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Volumn 67, Issue 5, 2011, Pages 827-839

Structure and binding specificity of the receiver domain of sensor histidine kinase CKI1 from Arabidopsis thaliana

Author keywords

Arabidopsis thaliana; CKI1; crystal structure; multistep phosphorelay; NMR spectroscopy; receiver domain

Indexed keywords

ACTIVE SITE; ARABIDOPSIS; ARABIDOPSIS THALIANA; BINDING SPECIFICITIES; CKI1; HISTIDINE KINASE; MOLECULAR MECHANISM; MULTI-STEP; NUCLEAR RESPONSE; PHOSPHO-TRANSFER; PROTEIN INTERACTION; TWO-COMPONENT;

EID: 80052264757     PISSN: 09607412     EISSN: 1365313X     Source Type: Journal    
DOI: 10.1111/j.1365-313X.2011.04637.x     Document Type: Article
Times cited : (44)

References (63)
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M., (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 57749182194 scopus 로고    scopus 로고
    • The HupR receiver domain crystal structure in its nonphospho and inhibitory phospho states
    • Davies, K.M., Lowe, E.D., Venien-Bryan, C., and, Johnson, L.N., (2009) The HupR receiver domain crystal structure in its nonphospho and inhibitory phospho states. J. Mol. Biol. 385, 51-64.
    • (2009) J. Mol. Biol. , vol.385 , pp. 51-64
    • Davies, K.M.1    Lowe, E.D.2    Venien-Bryan, C.3    Johnson, L.N.4
  • 7
    • 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
  • 8
    • 77953214257 scopus 로고    scopus 로고
    • Arabidopsis histidine kinase CKI1 acts upstream of histidine phosphotransfer proteins to regulate female gametophyte development and vegetative growth
    • Deng, Y., Dong, H., Mu, J., Ren, B., Zheng, B., Ji, Z., Yang, W.C., Liang, Y., and, Zuo, J., (2010) Arabidopsis histidine kinase CKI1 acts upstream of histidine phosphotransfer proteins to regulate female gametophyte development and vegetative growth. Plant Cell, 22, 1232-1248.
    • (2010) Plant Cell , vol.22 , pp. 1232-1248
    • Deng, Y.1    Dong, H.2    Mu, J.3    Ren, B.4    Zheng, B.5    Ji, Z.6    Yang, W.C.7    Liang, Y.8    Zuo, J.9
  • 9
    • 47749097140 scopus 로고    scopus 로고
    • The histidine kinase AHK5 integrates endogenous and environmental signals in Arabidopsis guard cells
    • Desikan, R., Horak, J., Chaban, C., et al. (2008) The histidine kinase AHK5 integrates endogenous and environmental signals in Arabidopsis guard cells. PLoS ONE, 3, e2491.
    • (2008) PLoS ONE , vol.3
    • Desikan, R.1    Horak, J.2    Chaban, C.3
  • 10
    • 33749385188 scopus 로고    scopus 로고
    • Analysis of protein interactions within the cytokinin-signaling pathway of Arabidopsis thaliana
    • DOI 10.1111/j.1742-4658.2006.05467.x
    • Dortay, H., Mehnert, N., Burkle, L., Schmulling, T., and, Heyl, A., (2006) Analysis of protein interactions within the cytokinin-signaling pathway of Arabidopsis thaliana. FEBS J. 273, 4631-4644. (Pubitemid 44506906)
    • (2006) FEBS Journal , vol.273 , Issue.20 , pp. 4631-4644
    • Dortay, H.1    Mehnert, N.2    Burkle, L.3    Schmulling, T.4    Heyl, A.5
  • 11
    • 55249110221 scopus 로고    scopus 로고
    • Toward an interaction map of the two-component signaling pathway of Arabidopsis thaliana
    • Dortay, H., Gruhn, N., Pfeifer, A., Schwerdtner, M., Schmulling, T., and, Heyl, A., (2008) Toward an interaction map of the two-component signaling pathway of Arabidopsis thaliana. J. Proteome Res. 7, 3649-3660.
    • (2008) J. Proteome Res. , vol.7 , pp. 3649-3660
    • Dortay, H.1    Gruhn, N.2    Pfeifer, A.3    Schwerdtner, M.4    Schmulling, T.5    Heyl, A.6
  • 13
    • 70349541000 scopus 로고    scopus 로고
    • Biological insights from structures of two-component proteins
    • Gao, R., and, Stock, A.M., (2009) Biological insights from structures of two-component proteins. Annu. Rev. Microbiol. 63, 133-154.
    • (2009) Annu. Rev. Microbiol. , vol.63 , pp. 133-154
    • Gao, R.1    Stock, A.M.2
  • 14
    • 80052265133 scopus 로고    scopus 로고
    • San Francisco, USA: University of California
    • Goddard, T.D., and, Kneller, D.G., (2006) SPARKY 3.115. San Francisco, USA: University of California.
    • (2006) SPARKY 3.115
    • Goddard, T.D.1    Kneller, D.G.2
  • 15
    • 33646767505 scopus 로고    scopus 로고
    • Crystal structures of beryllium fluoride-free and beryllium fluoride-bound CheY in complex with the conserved C-terminal peptide of CheZ reveal dual binding modes specific to CheY conformation
    • DOI 10.1016/j.jmb.2006.03.050, PII S0022283606004001
    • Guhaniyogi, J., Robinson, V.L., and, Stock, A.M., (2006) Crystal structures of beryllium fluoride-free and beryllium fluoride-bound CheY in complex with the conserved C-terminal peptide of CheZ reveal dual binding modes specific to CheY conformation. J. Mol. Biol. 359, 624-645. (Pubitemid 43767261)
    • (2006) Journal of Molecular Biology , vol.359 , Issue.3 , pp. 624-645
    • Guhaniyogi, J.1    Robinson, V.L.2    Stock, A.M.3
  • 17
    • 17144434817 scopus 로고    scopus 로고
    • The putative sensor histidine kinase CKI1 is involved in female gametophyte development in Arabidopsis
    • DOI 10.1007/s00438-003-0858-7
    • Hejatko, J., Pernisova, M., Eneva, T., Palme, K., and, Brzobohaty, B., (2003) The putative sensor histidine kinase CKI1 is involved in female gametophyte development in Arabidopsis. Mol. Genet. Genomics, 269, 443-453. (Pubitemid 36976152)
    • (2003) Molecular Genetics and Genomics , vol.269 , Issue.4 , pp. 443-453
    • Hejatko, J.1    Pernisova, M.2    Eneva, T.3    Palme, K.4    Brzobohaty, B.5
  • 18
    • 69949181547 scopus 로고    scopus 로고
    • The histidine kinases CYTOKININ-INDEPENDENT1 and ARABIDOPSIS HISTIDINE KINASE2 and 3 regulate vascular tissue development in Arabidopsis shoots
    • Hejatko, J., Ryu, H., Kim, G.T., et al. (2009) The histidine kinases CYTOKININ-INDEPENDENT1 and ARABIDOPSIS HISTIDINE KINASE2 and 3 regulate vascular tissue development in Arabidopsis shoots. Plant Cell, 21, 2008-2021.
    • (2009) Plant Cell , vol.21 , pp. 2008-2021
    • Hejatko, J.1    Ryu, H.2    Kim, G.T.3
  • 20
    • 47749148861 scopus 로고    scopus 로고
    • The Arabidopsis thaliana response regulator ARR22 is a putative AHP phospho-histidine phosphatase expressed in the chalaza of developing seeds
    • Horak, J., Grefen, C., Berendzen, K.W., Hahn, A., Stierhof, Y.D., Stadelhofer, B., Stahl, M., Koncz, C., and, Harter, K., (2008) The Arabidopsis thaliana response regulator ARR22 is a putative AHP phospho-histidine phosphatase expressed in the chalaza of developing seeds. BMC Plant Biol. 8, 77.
    • (2008) BMC Plant Biol. , vol.8 , pp. 77
    • Horak, J.1    Grefen, C.2    Berendzen, K.W.3    Hahn, A.4    Stierhof, Y.D.5    Stadelhofer, B.6    Stahl, M.7    Koncz, C.8    Harter, K.9
  • 22
    • 0035960031 scopus 로고    scopus 로고
    • Two-component circuitry in Arabidopsis cytokinin signal transduction
    • DOI 10.1038/35096500
    • Hwang, I., and, Sheen, J., (2001) Two-component circuitry in Arabidopsis cytokinin signal transduction. Nature, 413, 383-389. (Pubitemid 32928586)
    • (2001) Nature , vol.413 , Issue.6854 , pp. 383-389
    • Hwang, I.1    Sheen, J.2
  • 23
    • 33847179866 scopus 로고    scopus 로고
    • AHK5 histidine kinase regulates root elongation through an ETR1-dependent abscisic acid and ethylene signaling pathway in Arabidopsis thaliana
    • Iwama, A., Yamashino, T., Tanaka, Y., Sakakibara, H., Kakimoto, T., Sato, S., Kato, T., Tabata, S., Nagatani, A., and, Mizuno, T., (2007) AHK5 histidine kinase regulates root elongation through an ETR1-dependent abscisic acid and ethylene signaling pathway in Arabidopsis thaliana. Plant Cell Physiol. 48, 375-380.
    • (2007) Plant Cell Physiol. , vol.48 , pp. 375-380
    • Iwama, A.1    Yamashino, T.2    Tanaka, Y.3    Sakakibara, H.4    Kakimoto, T.5    Sato, S.6    Kato, T.7    Tabata, S.8    Nagatani, A.9    Mizuno, T.10
  • 25
    • 0030575903 scopus 로고    scopus 로고
    • CKI1, a histidine kinase homolog implicated in cytokinin signal transduction
    • DOI 10.1126/science.274.5289.982
    • Kakimoto, T., (1996) CKI1, a histidine kinase homolog implicated in cytokinin signal transduction. Science, 274, 982-985. (Pubitemid 26398420)
    • (1996) Science , vol.274 , Issue.5289 , pp. 982-985
    • Kakimoto, T.1
  • 26
    • 67449106493 scopus 로고    scopus 로고
    • Cloning, purification, crystallization and preliminary X-ray analysis of the receiver domain of the histidine kinase CKI1 from Arabidopsis thaliana
    • Klumpler, T., Pekarova, B., Marek, J., Borkovcova, P., Janda, L., and, Hejatko, J., (2009) Cloning, purification, crystallization and preliminary X-ray analysis of the receiver domain of the histidine kinase CKI1 from Arabidopsis thaliana. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 65, 478-481.
    • (2009) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. , vol.65 , pp. 478-481
    • Klumpler, T.1    Pekarova, B.2    Marek, J.3    Borkovcova, P.4    Janda, L.5    Hejatko, J.6
  • 28
    • 44449112421 scopus 로고    scopus 로고
    • Specificity in two-component signal transduction pathways
    • Laub, M.T., and, Goulian, M., (2007) Specificity in two-component signal transduction pathways. Annu. Rev. Genet. 41, 121-145.
    • (2007) Annu. Rev. Genet. , vol.41 , pp. 121-145
    • Laub, M.T.1    Goulian, M.2
  • 29
    • 0035844214 scopus 로고    scopus 로고
    • Crystal structure of activated CheY. Comparison with other activated receiver domains
    • Lee, S.Y., Cho, H.S., Pelton, J.G., Yan, D., Berry, E.A., and, Wemmer, D.E., (2001) Crystal structure of activated CheY. Comparison with other activated receiver domains. J. Biol. Chem. 276, 16425-16431.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16425-16431
    • Lee, S.Y.1    Cho, H.S.2    Pelton, J.G.3    Yan, D.4    Berry, E.A.5    Wemmer, D.E.6
  • 32
    • 29344438034 scopus 로고    scopus 로고
    • Two-component phosphorelay signal transduction systems in plants: From hormone responses to circadian rhythms
    • DOI 10.1271/bbb.69.2263
    • Mizuno, T., (2005) Two-component phosphorelay signal transduction systems in plants: from hormone responses to circadian rhythms. Biosci. Biotechnol. Biochem. 69, 2263-2276. (Pubitemid 43004353)
    • (2005) Bioscience, Biotechnology and Biochemistry , vol.69 , Issue.12 , pp. 2263-2276
    • Mizuno, T.1
  • 33
    • 0033003378 scopus 로고    scopus 로고
    • Microsecond time scale dynamics in the RXR DNA-binding domain from a combination of spin-echo and off-resonance rotating frame relaxation measurements
    • DOI 10.1023/A:1008354232281
    • Mulder, F.A.A., van Tilborg, P.J.A., Kaptein, R., and, Boelens, R., (1999) Microsecond time scale dynamics in the RXR DNA-binding domain from a combination of spin-echo and off-resonance rotating frame relaxation measurements. J. Biomol. NMR, 13, 275-288. (Pubitemid 29143534)
    • (1999) Journal of Biomolecular NMR , vol.13 , Issue.3 , pp. 275-288
    • Mulder, F.A.A.1    Van Tilborg, P.J.A.2    Kaptein, R.3    Boelens, R.4
  • 34
    • 0033573130 scopus 로고    scopus 로고
    • The structure of the signal receiver domain of the Arabidopsis thaliana ethylene receptor ETR1
    • DOI 10.1016/S0969-2126(00)88345-8
    • Muller-Dieckmann, H.J., Grantz, A.A., and, Kim, S.H., (1999) The structure of the signal receiver domain of the Arabidopsis thaliana ethylene receptor ETR1. Structure, 7, 1547-1556. (Pubitemid 30007240)
    • (1999) Structure , vol.7 , Issue.12 , pp. 1547-1556
    • Muller-Dieckmann, H.-J.1    Grantz, A.A.2    Kim, S.-H.3
  • 36
  • 37
    • 2942668572 scopus 로고    scopus 로고
    • Histidine kinase homologs that act as cytokinin receptors possess overlapping functions in the regulation of shoot and root growth in arabidopsis
    • DOI 10.1105/tpc.021477
    • Nishimura, C., Ohashi, Y., Sato, S., Kato, T., Tabata, S., and, Ueguchi, C., (2004) Histidine kinase homologs that act as cytokinin receptors possess overlapping functions in the regulation of shoot and root growth in Arabidopsis. Plant Cell, 16, 1365-1377. (Pubitemid 38774235)
    • (2004) Plant Cell , vol.16 , Issue.6 , pp. 1365-1377
    • Nishimura, C.1    Ohashi, Y.2    Sato, S.3    Kato, T.4    Tabata, S.5    Ueguchi, C.6
  • 38
    • 70149090337 scopus 로고    scopus 로고
    • Matching biochemical reaction kinetics to the timescales of life: Structural determinants that influence the autodephosphorylation rate of response regulator proteins
    • Pazy, Y., Wollish, A.C., Thomas, S.A., Miller, P.J., Collins, E.J., Bourret, R.B., and, Silversmith, R.E., (2009) Matching biochemical reaction kinetics to the timescales of life: structural determinants that influence the autodephosphorylation rate of response regulator proteins. J. Mol. Biol. 392, 1205-1220.
    • (2009) J. Mol. Biol. , vol.392 , pp. 1205-1220
    • Pazy, Y.1    Wollish, A.C.2    Thomas, S.A.3    Miller, P.J.4    Collins, E.J.5    Bourret, R.B.6    Silversmith, R.E.7
  • 41
    • 33645749116 scopus 로고    scopus 로고
    • Arabidopsis cytokinin receptors mutants reveal functions in shoot growth, leaf senescence, seed size, germination, root development, and cytokinin metabolism
    • DOI 10.1105/tpc.105.037796
    • Riefler, M., Novak, O., Strnad, M., and, Schmulling, T., (2006) Arabidopsis cytokinin receptor mutants reveal functions in shoot growth, leaf senescence, seed size, germination, root development, and cytokinin metabolism. Plant Cell, 18, 40-54. (Pubitemid 43951314)
    • (2006) Plant Cell , vol.18 , Issue.1 , pp. 40-54
    • Riefler, M.1    Novak, O.2    Strnad, M.3    Schmulling, T.4
  • 42
    • 33750336664 scopus 로고    scopus 로고
    • A New Structural Domain in the Escherichia coli RcsC Hybrid Sensor Kinase Connects Histidine Kinase and Phosphoreceiver Domains
    • DOI 10.1016/j.jmb.2006.07.052, PII S0022283606009302
    • Rogov, V.V., Rogova, N.Y., Bernhard, F., Koglin, A., Lohr, F., and, Dotsch, V., (2006) A new structural domain in the Escherichia coli RcsC hybrid sensor kinase connects histidine kinase and phosphoreceiver domains. J. Mol. Biol. 364, 68-79. (Pubitemid 44634525)
    • (2006) Journal of Molecular Biology , vol.364 , Issue.1 , pp. 68-79
    • Rogov, V.V.1    Rogova, N.Yu.2    Bernhard, F.3    Koglin, A.4    Lohr, F.5    Dotsch, V.6
  • 43
    • 0026761084 scopus 로고
    • A chemotactic signaling surface on CheY defined by suppressors of flagellar switch mutations
    • Roman, S.J., Meyers, M., Volz, K., and, Matsumura, P., (1992) A chemotactic signaling surface on CheY defined by suppressors of flagellar switch mutations. J. Bacteriol. 174, 6247-6255.
    • (1992) J. Bacteriol. , vol.174 , pp. 6247-6255
    • Roman, S.J.1    Meyers, M.2    Volz, K.3    Matsumura, P.4
  • 44
    • 0347722841 scopus 로고    scopus 로고
    • Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients
    • PII S0079656598000259
    • Sattler, M., Schleucher, J., and, Griesinger, C., (1999) Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients. Prog. Nucl. Magn. Reson. Spectrosc. 34, 93-158. (Pubitemid 129595216)
    • (1999) Progress in Nuclear Magnetic Resonance Spectroscopy , vol.34 , Issue.2 , pp. 93-158
    • Sattler, M.1    Schleucher, J.2    Griesinger, C.3
  • 45
    • 0029619085 scopus 로고
    • Ethylene-binding sites generated in yeast expressing the Arabidopsis ETR1 gene
    • Schaller, G.E., and, Bleecker, A.B., (1995) Ethylene-binding sites generated in yeast expressing the Arabidopsis ETR1 gene. Science, 270, 1809-1811. (Pubitemid 26007225)
    • (1995) Science , vol.270 , Issue.5243 , pp. 1809-1811
    • Schaller, G.E.1    Bleecker, A.B.2
  • 46
    • 42649087403 scopus 로고    scopus 로고
    • Ethylene signaling: Identification of a putative ETR1-AHP1 phosphorelay complex by fluorescence spectroscopy
    • Scharein, B., Voet-Van-Vormizeele, J., Harter, K., and, Groth, G., (2008) Ethylene signaling: identification of a putative ETR1-AHP1 phosphorelay complex by fluorescence spectroscopy. Anal. Biochem. 377, 72-76.
    • (2008) Anal. Biochem. , vol.377 , pp. 72-76
    • Scharein, B.1    Voet-Van-Vormizeele, J.2    Harter, K.3    Groth, G.4
  • 47
    • 0032578489 scopus 로고    scopus 로고
    • In vivo characterization of the type A and B vancomycin-resistant enterococci (VRE) VanRS two-component systems in Escherichia coli: A nonpathogenic model for studying the VRE signal transduction pathways
    • Silva, J.C., Haldimann, A., Prahalad, M.K., Walsh, C.T., and, Wanner, B.L., (1998) In vivo characterization of the type A and B vancomycin-resistant enterococci (VRE) VanRS two-component systems in Escherichia coli: a nonpathogenic model for studying the VRE signal transduction pathways. Proc. Natl Acad. Sci. USA, 95, 11951-11956.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 11951-11956
    • Silva, J.C.1    Haldimann, A.2    Prahalad, M.K.3    Walsh, C.T.4    Wanner, B.L.5
  • 48
    • 0024562159 scopus 로고
    • Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis
    • DOI 10.1038/337745a0
    • Stock, A.M., Mottonen, J.M., Stock, J.B., and, Schutt, C.E., (1989) 3-dimensional structure of Chey, the response regulator of bacterial chemotaxis. Nature, 337, 745-749. (Pubitemid 19064730)
    • (1989) Nature , vol.337 , Issue.6209 , pp. 745-749
    • Stock, A.M.1    Mottonen, J.M.2    Stock, J.B.3    Schutt, C.E.4
  • 49
    • 0027788051 scopus 로고
    • Structure of the Mg(2+)-bound form of CheY and mechanism of phosphoryl transfer in bacterial chemotaxis
    • Stock, A.M., Martinez-Hackert, E., Rasmussen, B.F., West, A.H., Stock, J.B., Ringe, D., and, Petsko, G.A., (1993) Structure of the Mg(2+)-bound form of CheY and mechanism of phosphoryl transfer in bacterial chemotaxis. Biochemistry, 32, 13375-13380.
    • (1993) Biochemistry , vol.32 , pp. 13375-13380
    • Stock, A.M.1    Martinez-Hackert, E.2    Rasmussen, B.F.3    West, A.H.4    Stock, J.B.5    Ringe, D.6    Petsko, G.A.7
  • 50
    • 39749178251 scopus 로고    scopus 로고
    • Cytokinin signaling: Two-components and more
    • To, J.P., and, Kieber, J.J., (2008) Cytokinin signaling: two-components and more. Trends Plant Sci. 13, 85-92.
