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Volumn 288, Issue 48, 2013, Pages 34514-34528

WhiB7, an Fe-S-dependent transcription factor that activates species-specific repertoires of drug resistance determinants in actinobacteria

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTIC RESISTANCE; HETEROLOGOUS EXPRESSION; IRON-SULFUR CLUSTERS; MULTIDRUG TRANSPORTERS; MYCOBACTERIUM SMEGMATIS; SECONDARY METABOLISM; STREPTOMYCES LIVIDANS; TRANSCRIPTIONAL ACTIVATIONS;

EID: 84888986254     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.516385     Document Type: Article
Times cited : (47)

References (83)
  • 1
    • 33746908131 scopus 로고    scopus 로고
    • The evolution of development in Streptomyces analysed by genome comparisons
    • Chater, K. F., and Chandra, G. (2006) The evolution of development in Streptomyces analysed by genome comparisons. FEMS Microbiol. Rev. 30, 651-672
    • (2006) FEMS Microbiol. Rev , vol.30 , pp. 651-672
    • Chater, K.F.1    Chandra, G.2
  • 3
    • 19644393308 scopus 로고    scopus 로고
    • Bioactive microbial metabolites
    • Bérdy, J. (2005) Bioactive microbial metabolites. J. Antibiot. 58, 1-26
    • (2005) J. Antibiot , vol.58 , pp. 1-26
    • Bérdy, J.1
  • 6
    • 0034528573 scopus 로고    scopus 로고
    • In vivo veritas: The search for TB drug targets goes live
    • McKinney, J. D. (2000) In vivo veritas: the search for TB drug targets goes live. Nat. Med. 6, 1330-1333
    • (2000) Nat. Med , vol.6 , pp. 1330-1333
    • McKinney, J.D.1
  • 8
    • 84868146046 scopus 로고    scopus 로고
    • WhiB7, a transcriptional activator that coordinates physiology with intrinsic drug resistance in Mycobacterium tuberculosis
    • Burian, J., Ramón-García, S., Howes, C. G., and Thompson, C. J. (2012) WhiB7, a transcriptional activator that coordinates physiology with intrinsic drug resistance in Mycobacterium tuberculosis. Expert Rev. Antiinfect. Ther. 10, 1037-1047
    • (2012) Expert Rev. Antiinfect. Ther , vol.10 , pp. 1037-1047
    • Burian, J.1    Ramón-García, S.2    Howes, C.G.3    Thompson, C.J.4
  • 9
    • 84855286330 scopus 로고    scopus 로고
    • The mycobacterial transcriptional regulator whiB7 gene links redox homeostasis and intrinsic antibiotic resistance
    • Burian, J., Ramón-García, S., Sweet, G., Gómez-Velasco, A., Av-Gay, Y., and Thompson, C. J. (2012) The mycobacterial transcriptional regulator whiB7 gene links redox homeostasis and intrinsic antibiotic resistance. J. Biol. Chem. 287, 299-310
    • (2012) J. Biol. Chem , vol.287 , pp. 299-310
    • Burian, J.1    Ramón-García, S.2    Sweet, G.3    Gómez-Velasco, A.4    Av-Gay, Y.5    Thompson, C.J.6
  • 10
    • 33746904362 scopus 로고    scopus 로고
    • Differential gene expression in response to exposure to antimycobacterial agents and other stress conditions among seven Mycobacterium tuberculosis whiB-like genes
    • Geiman, D. E., Raghunand, T. R., Agarwal, N., and Bishai, W. R. (2006) Differential gene expression in response to exposure to antimycobacterial agents and other stress conditions among seven Mycobacterium tuberculosis whiB-like genes. Antimicrob. Agents Chemother. 50, 2836-2841
