메뉴 건너뛰기




Volumn 5, Issue , 2014, Pages

Erratum: Visualizing autophosphorylation in histidine kinases (Nature Communications (2014) 5 (3258) DOI:10.1038/ncomms4258);Visualizing autophosphorylation in histidine kinases

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN HISTIDINE KINASE; ENVZ PROTEIN, E COLI; ESCHERICHIA COLI PROTEIN; MULTIENZYME COMPLEX; OUTER MEMBRANE PROTEIN; PROTEIN KINASE; PROTEIN-HISTIDINE KINASE;

EID: 84893827341     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms4645     Document Type: Erratum
Times cited : (116)

References (46)
  • 1
    • 70349541000 scopus 로고    scopus 로고
    • Biological insights from structures of two-component proteins
    • Gao, R. & Stock, A. M. Biological insights from structures of two-component proteins. Annu. Rev. Microbiol. 63, 133-154 (2009)
    • (2009) Annu. Rev. Microbiol , Issue.63 , pp. 133-154
    • Gao, R.1    Stock, A.M.2
  • 2
    • 0024759933 scopus 로고
    • Phosphorylation and dephosphorylation of a bacterial transcriptional activator by a transmembrane receptor
    • Igo, M. M., Ninfa, A. J., Stock, J. B. & Silhavy, T. J. Phosphorylation and dephosphorylation of a bacterial transcriptional activator by a transmembrane receptor. Genes Dev. 3, 1725-1734 (1989)
    • (1989) Genes Dev , vol.3 , pp. 1725-1734
    • Igo, M.M.1    Ninfa, A.J.2    Stock, J.B.3    Silhavy, T.J.4
  • 3
    • 0035798570 scopus 로고    scopus 로고
    • Structural and mutational analysis of the PhoQ histidine kinase catalytic domain. Insight into the reaction mechanism
    • Marina, A., Mott, C., Auyzenberg, A., Hendrickson, W. A. & Waldburger, C. D. Structural and mutational analysis of the PhoQ histidine kinase catalytic domain. Insight into the reaction mechanism. J. Biol. Chem. 276, 41182-41190 (2001)
    • (2001) J. Biol. Chem , vol.276 , pp. 41182-41190
    • Marina, A.1    Mott, C.2    Auyzenberg, A.3    Hendrickson, W.A.4
  • 5
    • 0033985080 scopus 로고    scopus 로고
    • GHKL, an emergent ATPase/kinase superfamily
    • DOI 10.1016/S0968-0004(99)01503-0, PII S0968000499015030
    • Dutta, R. & Inouye, M. GHKL, an emergent ATPase/kinase superfamily. Trends Biochem. Sci. 25, 24-28 (2000) (Pubitemid 30060426)
    • (2000) Trends in Biochemical Sciences , vol.25 , Issue.1 , pp. 24-28
    • Dutta, R.1    Inouye, M.2
  • 6
    • 29244433095 scopus 로고    scopus 로고
    • Structure of the entire cytoplasmic portion of a sensor histidine-kinase protein
    • DOI 10.1038/sj.emboj.7600886
    • Marina, A., Waldburger, C. D. & Hendrickson, W. A. Structure of the entire cytoplasmic portion of a sensor histidine-kinase protein. EMBO J. 24, 4247-4259 (2005) (Pubitemid 41828900)
    • (2005) EMBO Journal , vol.24 , Issue.24 , pp. 4247-4259
    • Marina, A.1    Waldburger, C.D.2    Hendrickson, W.A.3
  • 7
    • 70349795241 scopus 로고    scopus 로고
    • Structural insight into partner specificity and phosphoryl transfer in two-component signal transduction
    • Casino, P., Rubio, V. & Marina, A. Structural insight into partner specificity and phosphoryl transfer in two-component signal transduction. Cell 139, 325-336 (2009)
    • (2009) Cell , vol.139 , pp. 325-336
    • Casino, P.1    Rubio, V.2    Marina, A.3
  • 8
    • 84879836986 scopus 로고    scopus 로고
    • Structural basis of a rationally rewired protein-protein interface critical to bacterial signaling
