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Volumn 5, Issue 4, 2013, Pages 352-362

Co(ii)-detection does not follow Kco(ii) gradient: Channelling in Co(ii)-sensing

Author keywords

[No Author keywords available]

Indexed keywords

BIOSYNTHETIC PATHWAY; CYANOBACTERIUM; FLUORESCENCE ANISOTROPY; SEQUENCE SIMILARITY; SITE DIRECTED MUTAGENESIS; TETRAPYRROLES; TRANSCRIPTIONAL ACTIVATIONS; TRANSCRIPTIONAL ACTIVATORS;

EID: 84879585026     PISSN: 17565901     EISSN: 1756591X     Source Type: Journal    
DOI: 10.1039/c3mt20241k     Document Type: Article
Times cited : (13)

References (40)
  • 1
    • 57649207910 scopus 로고    scopus 로고
    • How do bacterial cells ensure that metalloproteins get the correct metal?
    • K. J. Waldron N. J. Robinson How do bacterial cells ensure that metalloproteins get the correct metal? Nat. Rev. Microbiol. 2009 7 25 35
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 25-35
    • Waldron, K.J.1    Robinson, N.J.2
  • 2
    • 34547229278 scopus 로고    scopus 로고
    • Metal sensor proteins: Nature's metalloregulated allosteric switches
    • D. P. Giedroc A. I. Arunkumar Metal sensor proteins: nature's metalloregulated allosteric switches Dalton Trans. 2007 3107 3120
    • (2007) Dalton Trans. , pp. 3107-3120
    • Giedroc, D.P.1    Arunkumar, A.I.2
  • 3
    • 34248669001 scopus 로고    scopus 로고
    • Functional specialization within the fur family of metalloregulators
    • J. W. Lee J. D. Helmann Functional specialization within the Fur family of metalloregulators Biometals 2007 20 485 499
    • (2007) Biometals , vol.20 , pp. 485-499
    • Lee, J.W.1    Helmann, J.D.2
  • 5
    • 77951999593 scopus 로고    scopus 로고
    • Coordinating intracellular nickel-metal-site structure-function relationships and the NikR and RcnR repressors
    • J. S. Iwig P. T. Chivers Coordinating intracellular nickel-metal-site structure-function relationships and the NikR and RcnR repressors Nat. Prod. Rep. 2010 27 658 667
    • (2010) Nat. Prod. Rep. , vol.27 , pp. 658-667
    • Iwig, J.S.1    Chivers, P.T.2
  • 7
    • 77952000337 scopus 로고    scopus 로고
    • Bacterial metal-sensing proteins exemplified by ArsR-SmtB family repressors
    • D. Osman J. S. Cavet Bacterial metal-sensing proteins exemplified by ArsR-SmtB family repressors Nat. Prod. Rep. 2010 27 668 680
    • (2010) Nat. Prod. Rep. , vol.27 , pp. 668-680
    • Osman, D.1    Cavet, J.S.2
  • 9
    • 0031002899 scopus 로고    scopus 로고
    • CopY is a copper-inducible repressor of the Enterococcus hirae copper ATPases
    • D. Strausak M. Solioz CopY is a copper-inducible repressor of the Enterococcus hirae copper ATPases J. Biol. Chem. 1997 272 8932 8936
    • (1997) J. Biol. Chem. , vol.272 , pp. 8932-8936
    • Strausak, D.1    Solioz, M.2
  • 11
    • 27644580799 scopus 로고    scopus 로고
    • Understanding how cells allocate metals using metal sensors and metallochaperones
    • S. Tottey D. R. Harvie N. J. Robinson Understanding how cells allocate metals using metal sensors and metallochaperones Acc. Chem. Res. 2005 38 775 783
    • (2005) Acc. Chem. Res. , vol.38 , pp. 775-783
    • Tottey, S.1    Harvie, D.R.2    Robinson, N.J.3
  • 12
    • 0033520471 scopus 로고    scopus 로고
    • Cobalt-dependent transcriptional switching by a dual-effector MerR-like protein regulates a cobalt-exporting variant CPx-type ATPase
    • J. C. Rutherford J. S. Cavet N. J. Robinson Cobalt-dependent transcriptional switching by a dual-effector MerR-like protein regulates a cobalt-exporting variant CPx-type ATPase J. Biol. Chem. 1999 274 25827 25832
