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Volumn , Issue , 2002, Pages 483-506

Molecular Evolution of Histidine Kinases

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; FUNGI; MACHINERY; MOLECULAR BIOLOGY; SIGNAL TRANSDUCTION;

EID: 84902389170     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-012372484-7/50024-2     Document Type: Chapter
Times cited : (5)

References (48)
  • 1
    • 0030884102 scopus 로고    scopus 로고
    • PAS domain S-boxes in Archaea, Bacteria and sensors for oxygen and redox
    • Zhulin I.B., Taylor B.L., Dixon R. PAS domain S-boxes in Archaea, Bacteria and sensors for oxygen and redox. Trends Biochem. Sci. 1997, 22:331-333.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 331-333
    • Zhulin, I.B.1    Taylor, B.L.2    Dixon, R.3
  • 2
    • 0031262875 scopus 로고    scopus 로고
    • PAS: A multifunctional domain family comes to light
    • Ponting C.P., Aravind L. PAS: A multifunctional domain family comes to light. Curr. Biol. 1997, 7:R674-R677.
    • (1997) Curr. Biol. , vol.7
    • Ponting, C.P.1    Aravind, L.2
  • 3
    • 0030712081 scopus 로고    scopus 로고
    • The GAF domain: An evolutionary link between diverse phototransducing proteins
    • Aravind L., Ponting C.P. The GAF domain: An evolutionary link between diverse phototransducing proteins. Trends Biochem. Sci. 1997, 22:458-459.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 458-459
    • Aravind, L.1    Ponting, C.P.2
  • 4
    • 0034676026 scopus 로고    scopus 로고
    • Structure of the GAF domain, a ubiquitous signalling motif and a new class of cyclic GMP receptor
    • Ho Y.S., Burden L.M., Hurley J.H. Structure of the GAF domain, a ubiquitous signalling motif and a new class of cyclic GMP receptor. EMBO J. 2000, 19:5288-5299.
    • (2000) EMBO J. , vol.19 , pp. 5288-5299
    • Ho, Y.S.1    Burden, L.M.2    Hurley, J.H.3
  • 7
    • 0034326854 scopus 로고    scopus 로고
    • 2+-channel subunits and a class of prokaryotic chemotaxis receptors
    • 2+-channel subunits and a class of prokaryotic chemotaxis receptors. Trends Biochem Sci. 2000, 25:535-537.
    • (2000) Trends Biochem Sci. , vol.25 , pp. 535-537
    • Anantharaman, V.1    Aravind, L.2
  • 8
    • 0019463941 scopus 로고
    • Structure of catabolite gene activator protein at 2.9 A resolution suggests binding to left-handed B-DNA
    • McKay D.B., Steitz T.A. Structure of catabolite gene activator protein at 2.9 A resolution suggests binding to left-handed B-DNA. Nature (London) 1981, 290:744-749.
    • (1981) Nature (London) , vol.290 , pp. 744-749
    • McKay, D.B.1    Steitz, T.A.2
  • 9
    • 0033197541 scopus 로고    scopus 로고
    • The FHA domain is a modular phosphopeptide recognition motif
    • Durocher D., Henckel J., Fersht A.R., Jackson S.P. The FHA domain is a modular phosphopeptide recognition motif. Mol. Cell. 1999, 4:387-394.
    • (1999) Mol. Cell. , vol.4 , pp. 387-394
    • Durocher, D.1    Henckel, J.2    Fersht, A.R.3    Jackson, S.P.4
  • 10
    • 0024563996 scopus 로고
    • Periplasmic binding protein structure and function: Refined X-ray structures of the leucine/isoleucine/valine-binding protein and its complex with leucine
    • Sack J.S., Saper M.A., Quiocho F.A. Periplasmic binding protein structure and function: Refined X-ray structures of the leucine/isoleucine/valine-binding protein and its complex with leucine. J. Mol. Biol. 1989, 206:171-191.