    • (2006) Antimicrob. Agents Chemother , vol.50 , pp. 2836-2841
    • Geiman, D.E.1    Raghunand, T.R.2    Agarwal, N.3    Bishai, W.R.4
  • 11
    • 77957671514 scopus 로고    scopus 로고
    • Functional genetic diversity among Mycobacterium tuberculosis complex clinical isolates: Delineation of conserved core and lineage-specific transcriptomes during intracellular survival
    • Homolka, S., Niemann, S., Russell, D. G., and Rohde, K. H. (2010) Functional genetic diversity among Mycobacterium tuberculosis complex clinical isolates: delineation of conserved core and lineage-specific transcriptomes during intracellular survival. PLoS Pathog. 6, e1000988
    • (2010) PLoS Pathog , vol.6
    • Homolka, S.1    Niemann, S.2    Russell, D.G.3    Rohde, K.H.4
  • 12
    • 84864050604 scopus 로고    scopus 로고
    • Gene expression of Mycobacterium tuberculosis putative transcription factors whiB1-7 in redox environments
    • Larsson, C., Luna, B., Ammerman, N. C., Maiga, M., Agarwal, N., and Bishai, W. R. (2012) Gene expression of Mycobacterium tuberculosis putative transcription factors whiB1-7 in redox environments. PLoS One 7, e37516
    • (2012) PLoS One , vol.7
    • Larsson, C.1    Luna, B.2    Ammerman, N.C.3    Maiga, M.4    Agarwal, N.5    Bishai, W.R.6
  • 15
    • 73949102884 scopus 로고    scopus 로고
    • Overexpression of the chromosomally encoded aminoglycoside acetyltransferase eis confers kanamycin resistance in Mycobacterium tuberculosis
    • Zaunbrecher, M. A., Sikes, R. D., Jr., Metchock, B., Shinnick, T. M., and Posey, J. E. (2009) Overexpression of the chromosomally encoded aminoglycoside acetyltransferase eis confers kanamycin resistance in Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. U.S.A. 106, 20004-20009
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 20004-20009
    • Zaunbrecher, M.A.1    Sikes Jr., R.D.2    Metchock, B.3    Shinnick, T.M.4    Posey, J.E.5
  • 18
    • 0033983745 scopus 로고    scopus 로고
    • Multiple paralogous genes related to the Streptomyces coelicolor developmental regulatory gene whiB are present in Streptomyces and other actinomycetes
    • Soliveri, J. A., Gomez, J., Bishai, W. R., and Chater, K. F. (2000) Multiple paralogous genes related to the Streptomyces coelicolor developmental regulatory gene whiB are present in Streptomyces and other actinomycetes. Microbiology 146, 333-343
    • (2000) Microbiology , vol.146 , pp. 333-343
    • Soliveri, J.A.1    Gomez, J.2    Bishai, W.R.3    Chater, K.F.4
  • 19
    • 14844290234 scopus 로고    scopus 로고
    • Evidence that the Streptomyces developmental protein WhiD, a member of the WhiB family, binds a [4Fe-4S] cluster
    • Jakimowicz, P., Cheesman, M. R., Bishai, W. R., Chater, K. F., Thomson, A. J., and Buttner, M. J. (2005) Evidence that the Streptomyces developmental protein WhiD, a member of the WhiB family, binds a [4Fe-4S] cluster. J. Biol. Chem. 280, 8309-8315
    • (2005) J. Biol. Chem , vol.280 , pp. 8309-8315
    • Jakimowicz, P.1    Cheesman, M.R.2    Bishai, W.R.3    Chater, K.F.4    Thomson, A.J.5    Buttner, M.J.6
  • 20
    • 0032190230 scopus 로고    scopus 로고