    • (2008) Trends Plant Sci. , vol.13 , pp. 85-92
    • To, J.P.1    Kieber, J.J.2
  • 51
    • 38049138593 scopus 로고    scopus 로고
    • Functional analysis of AHK1/ATHK1 and cytokinin receptor histidine kinases in response to abscisic acid, drought, and salt stress in Arabidopsis
    • Tran, L.S., Urao, T., Qin, F., Maruyama, K., Kakimoto, T., Shinozaki, K., and, Yamaguchi-Shinozaki, K., (2007) Functional analysis of AHK1/ATHK1 and cytokinin receptor histidine kinases in response to abscisic acid, drought, and salt stress in Arabidopsis. Proc. Natl Acad. Sci. USA, 104, 20623-20628.
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 20623-20628
    • Tran, L.S.1    Urao, T.2    Qin, F.3    Maruyama, K.4    Kakimoto, T.5    Shinozaki, K.6    Yamaguchi-Shinozaki, K.7
  • 53
    • 0034604698 scopus 로고    scopus 로고
    • Possible His to Asp phosphorelay signaling in an Arabidopsis two- component system
    • DOI 10.1016/S0014-5793(00)01860-3, PII S0014579300018603
    • Urao, T., Miyata, S., Yamaguchi-Shinozaki, K., and, Shinozaki, K., (2000a) Possible His to Asp phosphorelay signaling in an Arabidopsis two-component system. FEBS Lett. 478, 227-232. (Pubitemid 30621622)
    • (2000) FEBS Letters , vol.478 , Issue.3 , pp. 227-232
    • Urao, T.1    Miyata, S.2    Yamaguchi-Shinozaki, K.3    Shinozaki, K.4
  • 58
    • 0035369115 scopus 로고    scopus 로고
    • Histidine kinases and response regulator proteins in two-component signaling systems
    • DOI 10.1016/S0968-0004(01)01852-7, PII S0968000401018527
    • West, A.H., and, Stock, A.M., (2001) Histidine kinases and response regulator proteins in two-component signaling systems. Trends Biochem. Sci. 26, 369-376. (Pubitemid 32530655)
    • (2001) Trends in Biochemical Sciences , vol.26 , Issue.6 , pp. 369-376
    • West, A.H.1    Stock, A.M.2
  • 60
    • 0344436666 scopus 로고    scopus 로고
    • The yeast YPD1/SLN1 complex: Insights into molecular recognition in two-component signaling systems
    • DOI 10.1016/j.str.2003.10.016
    • Xu, Q., Porter, S.W., and, West, A.H., (2003) The yeast YPD1/SLN1 complex: insights into molecular recognition in two-component signaling systems. Structure, 11, 1569-1581. (Pubitemid 37510356)
    • (2003) Structure , vol.11 , Issue.12 , pp. 1569-1581
    • Xu, Q.1    Porter, S.W.2    West, A.H.3
  • 61
    • 0034793963 scopus 로고    scopus 로고
    • The arabidopsis AHK4 histidine kinase is a cytokinin-binding receptor that transduces cytokinin signals across the membrane
    • Yamada, H., Suzuki, T., Terada, K., Takei, K., Ishikawa, K., Miwa, K., Yamashino, T., and, Mizuno, T., (2001) The Arabidopsis AHK4 histidine kinase is a cytokinin-binding receptor that transduces cytokinin signals across the membrane. Plant Cell Physiol. 42, 1017-1023. (Pubitemid 32972608)
    • (2001) Plant and Cell Physiology , vol.42 , Issue.9 , pp. 1017-1023
    • Yamada, H.1    Suzuki, T.2    Terada, K.3    Takei, K.4    Ishikawa, K.5    Miwa, K.6    Yamashino, T.7    Mizuno, T.8
  • 63
    • 37449018128 scopus 로고    scopus 로고
    • Crystal Structure of a Complex between the Phosphorelay Protein YPD1 and the Response Regulator Domain of SLN1 Bound to a Phosphoryl Analog
    • DOI 10.1016/j.jmb.2007.11.045, PII S0022283607015161
    • Zhao, X., Copeland, D.M., Soares, A.S., and, West, A.H., (2008) Crystal structure of a complex between the phosphorelay protein YPD1 and the response regulator domain of SLN1 bound to a phosphoryl analog. J. Mol. Biol. 375, 1141-1151. (Pubitemid 50012875)
    • (2008) Journal of Molecular Biology , vol.375 , Issue.4 , pp. 1141-1151
    • Zhao, X.1    Copeland, D.M.2    Soares, A.S.3    West, A.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.