    • (1989) J. Mol. Biol. , vol.206 , pp. 171-191
    • Sack, J.S.1    Saper, M.A.2    Quiocho, F.A.3
  • 11
    • 0031055372 scopus 로고    scopus 로고
    • Evidence for PDZ domains in bacteria, yeast, and plants
    • Ponting C.P. Evidence for PDZ domains in bacteria, yeast, and plants. Protein Sci. 1997, 6:464-468.
    • (1997) Protein Sci. , vol.6 , pp. 464-468
    • Ponting, C.P.1
  • 12
    • 0030811371 scopus 로고    scopus 로고
    • Mutational analysis of the linker region of EnvZ, an osmosensor in Escherichia coli
    • Park H., Inouye M. Mutational analysis of the linker region of EnvZ, an osmosensor in Escherichia coli. J. Bacteriol. 1997, 179:4382-4390.
    • (1997) J. Bacteriol. , vol.179 , pp. 4382-4390
    • Park, H.1    Inouye, M.2
  • 13
    • 0032826834 scopus 로고    scopus 로고
    • Functional similarities among two-component sensors and methyl-acceptingchemotaxis proteins suggest a role for linker region amphipathic helices intransmembrane signal transduction
    • Williams S.B., Stewart V. Functional similarities among two-component sensors and methyl-acceptingchemotaxis proteins suggest a role for linker region amphipathic helices intransmembrane signal transduction. Mol. Microbiol. 1999, 33:1093-1102.
    • (1999) Mol. Microbiol. , vol.33 , pp. 1093-1102
    • Williams, S.B.1    Stewart, V.2
  • 14
    • 0032766134 scopus 로고    scopus 로고
    • The cytoplasmic helical linker domain of receptor histidine kinase andmethyl-accepting proteins is common to many prokaryotic signalling proteins
    • Aravind L., Ponting C.P. The cytoplasmic helical linker domain of receptor histidine kinase andmethyl-accepting proteins is common to many prokaryotic signalling proteins. FEMS Microbiol. Lett. 1999, 176:111-116.
    • (1999) FEMS Microbiol. Lett. , vol.176 , pp. 111-116
    • Aravind, L.1    Ponting, C.P.2
  • 15
    • 0032730205 scopus 로고    scopus 로고
    • Histidine kinases: Diversity of domain organization
    • Dutta R., Qin L., Inouye M. Histidine kinases: Diversity of domain organization. Mol. Microbiol. 1999, 34:633-640.
    • (1999) Mol. Microbiol. , vol.34 , pp. 633-640
    • Dutta, R.1    Qin, L.2    Inouye, M.3
  • 16
    • 0027056677 scopus 로고
    • Communication modules in bacterial signaling proteins
    • Parkinson J.S., Kofoid E.C. Communication modules in bacterial signaling proteins. Annu. Rev. Genet. 1992, 26:71-112.
    • (1992) Annu. Rev. Genet. , vol.26 , pp. 71-112
    • Parkinson, J.S.1    Kofoid, E.C.2
  • 18
    • 0030917808 scopus 로고    scopus 로고
    • A two-component system in Ralstonia (Pseudomonas) solanacearum modulates production of PhcA-regulated virulence factors in response to 3-hydroxypalmiticacid methyl ester
    • Clough S.J., Lee K.E., Schell M.A., Denny T.P. A two-component system in Ralstonia (Pseudomonas) solanacearum modulates production of PhcA-regulated virulence factors in response to 3-hydroxypalmiticacid methyl ester. J. Bacteriol. 1997, 179:3639-3648.
    • (1997) J. Bacteriol. , vol.179 , pp. 3639-3648
    • Clough, S.J.1    Lee, K.E.2    Schell, M.A.3    Denny, T.P.4
  • 19
    • 0032184886 scopus 로고    scopus 로고
    • Formation of a novel four-helix bundle and molecular recognition sites by dimerization of a response regulator phosphotransferase
    • Varughese K.I., Madhusudan, Zhou X.Z., Whiteley J.M., Hoch J.A. Formation of a novel four-helix bundle and molecular recognition sites by dimerization of a response regulator phosphotransferase. Mol. Cell. 1998, 2:485-493.