    • AT-hook motifs identified in a wide variety of DNA-binding proteins
    • Aravind, L., and Landsman, D. (1998) AT-hook motifs identified in a wide variety of DNA-binding proteins. Nucleic Acids Res. 26, 4413-4421
    • (1998) Nucleic Acids Res , vol.26 , pp. 4413-4421
    • Aravind, L.1    Landsman, D.2
  • 21
    • 0035904395 scopus 로고    scopus 로고
    • Molecular biology of HMGA proteins: Hubs of nuclear function
    • Reeves, R. (2001) Molecular biology of HMGA proteins: hubs of nuclear function. Gene 277, 63-81
    • (2001) Gene , vol.277 , pp. 63-81
    • Reeves, R.1
  • 22
    • 77954835360 scopus 로고    scopus 로고
    • Insights into the function of the WhiB-like protein of mycobacteriophage TM4 - A transcriptional inhibitor of WhiB2
    • Rybniker, J., Nowag, A., van Gumpel, E., Nissen, N., Robinson, N., Plum, G., and Hartmann, P. (2010) Insights into the function of the WhiB-like protein of mycobacteriophage TM4-a transcriptional inhibitor of WhiB2. Mol. Microbiol. 77, 642-657
    • (2010) Mol. Microbiol , vol.77 , pp. 642-657
    • Rybniker, J.1    Nowag, A.2    Van Gumpel, E.3    Nissen, N.4    Robinson, N.5    Plum, G.6    Hartmann, P.7
  • 23
    • 57649186810 scopus 로고    scopus 로고
    • Studies on structural and functional divergence among seven WhiB proteins of Mycobacterium tuberculosis H37Rv
    • Alam, M. S., Garg, S. K., and Agrawal, P. (2009) Studies on structural and functional divergence among seven WhiB proteins of Mycobacterium tuberculosis H37Rv. FEBS J. 276, 76-93
    • (2009) FEBS J. , vol.276 , pp. 76-93
    • Alam, M.S.1    Garg, S.K.2    Agrawal, P.3
  • 25
    • 70149116303 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis WhiB3 maintains redox homeostasis by regulating virulence lipid anabolism to modulate macrophage response
    • Singh, A., Crossman, D. K., Mai, D., Guidry, L., Voskuil, M. I., Renfrow, M. B., and Steyn, A. J. (2009) Mycobacterium tuberculosis WhiB3 maintains redox homeostasis by regulating virulence lipid anabolism to modulate macrophage response. PLoS Pathog. 5, e1000545
    • (2009) PLoS Pathog , vol.5
    • Singh, A.1    Crossman, D.K.2    Mai, D.3    Guidry, L.4    Voskuil, M.I.5    Renfrow, M.B.6    Steyn, A.J.7
  • 26
    • 33846942978 scopus 로고    scopus 로고
    • Molecular function of WhiB4/Rv3681c of Mycobacterium tuberculosis H37Rv: A [4Fe-4S] cluster co-ordinating protein disulphide reductase
    • Alam, M. S., Garg, S. K., and Agrawal, P. (2007) Molecular function of WhiB4/Rv3681c of Mycobacterium tuberculosis H37Rv: a [4Fe-4S] cluster co-ordinating protein disulphide reductase. Mol. Microbiol. 63, 1414 -1431
    • (2007) Mol. Microbiol , vol.63 , pp. 1414-1431
    • Alam, M.S.1    Garg, S.K.2    Agrawal, P.3
  • 28
    • 33748780411 scopus 로고    scopus 로고
    • Mapping essential domains of Mycobacterium smegmatis WhmD: Insights into WhiB structure and function
    • Raghunand, T. R., and Bishai, W. R. (2006) Mapping essential domains of Mycobacterium smegmatis WhmD: insights into WhiB structure and function. J. Bacteriol. 188, 6966-6976
    • (2006) J. Bacteriol , vol.188 , pp. 6966-6976