    • (1999) J. Biol. Chem. , vol.274 , pp. 25827-25832
    • Rutherford, J.C.1    Cavet, J.S.2    Robinson, N.J.3
  • 13
    • 0026530492 scopus 로고
    • Allosteric underwinding of DNA is a critical step in positive control of transcription by Hg-MerR
    • A. Z. Ansari M. L. Chael T. V. O'Halloran Allosteric underwinding of DNA is a critical step in positive control of transcription by Hg-MerR Nature 1992 355 87 89
    • (1992) Nature , vol.355 , pp. 87-89
    • Ansari, A.Z.1    Chael, M.L.2    O'Halloran, T.V.3
  • 14
    • 0027535743 scopus 로고
    • Metalloregulated expression of the ars operon
    • J. Wu B. P. Rosen Metalloregulated expression of the ars operon J. Biol. Chem. 1993 268 52 58
    • (1993) J. Biol. Chem. , vol.268 , pp. 52-58
    • Wu, J.1    Rosen, B.P.2
  • 15
    • 0032168014 scopus 로고    scopus 로고
    • An SmtB-like repressor from Synechocystis PCC 6803 regulates a zinc exporter
    • C. Thelwell N. J. Robinson J. S. Cavet An SmtB-like repressor from Synechocystis PCC 6803 regulates a zinc exporter Proc. Natl. Acad. Sci. U. S. A. 1998 95 10728 10733
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 10728-10733
    • Thelwell, C.1    Robinson, N.J.2    Cavet, J.S.3
  • 16
    • 33748666848 scopus 로고    scopus 로고
    • Nickel homeostasis in Escherichia coli-The rcnR-rcnA efflux pathway and its linkage to NikR function
    • J. S. Iwig J. L. Rowe P. T. Chivers Nickel homeostasis in Escherichia coli-the rcnR-rcnA efflux pathway and its linkage to NikR function Mol. Microbiol. 2006 62 252 262
    • (2006) Mol. Microbiol. , vol.62 , pp. 252-262
    • Iwig, J.S.1    Rowe, J.L.2    Chivers, P.T.3
  • 17
    • 84859510164 scopus 로고    scopus 로고
    • Cytosolic Ni(ii) sensor in cyanobacterium: Nickel detection follows nickel affinity across four families of metal sensors
    • A. W. Foster C. J. Patterson R. Pernil C. R. Hess N. J. Robinson Cytosolic Ni(ii) sensor in cyanobacterium: nickel detection follows nickel affinity across four families of metal sensors J. Biol. Chem. 2012 287 12142 12151
    • (2012) J. Biol. Chem. , vol.287 , pp. 12142-12151
    • Foster, A.W.1    Patterson, C.J.2    Pernil, R.3    Hess, C.R.4    Robinson, N.J.5
  • 18
    • 0031798662 scopus 로고    scopus 로고
    • The ZnuABC high-affinity zinc uptake system and its regulator Zur in Escherichia coli
    • S. I. Patzer K. Hantke The ZnuABC high-affinity zinc uptake system and its regulator Zur in Escherichia coli Mol. Microbiol. 1998 28 1199 1210
    • (1998) Mol. Microbiol. , vol.28 , pp. 1199-1210
    • Patzer, S.I.1    Hantke, K.2
  • 20
    • 0026063522 scopus 로고
    • Dihydroorotase from Escherichia coli. Substitution of Co(ii) for the active site Zn(ii)
    • D. C. Brown K. D. Collins Dihydroorotase from Escherichia coli. Substitution of Co(ii) for the active site Zn(ii) J. Biol. Chem. 1991 266 1597 1604
    • (1991) J. Biol. Chem. , vol.266 , pp. 1597-1604
    • Brown, D.C.1    Collins, K.D.2
  • 27
    • 0027500239 scopus 로고
    • Construction and characterization of a mercury-independent MerR activator (MerRAC): Transcriptional activation in the absence of Hg(ii) is accompanied by DNA distortion
    • J. Parkhill A. Z. Ansari J. G. Wright N. L. Brown T. V. O'Halloran Construction and characterization of a mercury-independent MerR activator (MerRAC): transcriptional activation in the absence of Hg(ii) is accompanied by DNA distortion EMBO J. 1993 12 413 421
    • (1993) EMBO J. , vol.12 , pp. 413-421