    • (1998) Mol. Cell. , vol.2 , pp. 485-493
    • Varughese, K.I.1    Madhusudan2    Zhou, X.Z.3    Whiteley, J.M.4    Hoch, J.A.5
  • 20
    • 0033534368 scopus 로고    scopus 로고
    • Structure of CheA, a signal-transducing histidine kinase
    • Bilwes A.M., Alex L.A., Crane B.R., Simon M.I. Structure of CheA, a signal-transducing histidine kinase. Cell. 1999, 96:131-141.
    • (1999) Cell. , vol.96 , pp. 131-141
    • Bilwes, A.M.1    Alex, L.A.2    Crane, B.R.3    Simon, M.I.4
  • 21
    • 0035903179 scopus 로고    scopus 로고
    • Crystal structure of the CheA histidine phosphotransfer domain that mediates response regulator phosphorylation in bacterial chemotaxis
    • Mourey L., Da Re S., Pedelacq J.D., Tolstykh T., Faurie C., Guillet V., Stock J.B., Samama J.P. Crystal structure of the CheA histidine phosphotransfer domain that mediates response regulator phosphorylation in bacterial chemotaxis. J. Biol. Chem. 2001.
    • (2001) J. Biol. Chem.
    • Mourey, L.1    Da Re, S.2    Pedelacq, J.D.3    Tolstykh, T.4    Faurie, C.5    Guillet, V.6    Stock, J.B.7    Samama, J.P.8
  • 22
    • 0032575326 scopus 로고    scopus 로고
    • Cysteine and disulfide scanning reveals two amphiphilic helices in the linker region of the aspartate chemoreceptor
    • Butler S.L., Falke J.J. Cysteine and disulfide scanning reveals two amphiphilic helices in the linker region of the aspartate chemoreceptor. Biochemistry 1998, 37:10746-10756.
    • (1998) Biochemistry , vol.37 , pp. 10746-10756
    • Butler, S.L.1    Falke, J.J.2
  • 23
    • 0032539854 scopus 로고    scopus 로고
    • Computational learning reveals coiled coil-like motifs in histidine kinase linker domains
    • Singh M., Berger B., Kim P.S., Berger J.M., Cochran A.G. Computational learning reveals coiled coil-like motifs in histidine kinase linker domains. Proc. Natl. Acad. Sci. USA 1998, 95:2738-2743.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2738-2743
    • Singh, M.1    Berger, B.2    Kim, P.S.3    Berger, J.M.4    Cochran, A.G.5
  • 25
    • 0030595328 scopus 로고    scopus 로고
    • Signal transduction via the multi-step phosphorelay: Not necessarily a road less traveled
    • Appleby J.L., Parkinson J.S., Bourret R.B. Signal transduction via the multi-step phosphorelay: Not necessarily a road less traveled. Cell 1996, 86:845-848.
    • (1996) Cell , vol.86 , pp. 845-848
    • Appleby, J.L.1    Parkinson, J.S.2    Bourret, R.B.3
  • 26
    • 0033104316 scopus 로고    scopus 로고
    • Signalling pathways in two-component phosphorelay systems
    • Perraud A.L., Weiss V., Gross R. Signalling pathways in two-component phosphorelay systems. Trends Microbiol. 1999, 7:115-120.
    • (1999) Trends Microbiol. , vol.7 , pp. 115-120
    • Perraud, A.L.1    Weiss, V.2    Gross, R.3
  • 27
    • 0007992814 scopus 로고    scopus 로고
    • Protein plasticity to the extreme: Changing the topology of a 4-alpha-helical bundle with a single amino acid substitution
    • Glykos N.M., Cesareni G., Kokkinidis M. Protein plasticity to the extreme: Changing the topology of a 4-alpha-helical bundle with a single amino acid substitution. Structure Fold. Des. 1999, 7:597-603.
