메뉴 건너뛰기




Volumn 86, Issue 2, 2013, Pages 149-171

Molecular and cellular characterisation of the zinc uptake (Znu) system of nostoc punctiforme

Author keywords

Heavy metals; Metal transporters; Nostoc punctiforme; Zinc

Indexed keywords

ABC TRANSPORTER; ADENOSINE TRIPHOSPHATASE; CATION TRANSPORT PROTEIN; ESCHERICHIA COLI PROTEIN; ZINC; ZNUA PROTEIN, E COLI; ZNUB PROTEIN, E COLI; ZNUC PROTEIN, E COLI;

EID: 84885955839     PISSN: 01686496     EISSN: 15746941     Source Type: Journal    
DOI: 10.1111/1574-6941.12153     Document Type: Article
Times cited : (14)

References (71)
  • 1
    • 0030052870 scopus 로고    scopus 로고
    • Cation-dependant uptake of zinc in human fibroblasts
    • Ackland ML & McArdle HJ (1996) Cation-dependant uptake of zinc in human fibroblasts. Biometals 9: 29-37.
    • (1996) Biometals , vol.9 , pp. 29-37
    • Ackland, M.L.1    McArdle, H.J.2
  • 3
    • 77954065271 scopus 로고    scopus 로고
    • I-TASSER: a unified platform for automated protein structure and function prediction
    • Ambrish R, Kucukural A & Zhang Y (2010) I-TASSER: a unified platform for automated protein structure and function prediction. Nat Protoc 5: 725-738.
    • (2010) Nat Protoc , vol.5 , pp. 725-738
    • Ambrish, R.1    Kucukural, A.2    Zhang, Y.3
  • 4
  • 5
    • 33751056968 scopus 로고    scopus 로고
    • A soluble 3D LC/MS/MS proteome of the filamentous cyanobacterium Nostoc punctiforme
    • Anderson DC, Campbell EL & Meeks JC (2006) A soluble 3D LC/MS/MS proteome of the filamentous cyanobacterium Nostoc punctiforme. J Proteome Res 5: 3096-3104.
    • (2006) J Proteome Res , vol.5 , pp. 3096-3104
    • Anderson, D.C.1    Campbell, E.L.2    Meeks, J.C.3
  • 6
    • 4544375619 scopus 로고    scopus 로고
    • SigC, the group 2 sigma factor of RNA polymerase, contributes to the late-stage gene expression and nitrogen promoter recognition in the cyanobacterium Synechocystis sp. strain PCC 6803
    • Asayama M, Imamura S, Yoshihara S et al. (2004) SigC, the group 2 sigma factor of RNA polymerase, contributes to the late-stage gene expression and nitrogen promoter recognition in the cyanobacterium Synechocystis sp. strain PCC 6803. Biosci Biotechnol Biochem 68: 477-487.
    • (2004) Biosci Biotechnol Biochem , vol.68 , pp. 477-487
    • Asayama, M.1    Imamura, S.2    Yoshihara, S.3
  • 7
    • 0007583011 scopus 로고
    • Nickel uptake and toxicity in cyanobacteria
    • Azeez PA & Banerjee DK (1991) Nickel uptake and toxicity in cyanobacteria. Toxicol Environ Chem 30: 43-50.
    • (1991) Toxicol Environ Chem , vol.30 , pp. 43-50
    • Azeez, P.A.1    Banerjee, D.K.2
  • 9
    • 0018117246 scopus 로고
    • Toxicity of zinc to fungi, bacteria and coliphages: influences of chloride ions
    • Babich H & Stotzky G (1978) Toxicity of zinc to fungi, bacteria and coliphages: influences of chloride ions. Appl Environ Microbiol 36: 906-914.
    • (1978) Appl Environ Microbiol , vol.36 , pp. 906-914
    • Babich, H.1    Stotzky, G.2
  • 10
    • 0142216623 scopus 로고    scopus 로고
    • Structural determinants of metal specificity in the zinc transport protein ZnuA from Synechocystis 6803
    • Banerjee S, Wei B, Bhattacharyya-Pakrasi M, Pakrasi HB & Smith TJ (2003) Structural determinants of metal specificity in the zinc transport protein ZnuA from Synechocystis 6803. J Mol Biol 333: 1061-1069.
    • (2003) J Mol Biol , vol.333 , pp. 1061-1069
    • Banerjee, S.1    Wei, B.2    Bhattacharyya-Pakrasi, M.3    Pakrasi, H.B.4    Smith, T.J.5
  • 11
    • 33747089192 scopus 로고    scopus 로고
    • Cyanobacteria metal interactions: requirements, toxicity, and ecological implications
    • Baptista MS & Vasconcelos TM (2006) Cyanobacteria metal interactions: requirements, toxicity, and ecological implications. Crit Rev Microbiol 32: 127-137.
    • (2006) Crit Rev Microbiol , vol.32 , pp. 127-137
    • Baptista, M.S.1    Vasconcelos, T.M.2
  • 16
    • 0036073696 scopus 로고    scopus 로고
    • Role of the high-affinity zinc uptake znuABC system in Salmonella enterica serovar Typhimurium virulence
    • Campoy S, Jara M, Busquets N, Perez De Rozas AM, Badiola I & Barbe J (2002) Role of the high-affinity zinc uptake znuABC system in Salmonella enterica serovar Typhimurium virulence. Infect Immun 70: 4721-4725.
    • (2002) Infect Immun , vol.70 , pp. 4721-4725
    • Campoy, S.1    Jara, M.2    Busquets, N.3    Perez De Rozas, A.M.4    Badiola, I.5    Barbe, J.6
  • 17
    • 0032922903 scopus 로고    scopus 로고
    • Characterisation of a new operon encoding a Zur-like protein and an associated ABC zinc permease in Listeria monocytogenes
    • Dalet K, Gouin E, Cenatiempo Y, Cossart P & Hechard Y (1999) Characterisation of a new operon encoding a Zur-like protein and an associated ABC zinc permease in Listeria monocytogenes. FEMS Microbiol Lett 174: 111-116.
    • (1999) FEMS Microbiol Lett , vol.174 , pp. 111-116
    • Dalet, K.1    Gouin, E.2    Cenatiempo, Y.3    Cossart, P.4    Hechard, Y.5
  • 19
    • 0030868591 scopus 로고    scopus 로고
    • Competence and virulence of Streptococcus pneumoniae: Adc and PsaA mutants exhibit a requirement for Zn and Mn resulting from inactivation of putative ABC metal permeases
    • Dintilhac A, Alloing G, Granadel C & Claverys JP (1997) Competence and virulence of Streptococcus pneumoniae: Adc and PsaA mutants exhibit a requirement for Zn and Mn resulting from inactivation of putative ABC metal permeases. Mol Microbiol 25: 727-739.
    • (1997) Mol Microbiol , vol.25 , pp. 727-739
    • Dintilhac, A.1    Alloing, G.2    Granadel, C.3    Claverys, J.P.4
  • 20
    • 0027132575 scopus 로고
    • ABC transporters: bacterial exporters
    • Fath MJ & Kolter R (1993) ABC transporters: bacterial exporters. Microbiol Rev 57: 995-1017.
    • (1993) Microbiol Rev , vol.57 , pp. 995-1017
    • Fath, M.J.1    Kolter, R.2
  • 21
    • 0031733646 scopus 로고    scopus 로고
    • Identification of a zinc-specific metalloregulatory protein, Zur, controlling zinc transport operons in Bacillus subtilis
    • Gaballa A & Helmann JD (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
  • 22
    • 0036889461 scopus 로고    scopus 로고
    • Functional analysis of the Bacillus subtilis Zur regulon
    • Gaballa A, Wang T, Ye RW & Helmann JD (2002) Functional analysis of the Bacillus subtilis Zur regulon. J Bacteriol 184: 6508-6514.
    • (2002) J Bacteriol , vol.184 , pp. 6508-6514
    • Gaballa, A.1    Wang, T.2    Ye, R.W.3    Helmann, J.D.4
  • 23
    • 0037432713 scopus 로고    scopus 로고
    • The high-affinity zinc-uptake system znuACB is under control of the iron-uptake regulator (fur) gene in the animal pathogen Pasteurella multocida
    • Garrido ME, Bosch M, Medina R, Llagostera M, Perez de Rozas AM, Badiola I & Barbe J (2003) The high-affinity zinc-uptake system znuACB is under control of the iron-uptake regulator (fur) gene in the animal pathogen Pasteurella multocida. FEMS Microbiol Lett 221: 31-37.
    • (2003) FEMS Microbiol Lett , vol.221 , pp. 31-37
    • Garrido, M.E.1    Bosch, M.2    Medina, R.3    Llagostera, M.4    Perez de Rozas, A.M.5    Badiola, I.6    Barbe, J.7
  • 25
    • 0027475029 scopus 로고
    • The prediction and characterisation of metal binding site in proteins
    • Gregory DS, Martin ACR, Cheetham JC & Rees AR (1993) The prediction and characterisation of metal binding site in proteins. Protein Eng 6: 29-35.
    • (1993) Protein Eng , vol.6 , pp. 29-35
    • Gregory, D.S.1    Martin, A.C.R.2    Cheetham, J.C.3    Rees, A.R.4
  • 26
    • 0032779505 scopus 로고    scopus 로고
    • Biochemical and genetic evidence for participation of DevR in a phosphorelay signal transduction pathway essential for heterocyst maturation in Nostoc punctiforme ATCC 29133
    • Haggen KD & Meeks JC (1999) Biochemical and genetic evidence for participation of DevR in a phosphorelay signal transduction pathway essential for heterocyst maturation in Nostoc punctiforme ATCC 29133. J Bacteriol 181: 4430-4434.
    • (1999) J Bacteriol , vol.181 , pp. 4430-4434
    • Haggen, K.D.1    Meeks, J.C.2
  • 27
    • 0035696323 scopus 로고    scopus 로고
    • Bacterial zinc transporters and regulators
    • Hantke K (2001) Bacterial zinc transporters and regulators. Biometals 14: 239-249.
    • (2001) Biometals , vol.14 , pp. 239-249
    • Hantke, K.1
  • 28
    • 15744394198 scopus 로고    scopus 로고
    • Bacterial zinc uptake and regulators
    • Hantke K (2005) Bacterial zinc uptake and regulators. Curr Opin Microbiol 8: 196-202.
    • (2005) Curr Opin Microbiol , vol.8 , pp. 196-202
    • Hantke, K.1
  • 29
    • 0025047590 scopus 로고
    • Transposon vectors containing non-antibiotic resistance selection markers for cloning and stable chromosomal insertion of foreign genes in gram-negative bacteria
    • Herrero M, De Lorenzo V & Timmis KN (1990) Transposon vectors containing non-antibiotic resistance selection markers for cloning and stable chromosomal insertion of foreign genes in gram-negative bacteria. J Bacteriol 172: 6557-6567.
    • (1990) J Bacteriol , vol.172 , pp. 6557-6567
    • Herrero, M.1    De Lorenzo, V.2    Timmis, K.N.3
  • 30
    • 0035019469 scopus 로고    scopus 로고
    • ABC transporters: physiology, structure and mechanism - an overview
    • Higgins CF (2001) ABC transporters: physiology, structure and mechanism - an overview. Res Microbiol 152: 205-210.
    • (2001) Res Microbiol , vol.152 , pp. 205-210
    • Higgins, C.F.1
  • 31
    • 0024234855 scopus 로고
    • Clustal: a package for performing multiple sequence alignment on microcomputer
    • Higgins DG & Sharp PM (1988) Clustal: a package for performing multiple sequence alignment on microcomputer. Gene 73: 237-244.
    • (1988) Gene , vol.73 , pp. 237-244
    • Higgins, D.G.1    Sharp, P.M.2
  • 32
    • 0032698874 scopus 로고    scopus 로고
    • ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules in organisms from bacteria to humans
    • Holland IB & Blight MA (1999) ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules in organisms from bacteria to humans. J Mol Biol 293: 381-399.
    • (1999) J Mol Biol , vol.293 , pp. 381-399
    • Holland, I.B.1    Blight, M.A.2
  • 35
    • 0026786329 scopus 로고
    • Topology of the hydrophobic membrane-bound components of the histidine periplasmic permease. Comparison with other members of the family
    • Kerppola RE & Ames GF (1992) Topology of the hydrophobic membrane-bound components of the histidine periplasmic permease. Comparison with other members of the family. J Biol Chem 267: 2329-2336.
    • (1992) J Biol Chem , vol.267 , pp. 2329-2336
    • Kerppola, R.E.1    Ames, G.F.2
  • 36
    • 0036209769 scopus 로고    scopus 로고
    • The crystal structure of Zn(II)-free Treponema pallidum TroA, a periplasmic metal-binding protein, reveals a closed conformation
    • Lee YH, Dorwart MR, Hazlett KR, Deka RK, Norgard MV, Radolf JD & Hasemann CA (2002) The crystal structure of Zn(II)-free Treponema pallidum TroA, a periplasmic metal-binding protein, reveals a closed conformation. J Bacteriol 184: 2300-2304.
    • (2002) J Bacteriol , vol.184 , pp. 2300-2304
    • Lee, Y.H.1    Dorwart, M.R.2    Hazlett, K.R.3    Deka, R.K.4    Norgard, M.V.5    Radolf, J.D.6    Hasemann, C.A.7
  • 37
    • 34247269203 scopus 로고    scopus 로고
    • Crystal structure of the zinc-binding transport protein ZnuA from Escherichia coli reveals an unexpected variation in metal coordination
    • Li H & Jogl G (2007) Crystal structure of the zinc-binding transport protein ZnuA from Escherichia coli reveals an unexpected variation in metal coordination. J Mol Biol 368: 1358-1366.
    • (2007) J Mol Biol , vol.368 , pp. 1358-1366
    • Li, H.1    Jogl, G.2
  • 38
    • 0035016446 scopus 로고    scopus 로고
    • zur: a Zn(2+)-responsive regulatory element of Staphylococcus aureus
    • Lindsay JA & Foster SJ (2001) zur: a Zn(2+)-responsive regulatory element of Staphylococcus aureus. Microbiology 147: 1259-1266.
    • (2001) Microbiology , vol.147 , pp. 1259-1266
    • Lindsay, J.A.1    Foster, S.J.2
  • 39
    • 33846688359 scopus 로고    scopus 로고
    • Structure and function of ABC transporters: the ATP switch provides flexible control
    • Linton KJ & Higgins CF (2007) Structure and function of ABC transporters: the ATP switch provides flexible control. Pflugers Arch 453: 555-567.
    • (2007) Pflugers Arch , vol.453 , pp. 555-567
    • Linton, K.J.1    Higgins, C.F.2
  • 40
    • 0031934940 scopus 로고    scopus 로고
    • Histidine-based zinc-binding sequences and the antimicrobial activity of calprotectin
    • Loomas HJ, Hahn BL, Li QQ, Phadnis SH & Sohnle PG (1997) Histidine-based zinc-binding sequences and the antimicrobial activity of calprotectin. J Infect Dis 177: 812-814.
    • (1997) J Infect Dis , vol.177 , pp. 812-814
    • Loomas, H.J.1    Hahn, B.L.2    Li, Q.Q.3    Phadnis, S.H.4    Sohnle, P.G.5
  • 41
    • 70350637580 scopus 로고    scopus 로고
    • Coordination chemistry of bacterial metal transport and sensing
    • Ma Z, Jacobsen FE & Giedroc DP (2009) Coordination chemistry of bacterial metal transport and sensing. Chem Rev 109: 4644-4681.
    • (2009) Chem Rev , vol.109 , pp. 4644-4681
    • Ma, Z.1    Jacobsen, F.E.2    Giedroc, D.P.3
  • 43
    • 0028838717 scopus 로고
    • Threading a database of protein cores
    • Madej T, Gibrat JF & Bryant SH (1995) Threading a database of protein cores. Proteins 23: 356-369.
    • (1995) Proteins , vol.23 , pp. 356-369
    • Madej, T.1    Gibrat, J.F.2    Bryant, S.H.3
  • 44
    • 0034055985 scopus 로고    scopus 로고
    • Zinc and health: current status and future directions
    • McCall KA, Huang C & Fierke CA (2000) Zinc and health: current status and future directions. J Nutr 22: 1437-1446.
    • (2000) J Nutr , vol.22 , pp. 1437-1446
    • McCall, K.A.1    Huang, C.2    Fierke, C.A.3
  • 46
    • 11144356954 scopus 로고    scopus 로고
    • Zinc is a key factor in controlling alternation of two types of L31 protein in the Bacillus subtilis ribosome
    • Nanamiya H, Akanuma G, Natori Y et al. (2004) Zinc is a key factor in controlling alternation of two types of L31 protein in the Bacillus subtilis ribosome. Mol Microbiol 52: 273-283.
    • (2004) Mol Microbiol , vol.52 , pp. 273-283
    • Nanamiya, H.1    Akanuma, G.2    Natori, Y.3
  • 47
  • 48
    • 0026732140 scopus 로고
    • CzcR and CzcD, gene products affecting regulation of resistance to cobalt, zinc, and cadmium (czc system) in Alcaligenes eutrophus
    • Nies DH (1992) CzcR and CzcD, gene products affecting regulation of resistance to cobalt, zinc, and cadmium (czc system) in Alcaligenes eutrophus. J Bacteriol 174: 8102-8110.
    • (1992) J Bacteriol , vol.174 , pp. 8102-8110
    • Nies, D.H.1
  • 49
    • 0037162511 scopus 로고    scopus 로고
    • How are the ABC transporters energized?
    • Nikaido H (2002) How are the ABC transporters energized? P Natl Acad Sci USA 99: 9609-9610.
    • (2002) P Natl Acad Sci USA , vol.99 , pp. 9609-9610
    • Nikaido, H.1
  • 50
    • 0035807029 scopus 로고    scopus 로고
    • Characterization of the metal receptor sites in Escherichia coli Zur, an ultrasensitive zinc(II) metalloregulatory protein
    • Outten CE, Tobin DA, Penner-Hahn JE & O'Halloran TV (2001) Characterization of the metal receptor sites in Escherichia coli Zur, an ultrasensitive zinc(II) metalloregulatory protein. Biochemistry 40: 10417-10423.
    • (2001) Biochemistry , vol.40 , pp. 10417-10423
    • Outten, C.E.1    Tobin, D.A.2    Penner-Hahn, J.E.3    O'Halloran, T.V.4
  • 51
    • 34249811787 scopus 로고    scopus 로고
    • Zinc-responsive regulation of alternative ribosomal protein genes in Streptomyces coelicolor involves Zur and sR
    • Owen GA, Pascoe B, Kallifidas D & Paget MSB (2007) Zinc-responsive regulation of alternative ribosomal protein genes in Streptomyces coelicolor involves Zur and sR. J Bacteriol 189: 4078-4086.
    • (2007) J Bacteriol , vol.189 , pp. 4078-4086
    • Owen, G.A.1    Pascoe, B.2    Kallifidas, D.3    Paget, M.S.B.4
  • 52
    • 0031798662 scopus 로고    scopus 로고
    • The ZnuABC high-affinity zinc uptake system and its regulator Zur in Escherichia coli
    • Patzer SI & Hantke K (1998) The ZnuABC high-affinity zinc uptake system and its regulator Zur in Escherichia coli. Mol Microbiol 28: 1199-1210.
    • (1998) Mol Microbiol , vol.28 , pp. 1199-1210
    • Patzer, S.I.1    Hantke, K.2
  • 53
    • 0034637471 scopus 로고    scopus 로고
    • The zinc-responsive regulator Zur and its control of the znu gene cluster encoding the ZnuABC zinc uptake system in Escherichia coli
    • Patzer SI & Hantke K (2000) The zinc-responsive regulator Zur and its control of the znu gene cluster encoding the ZnuABC zinc uptake system in Escherichia coli. J Biol Chem 275: 24321-24332.
    • (2000) J Biol Chem , vol.275 , pp. 24321-24332
    • Patzer, S.I.1    Hantke, K.2
  • 54
    • 3242774756 scopus 로고    scopus 로고
    • Fur is involved in manganese-dependant regulation of mantA (sitA) expression in Sinorhizobium meliloti
    • Platero R, Peixoto L, O'Bian MR & Fabiano E (2004) Fur is involved in manganese-dependant regulation of mantA (sitA) expression in Sinorhizobium meliloti. Appl Environ Microbiol 70: 4349-4355.
    • (2004) Appl Environ Microbiol , vol.70 , pp. 4349-4355
    • Platero, R.1    Peixoto, L.2    O'Bian, M.R.3    Fabiano, E.4
  • 55
    • 34547810826 scopus 로고    scopus 로고
    • Sinorhizobium meliloti fur-like (Mur) protein binds a fur box-like sequence present in the mntA promoter in a manganese-responsive manner
    • Platero R, de Lorenzo V, Garat B & Fabiano E (2007) Sinorhizobium meliloti fur-like (Mur) protein binds a fur box-like sequence present in the mntA promoter in a manganese-responsive manner. Appl Environ Microbiol 73: 4832-4838.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 4832-4838
    • Platero, R.1    de Lorenzo, V.2    Garat, B.3    Fabiano, E.4
  • 56
    • 25844497061 scopus 로고    scopus 로고
    • Functional expression of a low-affinity zinc uptake transporter (Fr ZIP2) from pufferfish (Takifugu rubripes) in MDCK cells
    • Qiu A & Hogstrand C (2005) Functional expression of a low-affinity zinc uptake transporter (Fr ZIP2) from pufferfish (Takifugu rubripes) in MDCK cells. Biochem J 390: 777-786.
    • (2005) Biochem J , vol.390 , pp. 777-786
    • Qiu, A.1    Hogstrand, C.2
  • 57
    • 33847240951 scopus 로고    scopus 로고
    • Proteomic analyses of the photoauto- and diazotrophically grown cyanobacterium Nostoc sp. PCC 73102
    • Ran L, Huang F, Ekman M, Klint J & Bergman B (2007) Proteomic analyses of the photoauto- and diazotrophically grown cyanobacterium Nostoc sp. PCC 73102. Microbiology 153: 608-618.
    • (2007) Microbiology , vol.153 , pp. 608-618
    • Ran, L.1    Huang, F.2    Ekman, M.3    Klint, J.4    Bergman, B.5
  • 58
    • 0031475157 scopus 로고    scopus 로고
    • The zntA gene of Escherichia coli encodes a Zn(II)-translocating P-type ATPase
    • Rensing C, Mitra B & Rosen BP (1997) The zntA gene of Escherichia coli encodes a Zn(II)-translocating P-type ATPase. P Natl Acad Sci USA 94: 14326-14331.
    • (1997) P Natl Acad Sci USA , vol.94 , pp. 14326-14331
    • Rensing, C.1    Mitra, B.2    Rosen, B.P.3
  • 60
    • 0032951188 scopus 로고    scopus 로고
    • Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters
    • Saurin W, Hofnung M & Dassa E (1999) Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J Mol Biol 48: 22-41.
    • (1999) J Mol Biol , vol.48 , pp. 22-41
    • Saurin, W.1    Hofnung, M.2    Dassa, E.3
  • 61
    • 0031810816 scopus 로고    scopus 로고
    • ATP-binding-cassette (ABC) transport systems: functional and structural aspects of the ATP-hydrolyzing subunits/domains
    • Schneider E & Hunke S (1998) ATP-binding-cassette (ABC) transport systems: functional and structural aspects of the ATP-hydrolyzing subunits/domains. FEMS Microbiol Rev 22: 1-20.
    • (1998) FEMS Microbiol Rev , vol.22 , pp. 1-20
    • Schneider, E.1    Hunke, S.2
  • 62
    • 33745933642 scopus 로고    scopus 로고
    • Metal homeostasis in cyanobacteria and chloroplasts. Balancing benefits and risks to the photosynthetic apparatus
    • Scholnick S & Keren N (2006) Metal homeostasis in cyanobacteria and chloroplasts. Balancing benefits and risks to the photosynthetic apparatus. Plant Physiol 141: 805-810.
    • (2006) Plant Physiol , vol.141 , pp. 805-810
    • Scholnick, S.1    Keren, N.2
  • 63
    • 34249806024 scopus 로고    scopus 로고
    • The zinc-responsive regulator Zur controls a zinc uptake system and some ribosomal proteins in Streptomyces coelicolor A3(2)
    • Shin JH, Oh SY, Kim SJ & Roe JH (2007) The zinc-responsive regulator Zur controls a zinc uptake system and some ribosomal proteins in Streptomyces coelicolor A3(2). J Bacteriol 189: 4070-4077.
    • (2007) J Bacteriol , vol.189 , pp. 4070-4077
    • Shin, J.H.1    Oh, S.Y.2    Kim, S.J.3    Roe, J.H.4
  • 64
    • 0028787216 scopus 로고
    • Genetic evidence of a major role for glucose-6-phosphate dehydrogenase in nitrogen fixation and dark growth of the cyanobacterium Nostoc sp. strain ATCC 29133
    • Summers ML, Wallis JG, Campbell EL & Meeks JC (1995) Genetic evidence of a major role for glucose-6-phosphate dehydrogenase in nitrogen fixation and dark growth of the cyanobacterium Nostoc sp. strain ATCC 29133. J Bacteriol 177: 6184-6194.
    • (1995) J Bacteriol , vol.177 , pp. 6184-6194
    • Summers, M.L.1    Wallis, J.G.2    Campbell, E.L.3    Meeks, J.C.4
  • 65
    • 0023225017 scopus 로고
    • Nucleotide sequence of a gene cluster involved in entry of E colicins and single-stranded DNA of infecting filamentous bacteriophages into Escherichia coli
    • Sun TP & Webster RE (1987) Nucleotide sequence of a gene cluster involved in entry of E colicins and single-stranded DNA of infecting filamentous bacteriophages into Escherichia coli. J Bacteriol 169: 2667-2674.
    • (1987) J Bacteriol , vol.169 , pp. 2667-2674
    • Sun, T.P.1    Webster, R.E.2
  • 66
    • 20644469022 scopus 로고    scopus 로고
    • The zinc uptake regulator Zur is essential for the full virulence of Xanthomonas campestris pv. campestris
    • Tang DJ, Li XJ, He YQ, Feng JX, Chen B & Tang JL (2005) The zinc uptake regulator Zur is essential for the full virulence of Xanthomonas campestris pv. campestris. Mol Plant Microbe Interact 18: 652-658.
    • (2005) Mol Plant Microbe Interact , vol.18 , pp. 652-658
    • Tang, D.J.1    Li, X.J.2    He, Y.Q.3    Feng, J.X.4    Chen, B.5    Tang, J.L.6
  • 67
    • 0027968068 scopus 로고
    • Clustal W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG & Gibson TJ (1994) Clustal W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22: 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 68
    • 0031574072 scopus 로고    scopus 로고
    • The Clustal X Windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson JD, Gibson TJ, Plewniak F & Higgins DG (1997) The Clustal X Windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 25: 4876-4881.
    • (1997) Nucleic Acids Res , vol.25 , pp. 4876-4881
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Higgins, D.G.4
  • 69
    • 34547646347 scopus 로고    scopus 로고
    • Possible regulatory role for the histidine-rich loop in the zinc transport protein, ZnuA
    • Wei B, Randich AM, Bhattacharyya-Pakrasi M, Pakrasi HB & Smith TJ (2007) Possible regulatory role for the histidine-rich loop in the zinc transport protein, ZnuA. Biochemistry 46: 8734-8743.
    • (2007) Biochemistry , vol.46 , pp. 8734-8743
    • Wei, B.1    Randich, A.M.2    Bhattacharyya-Pakrasi, M.3    Pakrasi, H.B.4    Smith, T.J.5
  • 70
    • 0030817277 scopus 로고    scopus 로고
    • Unusual structure of the tonB-exp DNA region of Xanthomonas campestris pv. campestris: tonB, exbB, and exbD1 are essential for ferric iron uptake, but exbD2 is not
    • Wiggerich HG, Klauke B, Koplin R, Priefer UB & Puhler A (1997) Unusual structure of the tonB-exp DNA region of Xanthomonas campestris pv. campestris: tonB, exbB, and exbD1 are essential for ferric iron uptake, but exbD2 is not. J Bacteriol 179: 7103-7110.
    • (1997) J Bacteriol , vol.179 , pp. 7103-7110
    • Wiggerich, H.G.1    Klauke, B.2    Koplin, R.3    Priefer, U.B.4    Puhler, A.5
  • 71
    • 36749061828 scopus 로고    scopus 로고
    • Template based modelling by I-TASSER in CASP7
    • Zhang Y (2007) Template based modelling by I-TASSER in CASP7. Proteins 69: 108-117.
    • (2007) Proteins , vol.69 , pp. 108-117
    • Zhang, Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.