    • Podgornaia, A. I., Casino, P., Marina, A. & Laub, M. T. Structural basis of a rationally rewired protein-protein interface critical to bacterial signaling. Structure 21, 1636-1647 (2013)
    • Structure , vol.21 , Issue.1636-1647 , pp. 2013
    • Podgornaia, A.I.1    Casino, P.2    Marina, A.3    Laub, M.T.4
  • 9
    • 84874684844 scopus 로고    scopus 로고
    • Mechanistic insights revealed by the crystal structure of a histidine kinase with signal transducer and sensor domains
    • Wang, C. et al. Mechanistic insights revealed by the crystal structure of a histidine kinase with signal transducer and sensor domains. PLoS Biol. 11, e1001493 (2013)
    • (2013) PLoS Biol , vol.11
    • Wang, C.1
  • 10
    • 70349764676 scopus 로고    scopus 로고
    • Structure of PAS-linked histidine kinase and the response regulator complex
    • Yamada, S. et al. Structure of PAS-linked histidine kinase and the response regulator complex. Structure 17, 1333-1344 (2009)
    • (2009) Structure , vol.17 , pp. 1333-1344
    • Yamada, S.1
  • 12
    • 0034595228 scopus 로고    scopus 로고
    • Asymmetry in the autophosphorylation of the two-component regulatory system transmitter protein nitrogen regulator II of Escherichia coli
    • DOI 10.1021/bi992921w
    • Jiang, P., Peliska, J. A. & Ninfa, A. J. Asymmetry in the autophosphorylation of the two-component regulatory system transmitter protein nitrogen regulator II of Escherichia coli. Biochemistry 39, 5057-5065 (2000) (Pubitemid 30241626)
    • (2000) Biochemistry , vol.39 , Issue.17 , pp. 5057-5065
    • Jiang, P.1    Peliska, J.A.2    Ninfa, A.J.3
  • 13
    • 84863006375 scopus 로고    scopus 로고
    • Structural basis of histidine kinase autophosphorylation deduced by integrating genomics, molecular dynamics, and mutagenesis
    • Dago, A. E. et al. Structural basis of histidine kinase autophosphorylation deduced by integrating genomics, molecular dynamics, and mutagenesis. Proc. Natl Acad. Sci. USA 109, E1733-E1742 (2012)
    • (2012) Proc. Natl Acad. Sci. USA , vol.109
    • Dago, A.E.1
  • 15
    • 0027439298 scopus 로고
    • Mechanism of autophosphorylation of Escherichia coli nitrogen regulator II (NR(II) or NtrB): Trans-Phosphorylation between subunits
    • Ninfa, E. G., Atkinson, M. R., Kamberov, E. S. & Ninfa, A. J. Mechanism of autophosphorylation of Escherichia coli nitrogen regulator II (NRII or NtrB): trans-phosphorylation between subunits. J. Bacteriol. 175, 7024-7032 (1993) (Pubitemid 23322455)
    • (1993) Journal of Bacteriology , vol.175 , Issue.21 , pp. 7024-7032
    • Ninfa, E.G.1    Atkinson, M.R.2    Kamberov, E.S.3    Ninfa, A.J.4
  • 16
    • 0037954135 scopus 로고    scopus 로고
    • Spontaneous subunit exchange and biochemical evidence for trans-autophosphorylation in a dimer of Escherichia coli histidine kinase (EnvZ)
    • DOI 10.1016/S0022-2836(03)00446-7
    • Cai, S. J. & Inouye, M. Spontaneous subunit exchange and biochemical evidence for trans-autophosphorylation in a dimer of Escherichia coli histidine kinase (EnvZ) J. Mol. Biol. 329, 495-503 (2003) (Pubitemid 36593208)
    • (2003) Journal of Molecular Biology , vol.329 , Issue.3 , pp. 495-503
    • Cai, S.-J.1    Inouye, M.2
  • 18
    • 78649658931 scopus 로고    scopus 로고
    • The mechanism of signal transduction by two-component systems
    • Casino, P., Rubio, V. & Marina, A. The mechanism of signal transduction by two-component systems. Curr. Opin. Struct. Biol. 20, 763-771 (2010)
    • Curr. Opin. Struct. Biol , vol.20 , Issue.763-771 , pp. 2010
    • Casino, P.1    Rubio, V.2    Marina, A.3
  • 19
    • 84875229542 scopus 로고    scopus 로고
    • Helix bundle loops determine whether histidine kinases autophosphorylate in cis or in trans
    • Ashenberg, O., Keating, A. E. & Laub, M. T. Helix bundle loops determine whether histidine kinases autophosphorylate in cis or in trans. J. Mol. Biol. 425, 1198-1209 (2013)
    • (2013) J. Mol. Biol. , vol.425 , pp. 1198-1209
    • Ashenberg, O.1    Keating, A.E.2    Laub, M.T.3
  • 21
    • 0027441194 scopus 로고
    • Mutational analysis of the bacterial signal-transducing protein kinase/phosphatase nitrogen regulator II (NR(II) or NtrB)
    • Atkinson, M. R. & Ninfa, A. J. Mutational analysis of the bacterial signaltransducing protein kinase/phosphatase nitrogen regulator II (NRII or NtrB) J. Bacteriol. 175, 7016-7023 (1993) (Pubitemid 23322454)
    • (1993) Journal of Bacteriology , vol.175 , Issue.21 , pp. 7016-7023
    • Atkinson, M.R.1    Ninfa, A.J.2
  • 22
    • 80052568134 scopus 로고    scopus 로고
    • CrdS and CrdA comprise a two-component system that is cooperatively regulated by the Che3 chemosensory system in Myxococcus xanthus
    • Willett, J. W. & Kirby, J. R. CrdS and CrdA comprise a two-component system that is cooperatively regulated by the Che3 chemosensory system in Myxococcus xanthus. mBio 2, e00110 (2011)
    • (2011) MBio , vol.2
    • Willett, J.W.1    Kirby, J.R.2
  • 23
    • 84870660891 scopus 로고    scopus 로고
    • Genetic and biochemical dissection of a HisKA domain identifies residues required exclusively for kinase and phosphatase activities
    • Willett, J. W. & Kirby, J. R. Genetic and biochemical dissection of a HisKA domain identifies residues required exclusively for kinase and phosphatase activities. PLoS Genet. 8, e1003084 (2012)
    • (2012) PLoS Genet , vol.8
    • Willett, J.W.1    Kirby, J.R.2
  • 24
    • 77950517828 scopus 로고    scopus 로고
    • Substrate binding and catalysis in carbamate kinase ascertained by crystallographic and site-directed mutagenesis studies: Movements and significance of a unique globular subdomain of this key enzyme for fermentative ATP production in bacteria
    • Ramon-Maiques, S. et al. Substrate binding and catalysis in carbamate kinase ascertained by crystallographic and site-directed mutagenesis studies: movements and significance of a unique globular subdomain of this key enzyme for fermentative ATP production in bacteria. J. Mol. Biol. 397, 1261-1275 (2010)
    • (2010) J. Mol. Biol , vol.397 , pp. 1261-1275
    • Ramon-Maiques, S.1
  • 25
    • 0031782823 scopus 로고    scopus 로고
    • Mutations that alter the kinase and phosphatase activities of the two- component sensor EnvZ
    • Hsing, W., Russo, F. D., Bernd, K. K. & Silhavy, T. J. Mutations that alter the kinase and phosphatase activities of the two-component sensor EnvZ. J. Bacteriol. 180, 4538-4546 (1998) (Pubitemid 28405579)
    • (1998) Journal of Bacteriology , vol.180 , Issue.17 , pp. 4538-4546
    • Hsing, W.1    Russo, F.D.2    Bernd, K.K.3    Silhavy, T.J.4
  • 26
    • 66249128912 scopus 로고    scopus 로고
    • A method for the analysis of domain movements in large biomolecular complexes
    • Poornam, G. P., Matsumoto, A., Ishida, H. & Hayward, S. A method for the analysis of domain movements in large biomolecular complexes. Proteins 76, 201-212 (2009)
    • (2009) Proteins , vol.76 , pp. 201-212
    • Poornam, G.P.1    Matsumoto, A.2    Ishida, H.3    Hayward, S.4
  • 28
    • 0030724727 scopus 로고    scopus 로고
    • Mechanisms of signaling and related enzymes
    • DOI 10.1002/(SICI)1097-0134(199712)29: 4<401::AID-PROT1>3.0.CO;2-B
    • Mildvan, A. S. Mechanisms of signaling and related enzymes. Proteins 29, 401-416 (1997) (Pubitemid 27520194)
    • (1997) Proteins: Structure, Function and Genetics , vol.29 , Issue.4 , pp. 401-416
    • Mildvan, A.S.1
  • 29
    • 0036372943 scopus 로고    scopus 로고
    • The role of the G2 box, a conserved motif in the histidine kinase superfamily, in modulating the function of EnvZ
    • DOI 10.1046/j.1365-2958.2002.03061.x
    • Zhu, Y. & Inouye, M. The role of the G2 box, a conserved motif in the histidine kinase superfamily, in modulating the function of EnvZ. Mol. Microbiol. 45, 653-663 (2002) (Pubitemid 34989174)
    • (2002) Molecular Microbiology , vol.45 , Issue.3 , pp. 653-663
    • Zhu, Y.1    Inouye, M.2
  • 31
    • 0347854362 scopus 로고    scopus 로고
    • The HWE Histidine Kinases, a New Family of Bacterial Two-Component Sensor Kinases with Potentially Diverse Roles in Environmental Signaling
    • DOI 10.1128/JB.186.2.445-453.2004
    • Karniol, B. & Vierstra, R. D. The HWE histidine kinases, a new family of bacterial two-component sensor kinases with potentially diverse roles in environmental signaling. J. Bacteriol. 186, 445-453 (2004) (Pubitemid 38076435)
    • (2004) Journal of Bacteriology , vol.186 , Issue.2 , pp. 445-453
    • Karniol, B.1    Vierstra, R.D.2
  • 32
    • 20444401591 scopus 로고    scopus 로고
    • Structural dissection of ATP turnover in the prototypical GHL ATPase TopoVI
    • DOI 10.1016/j.str.2005.03.013, PII S0969212605001371
    • Corbett, K. D. & Berger, J. M. Structural dissection of ATP turnover in the prototypical GHL ATPase TopoVI. Structure 13, 873-882 (2005) (Pubitemid 40804390)
    • (2005) Structure , vol.13 , Issue.6 , pp. 873-882
    • Corbett, K.D.1    Berger, J.M.2
  • 33
    • 33746364784 scopus 로고    scopus 로고
    • Structure and mechanism of the Hsp90 molecular chaperone machinery
    • DOI 10.1146/annurev.biochem.75.103004.142738
    • Pearl, L. H. & Prodromou, C. Structure and mechanism of the Hsp90 molecular chaperone machinery. Annu. Rev. Biochem. 75, 271-294 (2006) (Pubitemid 44118034)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 271-294
    • Pearl, L.H.1    Prodromou, C.2
  • 35
    • 84863622633 scopus 로고    scopus 로고
    • Adaptive mutations that prevent crosstalk enable the expansion of paralogous signaling protein families
    • Capra, E. J., Perchuk, B. S., Skerker, J. M. & Laub, M. T. Adaptive mutations that prevent crosstalk enable the expansion of paralogous signaling protein families. Cell 150, 222-232 (2012)
    • (2012) Cell , vol.150 , pp. 222-232
    • Capra, E.J.1    Perchuk, B.S.2    Skerker, J.M.3    Laub, M.T.4
  • 36
    • 58849159963 scopus 로고    scopus 로고
    • How to switch off a histidine kinase: Crystal structure of Geobacillus stearothermophilus KinB with the inhibitor Sda
    • Bick, M. J. et al. How to switch off a histidine kinase: crystal structure of Geobacillus stearothermophilus KinB with the inhibitor Sda. J. Mol. Biol. 386, 163-177 (2009)
