    • Sudo, Y.1    Iwamoto, M.2    Shimono, K.3    Kamo, N.4
  • 19
    • 0036283968 scopus 로고    scopus 로고
    • Tyr-199 and charged residues of pharaonis phoborhodopsin are important for the interaction with its transducer
    • Sudo, Y., Iwamoto, M., Shimono, K., and Kamo, N. (2002) Tyr-199 and charged residues of pharaonis phoborhodopsin are important for the interaction with its transducer, Biophys. J. 83, 427-432.
    • (2002) Biophys. J. , vol.83 , pp. 427-432
    • Sudo, Y.1    Iwamoto, M.2    Shimono, K.3    Kamo, N.4
  • 20
    • 7244224726 scopus 로고    scopus 로고
    • Role of charged residues of pharaonis phoborhodopsin (seonsory rhodopsin II) in its interaction with the transducer protein
    • Sudo, Y., Iwamoto, M., Shimono, K., and Kamo, N. (2004). Role of charged residues of pharaonis phoborhodopsin (seonsory rhodopsin II) in its interaction with the transducer protein, Biochemistry 43, 13748-13754.
    • (2004) Biochemistry , vol.43 , pp. 13748-13754
    • Sudo, Y.1    Iwamoto, M.2    Shimono, K.3    Kamo, N.4
  • 23
    • 0001690764 scopus 로고    scopus 로고
    • Four-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor
    • Kim, K. K., Yokota, H., and Kim, S. H. (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
  • 24
    • 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 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
  • 25
    • 0029900082 scopus 로고    scopus 로고
    • Protonatable residues at the cytoplasmic end of transmembrane helix-2 in the signal transducer HtrI control photochemistry and function of sensory rhodopsin I
    • Jung, K. H., and Spudich, J. L. (1996) Protonatable residues at the cytoplasmic end of transmembrane helix-2 in the signal transducer HtrI control photochemistry and function of sensory rhodopsin I, Proc. Natl. Acad. Sci. U.S.A. 93, 6557-6561.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 6557-6561
    • Jung, K.H.1    Spudich, J.L.2
  • 26
    • 0037059759 scopus 로고    scopus 로고
    • Sensing of cytoplasmic pH by bacterial chemoreceptors involves the linker region that connects the membrane-spanning and the signal- modulating helices
    • Umemura, T., Matsumoto, Y., Ohnishi, K., Homma, M., and Kawagishi, I. (2002) Sensing of cytoplasmic pH by bacterial chemoreceptors involves the linker region that connects the membrane-spanning and the signal- modulating helices, J. Biol. Chem. 277, 1593-1598.
    • (2002) J. Biol. Chem. , vol.277 , pp. 1593-1598
    • Umemura, T.1    Matsumoto, Y.2    Ohnishi, K.3    Homma, M.4    Kawagishi, I.5
  • 27
    • 5644247396 scopus 로고    scopus 로고
    • The cytoplasmic membrane-proximal domain of the HtrII transducer interacts with E-F loop of photoactivated Nactronomonas pharaonis sensory rhodopsin II
    • Yang, C. S., Sineshchekov, O., Spudich, E. N., and Spudich, J. L. (2004) The cytoplasmic membrane-proximal domain of the HtrII transducer interacts with E-F loop of photoactivated Nactronomonas pharaonis sensory rhodopsin II, J. Biol. Chem. 279, 42964-42969
    • (2004) J. Biol. Chem. , vol.279 , pp. 42964-42969
    • Yang, C.S.1    Sineshchekov, O.2    Spudich, E.N.3    Spudich, J.L.4
  • 28
    • 0345492028 scopus 로고    scopus 로고
    • Hydrogen bonding alteration of Thr-204 in the complex between pharaonis phoborhodopsin and its transducer protein
    • Sudo, Y., Furutani, Y., Shimono, K., Kamo, N., and Kandori, H. (2003) Hydrogen bonding alteration of Thr-204 in the complex between pharaonis phoborhodopsin and its transducer protein, Biochemistry 42, 14166-14172.
    • (2003) Biochemistry , vol.42 , pp. 14166-14172
    • Sudo, Y.1    Furutani, Y.2    Shimono, K.3    Kamo, N.4    Kandori, H.5
  • 29
    • 0035822679 scopus 로고    scopus 로고
    • Structural changes of pharaonis phoborhodopsin upon photoisomerization of the retinal chromophore: Infrared spectral comparison with bacteriorhodopsin
    • Kandori, H., Shimono, K., Sudo, Y., Iwamoto, M., Shichida, Y., and Kamo, N. (2001) Structural changes of pharaonis phoborhodopsin upon photoisomerization of the retinal chromophore: Infrared spectral comparison with bacteriorhodopsin, Biochemistry 40, 9238-9246.
    • (2001) Biochemistry , vol.40 , pp. 9238-9246
    • Kandori, H.1    Shimono, K.2    Sudo, Y.3    Iwamoto, M.4    Shichida, Y.5    Kamo, N.6
  • 30
    • 0031820941 scopus 로고    scopus 로고
    • The photophobic receptor from Natronobacterium pharaonis: Temperature and pH dependencies of the photocycle of sensory rhodopsin II
    • Chizhov, I., Schmies, G., Seidel, R., Sydor, J. R., Luttenberg, B., and Engelhard, M. (1998) The photophobic receptor from Natronobacterium pharaonis: Temperature and pH dependencies of the photocycle of sensory rhodopsin II, Biophys. J. 75, 999-1009.
    • (1998) Biophys. J. , vol.75 , pp. 999-1009
    • Chizhov, I.1    Schmies, G.2    Seidel, R.3    Sydor, J.R.4    Luttenberg, B.5    Engelhard, M.6
  • 31
    • 0036651031 scopus 로고    scopus 로고
    • Association between a photointermediate of a M-lacking mutant D75N of pharaonis phoborhodopsin and its cognate transducer
    • Sudo, Y., Iwamoto, M., Shimono, K., and Kamo, N. (2002) Association between a photointermediate of a M-lacking mutant D75N of pharaonis phoborhodopsin and its cognate transducer, J. Photochem. Photobiol., B 67, 171-176.
    • (2002) J. Photochem. Photobiol., B , vol.67 , pp. 171-176
    • Sudo, Y.1    Iwamoto, M.2    Shimono, K.3    Kamo, N.4
  • 32
    • 0026482090 scopus 로고
    • Flash photolysis study on pharaonis phoborhodopsin from a haloalkaliphilic bacterium (Natronobacterium pharonis)
    • Miyazaki, M., Hirayama, J., Hayakawa, M., and Kamo, N. (1992) Flash photolysis study on pharaonis phoborhodopsin from a haloalkaliphilic bacterium (Natronobacterium pharonis), Biochim. Biophys. Acta 1140, 22-29.
    • (1992) Biochim. Biophys. Acta , vol.1140 , pp. 22-29
    • Miyazaki, M.1    Hirayama, J.2    Hayakawa, M.3    Kamo, N.4
  • 33
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: A multidimensional spectral processing system based on UNIX pipes, J Biomol. NMR 6, 277-293.
    • (1995) J Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 34
    • 0004757060 scopus 로고    scopus 로고
    • University of California, San Francisco, CA
    • Goddard, T. D., and Kneller, D. G. SPARKY 3, University of California, San Francisco, CA.
    • SPARKY , vol.3
    • Goddard, T.D.1    Kneller, D.G.2
  • 35
    • 0035960642 scopus 로고    scopus 로고
    • Light-induced structural changes occur in the transmembrane helices of the Natronobacterium pharaonis HtrII transducer
    • Yang, C. S., and Spudich, J. L. (2001) Light-induced structural changes occur in the transmembrane helices of the Natronobacterium pharaonis HtrII transducer, Biochemistry 40, 14207-14214.
    • (2001) Biochemistry , vol.40 , pp. 14207-14214
    • Yang, C.S.1    Spudich, J.L.2
  • 36
    • 0031451150 scopus 로고    scopus 로고
    • Cysteine and disulfide scanning reveals a regulatory α-helix in the cytoplasmic domain of the aspartate receptor
    • Danielson, M. A., Bass, R. B., and Falke, J. J. (1997) Cysteine and disulfide scanning reveals a regulatory α-helix in the cytoplasmic domain of the aspartate receptor, J. Biol. Chem. 272, 32878-32888.
    • (1997) J. Biol. Chem. , vol.272 , pp. 32878-32888
    • Danielson, M.A.1    Bass, R.B.2    Falke, J.J.3
  • 37
    • 0034714097 scopus 로고    scopus 로고
    • Time-resolved detection of transient movement of helix F in spin-labeled pharaonis sensory rhodopsin II
    • Wegener, A. A., Chizhov, I., Engelhard, M., and Steinhoff, H. J. (2000) Time-resolved detection of transient movement of helix F in spin-labeled pharaonis sensory rhodopsin II, J. Mol. Biol. 301, 881-891.
    • (2000) J. Mol. Biol. , vol.301 , pp. 881-891
    • Wegener, A.A.1    Chizhov, I.2    Engelhard, M.3    Steinhoff, H.J.4
  • 38
    • 0034658269 scopus 로고    scopus 로고
    • Structure of the bacteriorhodopsin mutant F219L N intermediate revealed by electron crystallography
    • Vonck, J. (2000) Structure of the bacteriorhodopsin mutant F219L N intermediate revealed by electron crystallography, EMBO J. 19, 2152-2160.
    • (2000) EMBO J. , vol.19 , pp. 2152-2160
    • Vonck, J.1
  • 39
    • 0035016932 scopus 로고    scopus 로고
    • Time-resolved detection of transient movement of helices F and G in doubly spin-labeled bacteriorhodopsin
    • Radzwill, N., Gerwert, K., and Steinhoff, H. J. (2001) Time-resolved detection of transient movement of helices F and G in doubly spin-labeled bacteriorhodopsin, Biophys. J. 80, 2856-2866.
    • (2001) Biophys. J. , vol.80 , pp. 2856-2866
    • Radzwill, N.1    Gerwert, K.2    Steinhoff, H.J.3
  • 40
    • 0035477798 scopus 로고    scopus 로고
    • Structural insights into the early steps of receptor-transducer signal transfer in archaeal phototaxis
    • Wegener, A. A., Klare, J. P., Engelhard, M., and Steinhoff, H. J. (2001) Structural insights into the early steps of receptor-transducer signal transfer in archaeal phototaxis, EMBO J. 20, 5312-5319.
    • (2001) EMBO J. , vol.20 , pp. 5312-5319
    • Wegener, A.A.1    Klare, J.P.2    Engelhard, M.3    Steinhoff, H.J.4
  • 41
    • 0037763950 scopus 로고    scopus 로고
    • Electric-field dependent decays of two spectroscopically different M-states of photosensory rhodopsin II from Natronobacterium pharaonis
    • Rivas, L., Hippler-Mreyen, S., Engelhard, M., and Hildebrandt, P. (2003) Electric-field dependent decays of two spectroscopically different M-states of photosensory rhodopsin II from Natronobacterium pharaonis, Biophys. J. 84, 3864-3873.
    • (2003) Biophys. J. , vol.84 , pp. 3864-3873
    • Rivas, L.1    Hippler-Mreyen, S.2    Engelhard, M.3    Hildebrandt, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.