    • (1999) Structure Fold. Des. , vol.7 , pp. 597-603
    • Glykos, N.M.1    Cesareni, G.2    Kokkinidis, M.3
  • 28
    • 0033536688 scopus 로고    scopus 로고
    • Conservation of structure and function among histidine-containing phosphotransfer (Hpt) domains as revealed by crystal structure YPD1
    • Xu Q., West A. Conservation of structure and function among histidine-containing phosphotransfer (Hpt) domains as revealed by crystal structure YPD1. J. Mol. Biol. 1999, 292:1039-1050.
    • (1999) J. Mol. Biol. , vol.292 , pp. 1039-1050
    • Xu, Q.1    West, A.2
  • 29
    • 0030940479 scopus 로고    scopus 로고
    • Insights into multistep phosphorelay from the crystal structure of the C-terminal HPt domain of ArcB
    • Kato M., Mizuno T., Shimizu T., Hakoshima T. Insights into multistep phosphorelay from the crystal structure of the C-terminal HPt domain of ArcB. Cell 1997, 88:717-723.
    • (1997) Cell , vol.88 , pp. 717-723
    • Kato, M.1    Mizuno, T.2    Shimizu, T.3    Hakoshima, T.4
  • 32
    • 0032804537 scopus 로고    scopus 로고
    • Phosphatidylinositol phosphate kinase: A link between protein kinase and glutathione synthase folds
    • Grishin N.V. Phosphatidylinositol phosphate kinase: A link between protein kinase and glutathione synthase folds. J. Mol. Biol. 1999, 291:239-247.
    • (1999) J. Mol. Biol. , vol.291 , pp. 239-247
    • Grishin, N.V.1
  • 34
    • 0025185653 scopus 로고
    • Structural resemblance between the families of bacterial signal-transduction proteins and of G proteins revealed by graph-theoretical techniques
    • Artymiuk P.J., Rice D.W., Mitchell E.M., Willett P. Structural resemblance between the families of bacterial signal-transduction proteins and of G proteins revealed by graph-theoretical techniques. Protein Eng. 1990, 4:39-43.
    • (1990) Protein Eng. , vol.4 , pp. 39-43
    • Artymiuk, P.J.1    Rice, D.W.2    Mitchell, E.M.3    Willett, P.4
  • 35
    • 0033561221 scopus 로고    scopus 로고
    • Identification of the Mg(2+)-binding site in the P-type ATPase and phosphatase members of the HAD (haloacid dehalogenase) superfamily by structural similarity to the response regulator protein CheY
    • Ridder I.S., Dijkstra B.W. Identification of the Mg(2+)-binding site in the P-type ATPase and phosphatase members of the HAD (haloacid dehalogenase) superfamily by structural similarity to the response regulator protein CheY. Biochem. J. 1999, 339:223-226.
    • (1999) Biochem. J. , vol.339 , pp. 223-226
    • Ridder, I.S.1    Dijkstra, B.W.2
  • 36
    • 0028116826 scopus 로고
    • Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity: Application of an iterative approach to database search
    • Koonin E.V, Tatusov R.L. Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity: Application of an iterative approach to database search. J. Mol. Biol. 1994, 244:125-132.
    • (1994) J. Mol. Biol. , vol.244 , pp. 125-132
    • Koonin, E.V.1    Tatusov, R.L.2
  • 37
    • 0034649566 scopus 로고    scopus 로고
    • Analysis of the genome sequence of the flowering plant Arabidopsis thaliana
    • Arabidopsis Genome Initiative
    • Arabidopsis Genome Initiative Analysis of the genome sequence of the flowering plant Arabidopsis thaliana. Nature (London) 2000, 408:796-815.
    • (2000) Nature (London) , vol.408 , pp. 796-815
  • 38
    • 0030909737 scopus 로고    scopus 로고
    • Nonplastid eukaryotic response regulators have a monophyletic origin and evolved from their bacterial precursors in parallel with their cognate sensor kinases
    • Pao G.M., Saier M.H. Nonplastid eukaryotic response regulators have a monophyletic origin and evolved from their bacterial precursors in parallel with their cognate sensor kinases. J. Mol. Evol. 1997, 44:605-613.
    • (1997) J. Mol. Evol. , vol.44 , pp. 605-613
    • Pao, G.M.1    Saier, M.H.2
  • 40
    • 0033277340 scopus 로고    scopus 로고
    • The histidine protein kinase superfamily
    • Grebe T.W., Stock J.B. The histidine protein kinase superfamily. Adv. Microb. Physiol. 1999, 41:139-227.
    • (1999) Adv. Microb. Physiol. , vol.41 , pp. 139-227
    • Grebe, T.W.1    Stock, J.B.2
  • 41
    • 0035019043 scopus 로고    scopus 로고
    • Genomic analysis of the histidine kinase family in bacteria and archaea
    • Kim Dj., Forst S. Genomic analysis of the histidine kinase family in bacteria and archaea. Microbiology 2001, 147:1197-1212.
    • (2001) Microbiology , vol.147 , pp. 1197-1212
    • Kim, D.1    Forst, S.2
  • 42
    • 0028955458 scopus 로고
    • Response regulators of bacterial signal transduction systems: Selective domain shuffling during evolution
    • Pao G.M., Saier M.H. Response regulators of bacterial signal transduction systems: Selective domain shuffling during evolution. J. Mol. Evol. 1995, 40:136-154.
    • (1995) J. Mol. Evol. , vol.40 , pp. 136-154
    • Pao, G.M.1    Saier, M.H.2
  • 43
    • 0026510592 scopus 로고
    • A novel sensor-regulator protein that belongs to the homologous family of signal-transduction proteins involved in adaptive responses in Escherichia coli
    • Nagasawa S., Tokishita S., Aiba H., Mizuno T. A novel sensor-regulator protein that belongs to the homologous family of signal-transduction proteins involved in adaptive responses in Escherichia coli. Mol. Microbiol. 1992, 6:799-807.
    • (1992) Mol. Microbiol. , vol.6 , pp. 799-807
    • Nagasawa, S.1    Tokishita, S.2    Aiba, H.3    Mizuno, T.4
  • 44
    • 0031470387 scopus 로고    scopus 로고
    • Archaea and the prokaryote-to-eukaryote transition
    • Brown J.R., Doolittle W.F. Archaea and the prokaryote-to-eukaryote transition. Microbiol. Mol. Biol. Rev. 1997, 61:456-502.
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 456-502
    • Brown, J.R.1    Doolittle, W.F.2
  • 45
    • 0025300402 scopus 로고
    • Towards a natural system of organisms: Proposal for the domains Archaea, Bacteria and Eucarya
    • Woese C.R., Kandler O., Wheelis M.L. Towards a natural system of organisms: Proposal for the domains Archaea, Bacteria and Eucarya. Proc. Natl. Acad. Sci. USA 1990, 87:4576-4579.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4576-4579
    • Woese, C.R.1    Kandler, O.2    Wheelis, M.L.3
  • 46
    • 0026743174 scopus 로고
    • Multiple protein sequence alignment from tertiary structure comparison: Assignment of global and residue confidence levels
    • Russell R.B., Barton G.J. Multiple protein sequence alignment from tertiary structure comparison: Assignment of global and residue confidence levels. Proteins 1992, 14:309-323.
    • (1992) Proteins , vol.14 , pp. 309-323
    • Russell, R.B.1    Barton, G.J.2
  • 47
    • 0034663597 scopus 로고    scopus 로고
    • Application of multiple sequence alignment profiles to improve protein secondary structure prediction
    • Cuff J.A., Barton G.J. Application of multiple sequence alignment profiles to improve protein secondary structure prediction. Proteins 2000, 40:502-511.
    • (2000) Proteins , vol.40 , pp. 502-511
    • Cuff, J.A.1    Barton, G.J.2


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