    • Raghunand, T.R.1    Bishai, W.R.2
  • 29
    • 79955755909 scopus 로고    scopus 로고
    • The actinobacteria-specific gene wblA controls major developmental transitions in Streptomyces coelicolor A3(2)
    • Fowler-Goldsworthy, K., Gust, B., Mouz, S., Chandra, G., Findlay, K. C., and Chater, K. F. (2011) The actinobacteria-specific gene wblA controls major developmental transitions in Streptomyces coelicolor A3(2). Microbiology 157, 1312-1328
    • (2011) Microbiology , vol.157 , pp. 1312-1328
    • Fowler-Goldsworthy, K.1    Gust, B.2    Mouz, S.3    Chandra, G.4    Findlay, K.C.5    Chater, K.F.6
  • 30
    • 84863849311 scopus 로고    scopus 로고
    • WhiB2/Rv3260c, a cell division-associated protein of Mycobacterium tuberculosis H37Rv, has properties of a chaperone
    • Konar, M., Alam, M. S., Arora, C., and Agrawal, P. (2012) WhiB2/Rv3260c, a cell division-associated protein of Mycobacterium tuberculosis H37Rv, has properties of a chaperone. FEBS J. 279, 2781-2792
    • (2012) FEBS J. , vol.279 , pp. 2781-2792
    • Konar, M.1    Alam, M.S.2    Arora, C.3    Agrawal, P.4
  • 31
    • 84863402400 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis WhiB1 represses transcription of the essential chaperonin GroEL2
    • Stapleton, M. R., Smith, L. J., Hunt, D. M., Buxton, R. S., and Green, J. (2012) Mycobacterium tuberculosis WhiB1 represses transcription of the essential chaperonin GroEL2. Tuberculosis 92, 328-332
    • (2012) Tuberculosis , vol.92 , pp. 328-332
    • Stapleton, M.R.1    Smith, L.J.2    Hunt, D.M.3    Buxton, R.S.4    Green, J.5
  • 33
    • 84889059036 scopus 로고    scopus 로고
    • The mycobacterial antibiotic resistance determinant WhiB7 acts as a transcriptional activator by binding the primary σ factor SigA (RpoV)
    • 10.1093/nar/gkt751
    • Burian, J., Yim, G., Hsing, M., Axerio-Cilies, P., Cherkasov, A., Spiegelman, G. B., and Thompson, C. J. (2013) The mycobacterial antibiotic resistance determinant WhiB7 acts as a transcriptional activator by binding the primary σ factor SigA (RpoV). Nucleic Acids Res. 10.1093/nar/gkt751
    • (2013) Nucleic Acids Res
    • Burian, J.1    Yim, G.2    Hsing, M.3    Axerio-Cilies, P.4    Cherkasov, A.5    Spiegelman, G.B.6    Thompson, C.J.7
  • 34
  • 36
    • 0002935655 scopus 로고
    • The bialaphos biosynthetic genes of Streptomyces hygroscopicus: Molecular cloning of the gene cluster
    • Murakami, T., Anzai, H., Imai, S., Satoh, A., Nagaoka, K., and Thompson, C. J. (1986) The bialaphos biosynthetic genes of Streptomyces hygroscopicus: molecular cloning of the gene cluster. Mol. Gen. Genet. 205, 42-50
    • (1986) Mol. Gen. Genet , vol.205 , pp. 42-50
    • Murakami, T.1    Anzai, H.2    Imai, S.3    Satoh, A.4    Nagaoka, K.5    Thompson, C.J.6
  • 39
    • 0032725568 scopus 로고    scopus 로고
    • Functional assignment of the ORF2-iscS-iscU-iscA-hscB-hscA-fdx-ORF3 gene cluster involved in the assembly of Fe-S clusters in Escherichia coli
    • Takahashi, Y., and Nakamura, M. (1999) Functional assignment of the ORF2-iscS-iscU-iscA-hscB-hscA-fdx-ORF3 gene cluster involved in the assembly of Fe-S clusters in Escherichia coli. J. Biochem. 126, 917-926
    • (1999) J. Biochem , vol.126 , pp. 917-926
    • Takahashi, Y.1    Nakamura, M.2
  • 40
    • 0036774617 scopus 로고    scopus 로고
    • Specialized transduction: An efficient method for generating marked and unmarked targeted gene disruptions in Mycobacterium tuberculosis, M bovis BCG, and M. smegmatis
    • Bardarov, S., Bardarov, S., Jr., Pavelka, M. S., Jr., Sambandamurthy, V., Larsen, M., Tufariello, J., Chan, J., Hatfull, G., and Jacobs, W. R., Jr. (2002) Specialized transduction: an efficient method for generating marked and unmarked targeted gene disruptions in Mycobacterium tuberculosis, M. bovis BCG, and M. smegmatis. Microbiology 148, 3007-3017
    • (2002) Microbiology , vol.148 , pp. 3007-3017
    • Bardarov, S.1    Bardarov Jr., S.2    Pavelka Jr., M.S.3    Sambandamurthy, V.4    Larsen, M.5    Tufariello, J.6    Chan, J.7    Hatfull, G.8    Jacobs Jr., W.R.9
  • 42
    • 0025081151 scopus 로고
    • Isolation and characterization of efficient plasmid transformation mutants of Mycobacterium smegmatis
    • Snapper, S. B., Melton, R. E., Mustafa, S., Kieser, T., and Jacobs, W. R., Jr. (1990) Isolation and characterization of efficient plasmid transformation mutants of Mycobacterium smegmatis. Mol. Microbiol. 4, 1911-1919
    • (1990) Mol. Microbiol , vol.4 , pp. 1911-1919
    • Snapper, S.B.1    Melton, R.E.2    Mustafa, S.3    Kieser, T.4    Jacobs Jr., W.R.5
  • 43
    • 20444506446 scopus 로고    scopus 로고
    • Catabolism of benzoate and phthalate in Rhodococcus sp. strain RHA1: Redundancies and convergence
    • Patrauchan, M. A., Florizone, C., Dosanjh, M., Mohn, W. W., Davies, J., and Eltis, L. D. (2005) Catabolism of benzoate and phthalate in Rhodococcus sp. strain RHA1: redundancies and convergence. J. Bacteriol. 187, 4050-4063
    • (2005) J. Bacteriol , vol.187 , pp. 4050-4063
    • Patrauchan, M.A.1    Florizone, C.2    Dosanjh, M.3    Mohn, W.W.4    Davies, J.5    Eltis, L.D.6
  • 45
    • 0030591739 scopus 로고    scopus 로고
    • Construction of a family of Mycobacterium/Escherichia coli shuttle vectors derived from pAL5000 and pACYC184: Their use for cloning an antibiotic-resistance gene from Mycobacterium fortuitum
    • Aínsa, J. A., Martín, C., Cabeza, M., De la Cruz, F., and Mendiola, M. V. (1996) Construction of a family of Mycobacterium/Escherichia coli shuttle vectors derived from pAL5000 and pACYC184: their use for cloning an antibiotic-resistance gene from Mycobacterium fortuitum. Gene 176, 23-26
    • (1996) Gene , vol.176 , pp. 23-26
    • Aínsa, J.A.1    Martín, C.2    Cabeza, M.3    De La Cruz, F.4    Mendiola, M.V.5
  • 46
    • 4644233997 scopus 로고    scopus 로고
    • Isolation and characterization of a rolling-circle-type plasmid from Rhodococcus erythropolis and application of the plasmid to multiple-recombinant- protein expression
    • Nakashima, N., and Tamura, T. (2004) Isolation and characterization of a rolling-circle-type plasmid from Rhodococcus erythropolis and application of the plasmid to multiple-recombinant-protein expression. Appl. Environ. Microbiol. 70, 5557-5568
    • (2004) Appl. Environ. Microbiol , vol.70 , pp. 5557-5568
    • Nakashima, N.1    Tamura, T.2
  • 47
    • 34248679167 scopus 로고    scopus 로고
    • Tricine-SDS-PAGE
    • Schägger, H. (2006) Tricine-SDS-PAGE. Nat. Protoc. 1, 16-22
    • (2006) Nat. Protoc , vol.1 , pp. 16-22
    • Schägger, H.1
  • 48
    • 0017413173 scopus 로고
    • Inhibition of methylene blue formation during determination of the acid-labile sulfide of iron-sulfur protein samples containing dithionite
    • Chen, J. S., and Mortenson, L. E. (1977) Inhibition of methylene blue formation during determination of the acid-labile sulfide of iron-sulfur protein samples containing dithionite. Anal. Biochem. 79, 157-165
    • (1977) Anal. Biochem , vol.79 , pp. 157-165
    • Chen, J.S.1    Mortenson, L.E.2
  • 49
    • 0015510099 scopus 로고
    • Kinetic and Mossbauer studies on the mechanism of protocatechuic acid 4,5- oxygenase
    • Zabinski, R., Münck, E., Champion, P. M., and Wood, J. M. (1972) Kinetic and Mossbauer studies on the mechanism of protocatechuic acid 4,5- oxygenase. Biochemistry 11, 3212-3219
    • (1972) Biochemistry , vol.11 , pp. 3212-3219
    • Zabinski, R.1    Münck, E.2    Champion, P.M.3    Wood, J.M.4
  • 50
    • 17444425781 scopus 로고    scopus 로고
    • Comparative evaluation of the nitrate reduction assay, the MTT test, and the resazurin microtitre assay for drug susceptibility testing of clinical isolates of Mycobacterium tuberculosis
    • Montoro, E., Lemus, D., Echemendia, M., Martin, A., Portaels, F., and Palomino, J. C. (2005) Comparative evaluation of the nitrate reduction assay, the MTT test, and the resazurin microtitre assay for drug susceptibility testing of clinical isolates of Mycobacterium tuberculosis. J. Antimicrob. Chemother. 55, 500-505
    • (2005) J. Antimicrob. Chemother , vol.55 , pp. 500-505
    • Montoro, E.1    Lemus, D.2    Echemendia, M.3    Martin, A.4    Portaels, F.5    Palomino, J.C.6
  • 51
    • 0030764158 scopus 로고    scopus 로고
    • The solution structure of an HMGI (Y)-DNA complex defines a new architectural minor groove binding motif
    • Huth, J. R., Bewley, C. A., Nissen, M. S., Evans, J. N., Reeves, R., Gronenborn, A. M., and Clore, G. M. (1997) The solution structure of an HMGI (Y)-DNA complex defines a new architectural minor groove binding motif. Nat. Struct. Biol. 4, 657-665
    • (1997) Nat. Struct. Biol , vol.4 , pp. 657-665
    • Huth, J.R.1    Bewley, C.A.2    Nissen, M.S.3    Evans, J.N.4    Reeves, R.5    Gronenborn, A.M.6    Clore, G.M.7
  • 52
    • 0028989950 scopus 로고
    • 1H and 13C NMR assignments and molecular modelling of a minor groove DNA-binding peptide from the HMG-I protein
    • Evans, J. N., Zajicek, J., Nissen, M. S., Munske, G., Smith, V., and Reeves, R. (1995) 1H and 13C NMR assignments and molecular modelling of a minor groove DNA-binding peptide from the HMG-I protein. Int. J. Pept. Protein Res. 45, 554-560
    • (1995) Int. J. Pept. Protein Res , vol.45 , pp. 554-560
    • Evans, J.N.1    Zajicek, J.2    Nissen, M.S.3    Munske, G.4    Smith, V.5    Reeves, R.6
  • 53
    • 84863629218 scopus 로고    scopus 로고
    • Structurefunction relationships of the Mycobacterium tuberculosis transcription factor WhiB1
    • Smith, L. J., Stapleton, M. R., Buxton, R. S., and Green, J. (2012) Structurefunction relationships of the Mycobacterium tuberculosis transcription factor WhiB1. PLoS One 7, e40407
    • (2012) PLoS One , vol.7
    • Smith, L.J.1    Stapleton, M.R.2    Buxton, R.S.3    Green, J.4
  • 54
    • 84859627658 scopus 로고    scopus 로고
    • Iron-sulfur cluster proteins and microbial regulation: Implications for understanding tuberculosis
    • Saini, V., Farhana, A., Glasgow, J. N., and Steyn, A. J. (2012) Iron-sulfur cluster proteins and microbial regulation: implications for understanding tuberculosis. Curr. Opin. Chem. Biol. 16, 45-53
    • (2012) Curr. Opin. Chem. Biol , vol.16 , pp. 45-53
    • Saini, V.1    Farhana, A.2    Glasgow, J.N.3    Steyn, A.J.4
  • 58
  • 59
    • 0029152251 scopus 로고
    • Binuclear [2Fe-2S] clusters in the Escherichia coli SoxR protein and role of the metal centers in transcription
    • Hidalgo, E., Bollinger, J. M., Jr., Bradley, T. M., Walsh, C. T., and Demple, B. (1995) Binuclear [2Fe-2S] clusters in the Escherichia coli SoxR protein and role of the metal centers in transcription. J. Biol. Chem. 270, 20908-20914
    • (1995) J. Biol. Chem , vol.270 , pp. 20908-20914
    • Hidalgo, E.1    Bollinger Jr., J.M.2    Bradley, T.M.3    Walsh, C.T.4    Demple, B.5
  • 61
    • 23844452716 scopus 로고    scopus 로고
    • Radical S-adenosylmethionine enzyme coproporphyrinogen III oxidase HemN: Functional features of the [4Fe-4S] cluster and the two bound S-adenosyl-L-methionines
    • Layer, G., Grage, K., Teschner, T., Schünemann, V., Breckau, D., Masoumi, A., Jahn, M., Heathcote, P., Trautwein, A. X., and Jahn, D. (2005) Radical S-adenosylmethionine enzyme coproporphyrinogen III oxidase HemN: functional features of the [4Fe-4S] cluster and the two bound S-adenosyl-L-methionines. J. Biol. Chem. 280, 29038-29046
    • (2005) J. Biol. Chem , vol.280 , pp. 29038-29046
    • Layer, G.1    Grage, K.2    Teschner, T.3    Schünemann, V.4    Breckau, D.5    Masoumi, A.6    Jahn, M.7    Heathcote, P.8    Trautwein, A.X.9    Jahn, D.10
  • 62
    • 0028177774 scopus 로고
    • Optical, EPR, and 1H NMR spectroscopy of serine-ligated [2Fe-2S] ferredoxins produced by site-directed mutagenesis of cysteine residues in recombinant Anabaena 7120 vegetative ferredoxin
    • Cheng, H., Xia, B., Reed, G. H., and Markley, J. L. (1994) Optical, EPR, and 1H NMR spectroscopy of serine-ligated [2Fe-2S] ferredoxins produced by site-directed mutagenesis of cysteine residues in recombinant Anabaena 7120 vegetative ferredoxin. Biochemistry 33, 3155-3164
    • (1994) Biochemistry , vol.33 , pp. 3155-3164
    • Cheng, H.1    Xia, B.2    Reed, G.H.3    Markley, J.L.4
  • 63
    • 0028848166 scopus 로고
    • A bacterial thioredoxin-like protein that is exposed to the periplasm has redox properties comparable with those of cytoplasmic thioredoxins
    • Loferer, H., Wunderlich, M., Hennecke, H., and Glockshuber, R. (1995) A bacterial thioredoxin-like protein that is exposed to the periplasm has redox properties comparable with those of cytoplasmic thioredoxins. J. Biol. Chem. 270, 26178-26183
    • (1995) J. Biol. Chem , vol.270 , pp. 26178-26183
    • Loferer, H.1    Wunderlich, M.2    Hennecke, H.3    Glockshuber, R.4
  • 64
    • 0031882182 scopus 로고    scopus 로고
    • A novel regulatory switch mediated by the FNR-like protein of Lactobacillus casei
    • Gostick, D. O., Green, J., Irvine, A. S., Gasson, M. J., and Guest, J. R. (1998) A novel regulatory switch mediated by the FNR-like protein of Lactobacillus casei. Microbiology 144, 705-717
    • (1998) Microbiology , vol.144 , pp. 705-717
    • Gostick, D.O.1    Green, J.2    Irvine, A.S.3    Gasson, M.J.4    Guest, J.R.5
  • 66
    • 0345627986 scopus 로고    scopus 로고
    • The structure of iron-sulfur proteins
    • Sticht, H., and Rösch, P. (1998) The structure of iron-sulfur proteins. Prog. Biophys. Mol. Biol. 70, 95-136
    • (1998) Prog. Biophys. Mol. Biol , vol.70 , pp. 95-136
    • Sticht, H.1    Rösch, P.2
  • 67
    • 33646427470 scopus 로고    scopus 로고
    • IscR-dependent gene expression links iron-sulphur cluster assembly to the control of O2-regulated genes in Escherichia coli
    • Giel, J. L., Rodionov, D., Liu, M., Blattner, F. R., and Kiley, P. J. (2006) IscR-dependent gene expression links iron-sulphur cluster assembly to the control of O2-regulated genes in Escherichia coli. Mol. Microbiol. 60, 1058-1075
    • (2006) Mol. Microbiol , vol.60 , pp. 1058-1075
    • Giel, J.L.1    Rodionov, D.2    Liu, M.3    Blattner, F.R.4    Kiley, P.J.5
  • 68
    • 0038352097 scopus 로고    scopus 로고
    • The role of Fe-S proteins in sensing and regulation in bacteria
    • Kiley, P. J., and Beinert, H. (2003) The role of Fe-S proteins in sensing and regulation in bacteria. Curr. Opin. Microbiol. 6, 181-185
    • (2003) Curr. Opin. Microbiol , vol.6 , pp. 181-185
    • Kiley, P.J.1    Beinert, H.2
  • 69
    • 0032739921 scopus 로고    scopus 로고
    • Direct evidence for mRNA binding and post-transcriptional regulation by Escherichia coli aconitases
    • Tang, Y., and Guest, J. R. (1999) Direct evidence for mRNA binding and post-transcriptional regulation by Escherichia coli aconitases. Microbiology 145, 3069-3079
    • (1999) Microbiology , vol.145 , pp. 3069-3079
    • Tang, Y.1    Guest, J.R.2
  • 70
    • 0033621064 scopus 로고    scopus 로고
    • Bacillus subtilis aconitase is an RNA-binding protein
    • Alén, C., and Sonenshein, A. L. (1999) Bacillus subtilis aconitase is an RNA-binding protein. Proc. Natl. Acad. Sci. U.S.A. 96, 10412-10417
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 10412-10417
    • Alén, C.1    Sonenshein, A.L.2
  • 71
    • 0035283587 scopus 로고    scopus 로고
    • Redox-operated genetic switches: The SoxR and OxyR transcription factors
    • Pomposiello, P. J., and Demple, B. (2001) Redox-operated genetic switches: the SoxR and OxyR transcription factors. Trends Biotechnol. 19, 109-114
    • (2001) Trends Biotechnol , vol.19 , pp. 109-114
    • Pomposiello, P.J.1    Demple, B.2
  • 72
    • 0035036283 scopus 로고    scopus 로고
    • Role of acid metabolism in Streptomyces coelicolor morphological development and antibiotic biosynthesis
    • