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Volumn 108, Issue 12, 2011, Pages 5045-5050

Graded expression of zinc-responsive genes through two regulatory zinc-binding sites in Zur

Author keywords

Ferric uptake regulator; Graded transcription regulation; Regulatory metal

Indexed keywords

CHELATING AGENT; EDETIC ACID; N,N,N',N' TETRAKIS (2 PYRIDYLMETHYL)ETHYLENEDIAMINE; PROTEIN ZUR; UNCLASSIFIED DRUG; ZINC; ZINC BINDING PROTEIN;

EID: 79953212617     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1017744108     Document Type: Article
Times cited : (108)

References (39)
  • 4
    • 0035968001 scopus 로고    scopus 로고
    • Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis
    • DOI 10.1126/science.1060331
    • Outten CE, O'Halloran TV (2001) Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis. Science 292:2488-2492. (Pubitemid 32605687)
    • (2001) Science , vol.292 , Issue.5526 , pp. 2488-2492
    • Outten, C.E.1    O'Halloran, T.V.2
  • 5
    • 34547229278 scopus 로고    scopus 로고
    • Metal sensor proteins: Nature's metalloregulated allosteric switches
    • DOI 10.1039/b706769k
    • Giedroc DP, Arunkumar AI (2007) Metal sensor proteins: Nature's metalloregulated allosteric switches. Dalton Trans 29:3107-3120. (Pubitemid 47117766)
    • (2007) Dalton Transactions , Issue.29 , pp. 3107-3120
    • Giedroc, D.P.1    Arunkumar, A.I.2
  • 6
    • 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
  • 7
    • 33645242873 scopus 로고    scopus 로고
    • Liberation of zinc-containing L31 (RpmE) from ribosomes by its paralogous gene product, YtiA, in Bacillus subtilis
    • Akanuma G, Nanamiya H, Natori Y, Nomura N, Kawamura F (2006) Liberation of zinc-containing L31 (RpmE) from ribosomes by its paralogous gene product, YtiA, in Bacillus subtilis. J Bacteriol 188:2715-2720.
    • (2006) J Bacteriol , vol.188 , pp. 2715-2720
    • Akanuma, G.1    Nanamiya, H.2    Natori, Y.3    Nomura, N.4    Kawamura, F.5
  • 10
    • 34249811787 scopus 로고    scopus 로고
    • R
    • DOI 10.1128/JB.01901-06
    • Owen GA, Pascoe B, Kallifidas D, Paget MS (2007) Zinc-responsive regulation of alternative ribosomal protein genes in Streptomyces coelicolor involves zur and sigmaR. J Bacteriol 189:4078-4086. (Pubitemid 46847355)
    • (2007) Journal of Bacteriology , vol.189 , Issue.11 , pp. 4078-4086
    • Owen, G.A.1    Pascoe, B.2    Kallifidas, D.3    Paget, M.S.B.4
  • 12
    • 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
  • 13
    • 72049104812 scopus 로고    scopus 로고
    • The role of absC, a novel regulatory gene for secondary metabolism, in zinc-dependent antibiotic production in Streptomyces coelicolor A3(2)
    • Hesketh A, Kock H, Mootien S, Bibb M (2009) The role of absC, a novel regulatory gene for secondary metabolism, in zinc-dependent antibiotic production in Streptomyces coelicolor A3(2). Mol Microbiol 74:1427-1444.
    • (2009) Mol Microbiol , vol.74 , pp. 1427-1444
    • Hesketh, A.1    Kock, H.2    Mootien, S.3    Bibb, M.4
  • 14
    • 73649136810 scopus 로고    scopus 로고
    • The zinc-responsive regulator Zur controls expression of the coelibactin gene cluster in Streptomyces coelicolor
    • Kallifidas D, et al. (2010) The zinc-responsive regulator Zur controls expression of the coelibactin gene cluster in Streptomyces coelicolor. J Bacteriol 192:608-611.
    • (2010) J Bacteriol , vol.192 , pp. 608-611
    • Kallifidas, D.1
  • 15
    • 48349136542 scopus 로고    scopus 로고
    • The Zur of Xanthomonas campestris functions as a repressor and an activator of putative zinc homeostasis genes via recognizing two distinct sequences within its target promoters
    • Huang DL, et al. (2008) The Zur of Xanthomonas campestris functions as a repressor and an activator of putative zinc homeostasis genes via recognizing two distinct sequences within its target promoters. Nucleic Acids Res 36:4295-4309.
    • (2008) Nucleic Acids Res , vol.36 , pp. 4295-4309
    • Huang, D.L.1
  • 16
    • 34248669001 scopus 로고    scopus 로고
    • Functional specialization within the fur family of metalloregulators
    • Lee JW, Helmann JD (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.D.2
  • 18
    • 0344321893 scopus 로고    scopus 로고
    • Architecture of a protein central to iron homeostasis: Crystal structure and spectroscopic analysis of the ferric uptake regulator
    • DOI 10.1046/j.1365-2958.2003.03337.x
    • Pohl E, et al. (2003) Architecture of a protein central to iron homeostasis: Crystal structure and spectroscopic analysis of the ferric uptake regulator. Mol Microbiol 47:903-915. (Pubitemid 36232790)
    • (2003) Molecular Microbiology , vol.47 , Issue.4 , pp. 903-915
    • Pohl, E.1    Haller, J.C.2    Mijovilovich, A.3    Meyer-Klaucke, W.4    Garman, E.5    Vasil, M.L.6
  • 19
    • 65949087462 scopus 로고    scopus 로고
    • Crystal structure of the Vibrio cholerae ferric uptake regulator (Fur) reveals insights into metal co-ordination
    • Sheikh MA, Taylor GL (2009) Crystal structure of the Vibrio cholerae ferric uptake regulator (Fur) reveals insights into metal co-ordination. Mol Microbiol 72:1208-1220.
    • (2009) Mol Microbiol , vol.72 , pp. 1208-1220
    • Sheikh, M.A.1    Taylor, G.L.2
  • 21
    • 67249103599 scopus 로고    scopus 로고
    • Structural basis for the specialization of Nur, a nickel-specific fur homolog, in metal sensing and DNA recognition
    • An YJ, et al. (2009) Structural basis for the specialization of Nur, a nickel-specific Fur homolog, in metal sensing and DNA recognition. Nucleic Acids Res 37:3442-3451.
    • (2009) Nucleic Acids Res , vol.37 , pp. 3442-3451
    • An, Y.J.1
  • 22
    • 67649419186 scopus 로고    scopus 로고
    • Structural characterization of the active form of PerR: Insights into the metal-induced activation of PerR and fur proteins for DNA binding
    • Jacquamet L, et al. (2009) Structural characterization of the active form of PerR: Insights into the metal-induced activation of PerR and Fur proteins for DNA binding. Mol Microbiol 73:20-31.
    • (2009) Mol Microbiol , vol.73 , pp. 20-31
    • Jacquamet, L.1
  • 23
    • 67649425407 scopus 로고    scopus 로고
    • Hydrogen peroxide sensing in Bacillus subtilis: It is all about the (metallo)regulator
    • Giedroc DP (2009) Hydrogen peroxide sensing in Bacillus subtilis: It is all about the (metallo)regulator. Mol Microbiol 73:1-4.
    • (2009) Mol Microbiol , vol.73 , pp. 1-4
    • Giedroc, D.P.1
  • 27
    • 33747722767 scopus 로고    scopus 로고
    • Biochemical characterization of the structural Zn2+ site in the Bacillus subtilis peroxide sensor PerR
    • Lee JW, Helmann JD (2006) Biochemical characterization of the structural Zn2+ site in the Bacillus subtilis peroxide sensor PerR. J Biol Chem 281:23567-23578.
    • (2006) J Biol Chem , vol.281 , pp. 23567-23578
    • Lee, J.W.1    Helmann, J.D.2
  • 28
    • 67649229862 scopus 로고    scopus 로고
    • A ZnS(4) structural zinc site in the Helicobacter pylori ferric uptake regulator
    • Vitale S, et al. (2009) A ZnS(4) structural zinc site in the Helicobacter pylori ferric uptake regulator. Biochemistry 48:5582-5591.
    • (2009) Biochemistry , vol.48 , pp. 5582-5591
    • Vitale, S.1
  • 29
    • 79951777617 scopus 로고    scopus 로고
    • The structure of the Helicobacter pylori ferric uptake regulator fur reveals three functional metal binding sites
    • 10.1111/j.1365-2958.2010.07517.x
    • Dian C, et al. (2011) The structure of the Helicobacter pylori ferric uptake regulator Fur reveals three functional metal binding sites. Mol Microbiol, 10.1111/j.1365-2958.2010.07517.x.
    • (2011) Mol Microbiol
    • Dian, C.1
  • 30
    • 0028920231 scopus 로고
    • The rpoE gene encoding the sigma e (sigma 24) heat shock sigma factor of Escherichia coli
    • Raina S, Missiakas D, Georgopoulos C (1995) The rpoE gene encoding the sigma E (sigma 24) heat shock sigma factor of Escherichia coli. EMBO J 14:1043-1055.
    • (1995) EMBO J , vol.14 , pp. 1043-1055
    • Raina, S.1    Missiakas, D.2    Georgopoulos, C.3
  • 31
    • 0028907529 scopus 로고
    • RpoE, the gene encoding the second heat-shock sigma factor, sigma E, in Escherichia coli
    • Rouvière PE, et al. (1995) rpoE, the gene encoding the second heat-shock sigma factor, sigma E, in Escherichia coli. EMBO J 14:1032-1042.
    • (1995) EMBO J , vol.14 , pp. 1032-1042
    • Rouvière, P.E.1
  • 32
    • 0024727149 scopus 로고
    • Identification of the sigma e subunit of Escherichia coli RNA polymerase: A second alternate sigma factor involved in high-temperature gene expression
    • Erickson JW, Gross CA (1989) Identification of the sigma E subunit of Escherichia coli RNA polymerase: a second alternate sigma factor involved in high-temperature gene expression. Genes Dev 3:1462-1471.
    • (1989) Genes Dev , vol.3 , pp. 1462-1471
    • Erickson, J.W.1    Gross, C.A.2
  • 33
    • 0036198859 scopus 로고    scopus 로고
    • 2) levels in fission yeast Schizosaccharomyces pombe
    • 2) levels in fission yeast Schizosaccharomyces pombe. Mol Biol Cell 13:805-816.
    • (2002) Mol Biol Cell , vol.13 , pp. 805-816
    • Quinn, J.1
  • 34
    • 51749088801 scopus 로고    scopus 로고
    • Differential control of Zap1-regulated genes in response to zinc deficiency in Saccharomyces cerevisiae
    • Wu CY, et al. (2008) Differential control of Zap1-regulated genes in response to zinc deficiency in Saccharomyces cerevisiae. BMC Genomics 9:370.
    • (2008) BMC Genomics , vol.9 , pp. 370
    • Wu, C.Y.1
  • 35
    • 77949885386 scopus 로고    scopus 로고
    • Nutritional immunity beyond iron: A role for manganese and zinc
    • Kehl-Fie TE, Skaar EP (2010) Nutritional immunity beyond iron: A role for manganese and zinc. Curr Opin Chem Biol 14:218-224.
    • (2010) Curr Opin Chem Biol , vol.14 , pp. 218-224
    • Kehl-Fie, T.E.1    Skaar, E.P.2
  • 38
    • 0024327340 scopus 로고
    • Intergeneric conjugation between Escherichia coli and Streptomyces species
    • Mazodier P, Petter R, Thompson C (1989) Intergeneric conjugation between Escherichia coli and Streptomyces species. J Bacteriol 171:3583-3585. (Pubitemid 19145722)
    • (1989) Journal of Bacteriology , vol.171 , Issue.6 , pp. 3583-3585
    • Mazodier, P.1    Petter, R.2    Thompson, C.3
  • 39
    • 0030745896 scopus 로고    scopus 로고
    • + channel (SKC1): Oligomeric stoichiometry and stability
    • + channel (SKC1): Oligomeric stoichiometry and stability. Biochemistry 36:10343-10352.
    • (1997) Biochemistry , vol.36 , pp. 10343-10352
    • Cortes, D.M.1    Perozo, E.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.