    • Parkhill, J.1    Ansari, A.Z.2    Wright, J.G.3    Brown, N.L.4    O'Halloran, T.V.5
  • 28
    • 35648957195 scopus 로고    scopus 로고
    • The CbiB protein of Salmonella enterica is an integral membrane protein involved in the last step of the de novo corrin ring biosynthetic pathway
    • C. L. Zayas K. Claas J. C. Escalante-Semerena The CbiB protein of Salmonella enterica is an integral membrane protein involved in the last step of the de novo corrin ring biosynthetic pathway J. Bacteriol. 2007 189 7697 7708
    • (2007) J. Bacteriol. , vol.189 , pp. 7697-7708
    • Zayas, C.L.1    Claas, K.2    Escalante-Semerena, J.C.3
  • 30
    • 36048943681 scopus 로고    scopus 로고
    • Membrane proteins from the cyanobacterium Synechocystis sp. PCC 6803 interacting with thioredoxin
    • A. Mata-Cabana F. J. Florencio M. Lindahl Membrane proteins from the cyanobacterium Synechocystis sp. PCC 6803 interacting with thioredoxin Proteomics 2007 7 3953 3963
    • (2007) Proteomics , vol.7 , pp. 3953-3963
    • Mata-Cabana, A.1    Florencio, F.J.2    Lindahl, M.3
  • 33
    • 33748748114 scopus 로고    scopus 로고
    • Mutagenesis of hydrogenase accessory genes of Synechocystis sp. PCC 6803, additional homologues of hypA and hypB are not active in hydrogenase maturation
    • D. Hoffmann K. Gutekunst M. Klissenbauer R. Schulz-Friedrich J. Appel Mutagenesis of hydrogenase accessory genes of Synechocystis sp. PCC 6803, additional homologues of hypA and hypB are not active in hydrogenase maturation FEBS J. 2006 273 4516 4527
    • (2006) FEBS J. , vol.273 , pp. 4516-4527
    • Hoffmann, D.1    Gutekunst, K.2    Klissenbauer, M.3    Schulz-Friedrich, R.4    Appel, J.5
  • 34
    • 0027497266 scopus 로고
    • The Escherichia coli cysG gene encodes the multifunctional protein, siroheme synthase
    • J. B. Spencer N. J. Stolwich C. A. Roessner I. Scott The Escherichia coli cysG gene encodes the multifunctional protein, siroheme synthase FEBS J. 1993 335 57 60
    • (1993) FEBS J. , vol.335 , pp. 57-60
    • Spencer, J.B.1    Stolwich, N.J.2    Roessner, C.A.3    Scott, I.4
  • 35
    • 0032189235 scopus 로고    scopus 로고
    • 12) biosynthesis: Identification and characterization of a Bacillus megaterium cobI operon
    • 12) biosynthesis: identification and characterization of a Bacillus megaterium cobI operon Biochem. J. 1998 335 159 166
    • (1998) Biochem. J. , vol.335 , pp. 159-166
    • Raux, E.1    Lanois, A.2    Warren, M.J.3    Rambach, A.4    Thermes, C.5
  • 38
    • 0027434568 scopus 로고
    • Isolation of a prokaryotic metallothionein locus and analysis of transcriptional control by trace metal ions
    • J. W. Huckle A. P. Morby J. S. Turner N. J. Robinson Isolation of a prokaryotic metallothionein locus and analysis of transcriptional control by trace metal ions Mol. Microbiol. 1993 7 177 187
    • (1993) Mol. Microbiol. , vol.7 , pp. 177-187
    • Huckle, J.W.1    Morby, A.P.2    Turner, J.S.3    Robinson, N.J.4
  • 40
    • 0027247583 scopus 로고
    • SmtB is a metal-dependent repressor of the cyanobacterial metallothionein gene smtA: Identification of a Zn inhibited DNA-protein complex
    • A. P. Morby J. S. Turner J. W. Huckle N. J. Robinson SmtB is a metal-dependent repressor of the cyanobacterial metallothionein gene smtA: identification of a Zn inhibited DNA-protein complex Nucleic Acids Res. 1993 21 921 925
    • (1993) Nucleic Acids Res. , vol.21 , pp. 921-925
    • Morby, A.P.1    Turner, J.S.2    Huckle, J.W.3    Robinson, N.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.