메뉴 건너뛰기




Volumn 52, Issue 10, 2013, Pages 1788-1801

Metal binding properties of escherichia coli YjiA, a member of the metal homeostasis-associated COG0523 family of GTPases

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL FUNCTIONS; DISSOCIATION CONSTANT; METAL BINDING PROPERTIES; NUCLEOTIDE-BINDING SITES; OLIGOMERIC STRUCTURE; REGULATORY FUNCTIONS; SITE DIRECTED MUTAGENESIS; STRUCTURAL INFORMATION;

EID: 84874997087     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi301600z     Document Type: Article
Times cited : (42)

References (65)
  • 1
    • 78649343406 scopus 로고    scopus 로고
    • Ribosome-associated GTPases: The role of RNA for GTPase activation
    • Clementi, N. and Polacek, N. (2010) Ribosome-associated GTPases: The role of RNA for GTPase activation RNA Biol. 7, 521-527
    • (2010) RNA Biol. , vol.7 , pp. 521-527
    • Clementi, N.1    Polacek, N.2
  • 3
    • 0025010979 scopus 로고
    • The GTPase superfamily: A conserved switch for diverse cell functions
    • Bourne, H. R., Sanders, D. A., and McCormick, F. (1990) The GTPase superfamily: A conserved switch for diverse cell functions Nature 348, 125-132
    • (1990) Nature , vol.348 , pp. 125-132
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 4
    • 0036295212 scopus 로고    scopus 로고
    • Classification and evolution of P-loop GTPases and related ATPases
    • Leipe, D. D., Wolf, Y. I., Koonin, E. V., and Aravind, L. (2002) Classification and evolution of P-loop GTPases and related ATPases J. Mol. Biol. 317, 41-72
    • (2002) J. Mol. Biol. , vol.317 , pp. 41-72
    • Leipe, D.D.1    Wolf, Y.I.2    Koonin, E.V.3    Aravind, L.4
  • 5
    • 0025048136 scopus 로고
    • The P-loop: A common motif in ATP- and GTP-binding proteins
    • Saraste, M., Sibbald, P. R., and Wittinghofer, A. (1990) The P-loop: A common motif in ATP- and GTP-binding proteins Trends Biochem. Sci. 15, 430-434
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 430-434
    • Saraste, M.1    Sibbald, P.R.2    Wittinghofer, A.3
  • 6
    • 70449732603 scopus 로고    scopus 로고
    • A subset of the diverse COG0523 family of putative metal chaperones is linked to zinc homeostasis in all kingdoms of life
    • Haas, C., Rodionov, D., Kropat, J., Malasarn, D., Merchant, S., and de Crecy-Lagard, V. (2009) A subset of the diverse COG0523 family of putative metal chaperones is linked to zinc homeostasis in all kingdoms of life BMC Genomics 10, 470
    • (2009) BMC Genomics , vol.10 , pp. 470
    • Haas, C.1    Rodionov, D.2    Kropat, J.3    Malasarn, D.4    Merchant, S.5    De Crecy-Lagard, V.6
  • 7
    • 0031733646 scopus 로고    scopus 로고
    • Identification of a Zinc-Specific Metalloregulatory Protein, Zur, Controlling Zinc Transport Operons in Bacillus subtilis
    • Gaballa, A. and Helmann, J. D. (1998) Identification of a Zinc-Specific Metalloregulatory Protein, Zur, Controlling Zinc Transport Operons in Bacillus subtilis J. Bacteriol. 180, 5815-5821
    • (1998) J. Bacteriol. , vol.180 , pp. 5815-5821
    • Gaballa, A.1    Helmann, J.D.2
  • 8
    • 76949106554 scopus 로고    scopus 로고
    • The Zur regulon of Corynebacterium glutamicum ATCC 13032
    • Schroeder, J., Jochmann, N., Rodionov, D., and Tauch, A. (2010) The Zur regulon of Corynebacterium glutamicum ATCC 13032 BMC Genomics 11, 12
    • (2010) BMC Genomics , vol.11 , pp. 12
    • Schroeder, J.1    Jochmann, N.2    Rodionov, D.3    Tauch, A.4
  • 9
    • 84861361870 scopus 로고    scopus 로고
    • Characterization of the Response to Zinc Deficiency in the Cyanobacterium Anabaena sp. Strain PCC 7120
    • Napolitano, M., Rubio, M. á., Santamaría-Gómez, J., Olmedo-Verd, E., Robinson, N. J., and Luque, I. (2012) Characterization of the Response to Zinc Deficiency in the Cyanobacterium Anabaena sp. Strain PCC 7120 J. Bacteriol. 194, 2426-2436
    • (2012) J. Bacteriol. , vol.194 , pp. 2426-2436
    • Napolitano, M.1    Santamaría-Gómez, J.2    Olmedo-Verd, E.3    Robinson, N.J.4    Luque, I.5
  • 10
    • 0026094290 scopus 로고
    • Nucleotide sequence and genetic analysis of a 13.1-kilobase-pair Pseudomonas denitrificans DNA fragment containing five cob genes and identification of structural genes encoding Cob(I)alamin adenosyltransferase, cobyric acid synthase, and bifunctional cobinamide kinase-cobinamide phosphate guanylyltransferase
    • Crouzet, J., Levy-Schil, S., Cameron, B., Cauchois, L., Rigault, S., Rouyez, M. C., Blanche, F., Debussche, L., and Thibaut, D. (1991) Nucleotide sequence and genetic analysis of a 13.1-kilobase-pair Pseudomonas denitrificans DNA fragment containing five cob genes and identification of structural genes encoding Cob(I)alamin adenosyltransferase, cobyric acid synthase, and bifunctional cobinamide kinase-cobinamide phosphate guanylyltransferase J. Bacteriol. 173, 6074-6087
    • (1991) J. Bacteriol. , vol.173 , pp. 6074-6087
    • Crouzet, J.1    Levy-Schil, S.2    Cameron, B.3    Cauchois, L.4    Rigault, S.5    Rouyez, M.C.6    Blanche, F.7    Debussche, L.8    Thibaut, D.9
  • 13
    • 0142071742 scopus 로고    scopus 로고
    • Comparative Genomics of the Vitamin B12 Metabolism and Regulation in Prokaryotes
    • Rodionov, D. A., Vitreschak, A. G., Mironov, A. A., and Gelfand, M. S. (2003) Comparative Genomics of the Vitamin B12 Metabolism and Regulation in Prokaryotes J. Biol. Chem. 278, 41148-41159
    • (2003) J. Biol. Chem. , vol.278 , pp. 41148-41159
    • Rodionov, D.A.1    Vitreschak, A.G.2    Mironov, A.A.3    Gelfand, M.S.4
  • 14
    • 0142231423 scopus 로고    scopus 로고
    • Motif CXCC in nitrile hydratase activator is critical for NHase biogenesis in vivo
    • Lu, J., Zheng, Y., Yamagishi, H., Odaka, M., Tsujimura, M., Maeda, M., and Endo, I. (2003) Motif CXCC in nitrile hydratase activator is critical for NHase biogenesis in vivo FEBS Lett. 553, 391-396
    • (2003) FEBS Lett. , vol.553 , pp. 391-396
    • Lu, J.1    Zheng, Y.2    Yamagishi, H.3    Odaka, M.4    Tsujimura, M.5    Maeda, M.6    Endo, I.7
  • 15
    • 34248669001 scopus 로고    scopus 로고
    • Functional specialization within the fur family of metalloregulators
    • Lee, J. W. and Helmann, J. (2007) Functional specialization within the Fur family of metalloregulators BioMetals 20, 485-499
    • (2007) BioMetals , vol.20 , pp. 485-499
    • Lee, J.W.1    Helmann, J.2
  • 16
    • 84860732015 scopus 로고    scopus 로고
    • YeiR: A metal-binding GTPase from Escherichia coli involved in metal homeostasis
    • Blaby-Haas, C. E., Flood, J. A., de Crécy-Lagard, V., and Zamble, D. B. (2012) YeiR: A metal-binding GTPase from Escherichia coli involved in metal homeostasis Metallomics 4, 488-497
    • (2012) Metallomics , vol.4 , pp. 488-497
    • Blaby-Haas, C.E.1    Flood, J.A.2    De Crécy-Lagard, V.3    Zamble, D.B.4
  • 18
    • 33748749374 scopus 로고    scopus 로고
    • Structural insights into HypB, a GTP-binding protein that regulates metal binding
    • Gasper, R., Scrima, A., and Wittinghofer, A. (2006) Structural insights into HypB, a GTP-binding protein that regulates metal binding J. Biol. Chem. 281, 27492-27502
    • (2006) J. Biol. Chem. , vol.281 , pp. 27492-27502
    • Gasper, R.1    Scrima, A.2    Wittinghofer, A.3
  • 19
    • 58949095956 scopus 로고    scopus 로고
    • Zn(II)-linked dimerization of UreG from Helicobacter pylori, a chaperone involved in nickel trafficking and urease activation
    • Zambelli, B., Turano, P., Musiani, F., Neyroz, P., and Ciurli, S. (2009) Zn(II)-linked dimerization of UreG from Helicobacter pylori, a chaperone involved in nickel trafficking and urease activation Proteins: Struct., Funct., Bioinf. 74, 222-239
    • (2009) Proteins: Struct., Funct., Bioinf. , vol.74 , pp. 222-239
    • Zambelli, B.1    Turano, P.2    Musiani, F.3    Neyroz, P.4    Ciurli, S.5
  • 20
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S. C. and von Hippel, P. H. (1989) Calculation of protein extinction coefficients from amino acid sequence data Anal. Biochem. 182, 319-326
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 21
    • 0022051541 scopus 로고
    • The use of 4-(2-pyridylazo)resorcinol in studies of zinc release from Escherichia coli aspartate transcarbamoylase
    • Hunt, J. B., Neece, S. H., and Ginsburg, A. (1985) The use of 4-(2-pyridylazo)resorcinol in studies of zinc release from Escherichia coli aspartate transcarbamoylase Anal. Biochem. 146, 150-157
    • (1985) Anal. Biochem. , vol.146 , pp. 150-157
    • Hunt, J.B.1    Neece, S.H.2    Ginsburg, A.3
  • 22
    • 7444271910 scopus 로고    scopus 로고
    • A high-performance liquid chromatography method for determining transition metal content in proteins
    • Atanassova, A., Lam, R., and Zamble, D. B. (2004) A high-performance liquid chromatography method for determining transition metal content in proteins Anal. Biochem. 335, 103-111
    • (2004) Anal. Biochem. , vol.335 , pp. 103-111
    • Atanassova, A.1    Lam, R.2    Zamble, D.B.3
  • 23
    • 29244444273 scopus 로고
    • Visual EGTA titration of calcium in the presence of magnesium
    • Sadek, F. S., Schmid, R. W., and Reilley, C. N. (1959) Visual EGTA titration of calcium in the presence of magnesium Talanta 2, 38-51
    • (1959) Talanta , vol.2 , pp. 38-51
    • Sadek, F.S.1    Schmid, R.W.2    Reilley, C.N.3
  • 24
    • 39749137469 scopus 로고    scopus 로고
    • Binding of zinc(II) and copper(II) to the full-length Alzheimer's amyloid-β peptide
    • Tõugu, V., Karafin, A., and Palumaa, P. (2008) Binding of zinc(II) and copper(II) to the full-length Alzheimer's amyloid-β peptide J. Neurochem. 104, 1249-1259
    • (2008) J. Neurochem. , vol.104 , pp. 1249-1259
    • Tõugu, V.1    Karafin, A.2    Palumaa, P.3
  • 25
    • 23444456924 scopus 로고    scopus 로고
    • How to study proteins by circular dichroism
    • Kelly, S. M., Jess, T. J., and Price, N. C. (2005) How to study proteins by circular dichroism Biochim. Biophys. Acta 1751, 119-139
    • (2005) Biochim. Biophys. Acta , vol.1751 , pp. 119-139
    • Kelly, S.M.1    Jess, T.J.2    Price, N.C.3
  • 26
    • 84868200797 scopus 로고    scopus 로고
    • Prediction of protein secondary structure from circular dichroism using theoretically derived spectra
    • Louis-Jeune, C., Andrade-Navarro, M. A., and Perez-Iratxeta, C. (2012) Prediction of protein secondary structure from circular dichroism using theoretically derived spectra Proteins: Struct., Funct., Bioinf. 80, 374-381
    • (2012) Proteins: Struct., Funct., Bioinf. , vol.80 , pp. 374-381
    • Louis-Jeune, C.1    Andrade-Navarro, M.A.2    Perez-Iratxeta, C.3
  • 27
    • 0018600707 scopus 로고
    • An improved assay for nanomole amounts of inorganic phosphate
    • Lanzetta, P. A., Alvarez, L. J., Reinach, P. S., and Candia, O. A. (1979) An improved assay for nanomole amounts of inorganic phosphate Anal. Biochem. 100, 95-97
    • (1979) Anal. Biochem. , vol.100 , pp. 95-97
    • Lanzetta, P.A.1    Alvarez, L.J.2    Reinach, P.S.3    Candia, O.A.4
  • 28
    • 0035121475 scopus 로고    scopus 로고
    • CHOOCH: A program for deriving anomalous-scattering factors from X-ray fluorescence spectra
    • Evans, G. and Pettifer, R. F. (2001) CHOOCH: A program for deriving anomalous-scattering factors from X-ray fluorescence spectra J. Appl. Crystallogr. 34, 82-86
    • (2001) J. Appl. Crystallogr. , vol.34 , pp. 82-86
    • Evans, G.1    Pettifer, R.F.2
  • 30
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • (Charles, W. Carter, J. and Sweet, R. M. Eds.) pp, Academic Press, New York.
    • Otwinowski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. In Methods in Enzymology (Charles, W., Carter, J., and Sweet, R. M., Eds.) pp 307-326, Academic Press, New York.
    • (1997) Methods in Enzymology , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 36
    • 33646260450 scopus 로고    scopus 로고
    • Optimal description of a protein structure in terms of multiple groups undergoing TLS motion
    • Painter, J. and Merritt, E. A. (2006) Optimal description of a protein structure in terms of multiple groups undergoing TLS motion Acta Crystallogr. D62, 439-450
    • (2006) Acta Crystallogr. , vol.62 , pp. 439-450
    • Painter, J.1    Merritt, E.A.2
  • 37
    • 33645158291 scopus 로고    scopus 로고
    • TLSMD web server for the generation of multi-group TLS models
    • Painter, J. and Merritt, E. A. (2006) TLSMD web server for the generation of multi-group TLS models J. Appl. Crystallogr. 39, 109-111
    • (2006) J. Appl. Crystallogr. , vol.39 , pp. 109-111
    • Painter, J.1    Merritt, E.A.2
  • 41
    • 79955574923 scopus 로고    scopus 로고
    • version 1.3rl () Schrodinger, LLC, New York
    • The PyMOL Molecular Graphics System, version 1.3rl (2010) Schrodinger, LLC, New York.
    • (2010) The PyMOL Molecular Graphics System
  • 44
    • 70350680999 scopus 로고    scopus 로고
    • Nickel Homeostasis and Nickel Regulation: An Overview
    • Li, Y. and Zamble, D. B. (2009) Nickel Homeostasis and Nickel Regulation: An Overview Chem. Rev. 109, 4617-4643
    • (2009) Chem. Rev. , vol.109 , pp. 4617-4643
    • Li, Y.1    Zamble, D.B.2
  • 48
    • 0017818322 scopus 로고
    • Preparation and properties of cobalt(II) rubredoxin
    • May, S. W. and Kuo, J. Y. (1978) Preparation and properties of cobalt(II) rubredoxin Biochemistry 17, 3333-3338
    • (1978) Biochemistry , vol.17 , pp. 3333-3338
    • May, S.W.1    Kuo, J.Y.2
  • 50
    • 34548232365 scopus 로고    scopus 로고
    • Inference of Macromolecular Assemblies from Crystalline State
    • Krissinel, E. and Henrick, K. (2007) Inference of Macromolecular Assemblies from Crystalline State J. Mol. Biol. 372, 774-797
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 52
    • 79251559383 scopus 로고    scopus 로고
    • The Base-Pairing RNA Spot 42 Participates in a Multioutput Feedforward Loop to Help Enact Catabolite Repression in Escherichia coli
    • Beisel, C. L. and Storz, G. (2011) The Base-Pairing RNA Spot 42 Participates in a Multioutput Feedforward Loop to Help Enact Catabolite Repression in Escherichia coli Mol. Cell 41, 286-297
    • (2011) Mol. Cell , vol.41 , pp. 286-297
    • Beisel, C.L.1    Storz, G.2
  • 53
    • 0036224939 scopus 로고    scopus 로고
    • Over 1000 genes are involved in the DNA damage response of Escherichia coli
    • Khil, P. P. and Camerini-Otero, R. D. (2002) Over 1000 genes are involved in the DNA damage response of Escherichia coli Mol. Microbiol. 44, 89-105
    • (2002) Mol. Microbiol. , vol.44 , pp. 89-105
    • Khil, P.P.1    Camerini-Otero, R.D.2
  • 55
    • 21544440823 scopus 로고
    • Order of stability of metal complexes
    • Irving, H. and Williams, R. J. P. (1948) Order of stability of metal complexes Nature 162, 746-747
    • (1948) Nature , vol.162 , pp. 746-747
    • Irving, H.1    Williams, R.J.P.2
  • 56
    • 35748974830 scopus 로고    scopus 로고
    • Occurrence, classification, and biological function of hydrogenases: An overview
    • Vignais, P. M. and Billoud, B. (2007) Occurrence, classification, and biological function of hydrogenases: An overview Chem. Rev. 107, 4206-4272
    • (2007) Chem. Rev. , vol.107 , pp. 4206-4272
    • Vignais, P.M.1    Billoud, B.2
  • 57
    • 55549132995 scopus 로고    scopus 로고
    • Microbial Physiology of Nickel and Cobalt
    • (Nies, D. and Silver, S. Eds.) pp, Springer, Berlin. - 320
    • Hausinger, R. and Zamble, D. (2007) Microbial Physiology of Nickel and Cobalt. In Molecular Microbiology of Heavy Metals (Nies, D. and Silver, S., Eds.) pp 287-320, Springer, Berlin.
    • (2007) Molecular Microbiology of Heavy Metals , pp. 287
    • Hausinger, R.1    Zamble, D.2
  • 58
    • 80051546547 scopus 로고    scopus 로고
    • Relationship between the GTPase, metal-binding, and dimerization activities of E. coli HypB
    • Cai, F., Ngu, T., Kaluarachchi, H., and Zamble, D. (2011) Relationship between the GTPase, metal-binding, and dimerization activities of E. coli HypB J. Biol. Inorg. Chem. 16, 857-868
    • (2011) J. Biol. Inorg. Chem. , vol.16 , pp. 857-868
    • Cai, F.1    Ngu, T.2    Kaluarachchi, H.3    Zamble, D.4
  • 59
    • 79952385857 scopus 로고    scopus 로고
    • Effects of Metal on the Biochemical Properties of Helicobacter pylori HypB, a Maturation Factor of [NiFe]-Hydrogenase and Urease
    • Sydor, A. M., Liu, J., and Zamble, D. B. (2011) Effects of Metal on the Biochemical Properties of Helicobacter pylori HypB, a Maturation Factor of [NiFe]-Hydrogenase and Urease J. Bacteriol. 193, 1359-1368
    • (2011) J. Bacteriol. , vol.193 , pp. 1359-1368
    • Sydor, A.M.1    Liu, J.2    Zamble, D.B.3
  • 60
    • 84863149329 scopus 로고    scopus 로고
    • Metallo-GTPase HypB from Helicobacter pylori and Its Interaction with Nickel Chaperone Protein HypA
    • Xia, W., Li, H., Yang, X., Wong, K. B., and Sun, H. (2012) Metallo-GTPase HypB from Helicobacter pylori and Its Interaction with Nickel Chaperone Protein HypA J. Biol. Chem. 287, 6753-6763
    • (2012) J. Biol. Chem. , vol.287 , pp. 6753-6763
    • Xia, W.1    Li, H.2    Yang, X.3    Wong, K.B.4    Sun, H.5
  • 61
    • 0027450599 scopus 로고
    • The product of the hypB gene, which is required for nickel incorporation into hydrogenases, is a novel guanine nucleotide-binding protein
    • Maier, T., Jacobi, A., Sauter, M., and Böck, A. (1993) The product of the hypB gene, which is required for nickel incorporation into hydrogenases, is a novel guanine nucleotide-binding protein J. Bacteriol. 175, 630-635
    • (1993) J. Bacteriol. , vol.175 , pp. 630-635
    • Maier, T.1    Jacobi, A.2    Sauter, M.3    Böck, A.4
  • 63
    • 83455221556 scopus 로고    scopus 로고
    • Escherichia coli SlyD, More Than a Ni(II) Reservoir
    • Kaluarachchi, H., Zhang, J. W., and Zamble, D. B. (2011) Escherichia coli SlyD, More Than a Ni(II) Reservoir Biochemistry 50, 10761-10763
    • (2011) Biochemistry , vol.50 , pp. 10761-10763
    • Kaluarachchi, H.1    Zhang, J.W.2    Zamble, D.B.3
  • 65
    • 34249857539 scopus 로고    scopus 로고
    • COBALT: Constraint-based alignment tool for multiple protein sequences
    • Papadopoulos, J. S. and Agarwala, R. (2007) COBALT: Constraint-based alignment tool for multiple protein sequences Bioinformatics 23, 1073-1079
    • (2007) Bioinformatics , vol.23 , pp. 1073-1079
    • Papadopoulos, J.S.1    Agarwala, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.