    • (2009) J. Mol. Biol , vol.386 , pp. 163-177
    • Bick, M.J.1
  • 37
    • 84859388839 scopus 로고    scopus 로고
    • An asymmetry-to-symmetry switch in signal transmission by the histidine kinase receptor for TMAO
    • Moore, J. O. & Hendrickson, W. A. An asymmetry-to-symmetry switch in signal transmission by the histidine kinase receptor for TMAO. Structure 20, 729-741 (2012)
    • (2012) Structure , vol.20 , pp. 729-741
    • Moore, J.O.1    Hendrickson, W.A.2
  • 39
    • 0042848687 scopus 로고    scopus 로고
    • Mechanism of the PII-activated phosphatase activity of Escherichia coli NRII (NtrB): How the different domains of NRII collaborate to act as a phosphatase
    • DOI 10.1021/bi030065p
    • Pioszak, A. A. & Ninfa, A. J. Mechanism of the PII-activated phosphatase activity of Escherichia coli NRII (NtrB): how the different domains of NRII collaborate to act as a phosphatase. Biochemistry 42, 8885-8899 (2003) (Pubitemid 36899833)
    • (2003) Biochemistry , vol.42 , Issue.29 , pp. 8885-8899
    • Pioszak, A.A.1    Ninfa, A.J.2
  • 40
    • 77956181585 scopus 로고    scopus 로고
    • High-throughput production of human proteins for crystallization: The SGC experience
    • Savitsky, P. et al. High-throughput production of human proteins for crystallization: the SGC experience. J. Struct. Biol. 172, 3-13 (2010)
    • J. Struct. Biol , vol.172 , Issue.3-13 , pp. 2010
    • Savitsky, P.1
  • 41
    • 33847290484 scopus 로고    scopus 로고
    • Production of selenomethionyl proteins in prokaryotic and eukaryotic expression systems
    • DOI 10.1385/1-59745-209-2:91, Macromolecular Crystallography Protocols, Volume 1: Preparation and Crystallizationof Macromolecules
    • Doublie, S. Production of selenomethionyl proteins in prokaryotic and eukaryotic expression systems. Methods Mol. Biol. 363, 91-108 (2007) (Pubitemid 350183146)
    • (2007) Methods in Molecular Biology , vol.363 , pp. 91-108
    • Doublie, S.1
  • 42
    • 76449099287 scopus 로고    scopus 로고
    • Xds. Acta crystallogr
    • Kabsch, W. Xds. Acta Crystallogr. D Biol. Crystallogr. 66, 125-132 (2010)
    • (2010) D Biol. Crystallogr , vol.66 , pp. 125-132
    • Kabsch, W.1
  • 43
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66, 213-221 (2010)
    • Acta Crystallogr. D Biol. Crystallogr , vol.66 , Issue.213-221 , pp. 2010
    • Adams, P.D.1
  • 45
    • 79953737180 scopus 로고    scopus 로고
    • Overview of the CCP4 suite and current developments. Acta Crystallogr
    • Winn, M. D. et al. Overview of the CCP4 suite and current developments. Acta Crystallogr. D Biol. Crystallogr. 67, 235-242 (2011)
    • D Biol. Crystallogr , vol.67 , Issue.235-242 , pp. 2011
    • Winn, M.D.1
  • 46
    • 34247591513 scopus 로고    scopus 로고
    • Identification of a novel two component system in Thermotoga maritima. Complex stoichiometry and crystallization
    • DOI 10.1016/j.bbapap.2007.02.005, PII S1570963907000313
    • Casino, P., Fernandez-Alvarez, A., Alfonso, C., Rivas, G. & Marina, A. Identification of a novel two component system in Thermotoga maritima. Complex stoichiometry and crystallization. Biochim. Biophys. Acta 1774, 603-609 (2007) (Pubitemid 46670798)
    • (2007) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1774 , Issue.5 , pp. 603-609
    • Casino, P.1    Fernandez-Alvarez, A.2    Alfonso, C.3    Rivas, G.4    Marina, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.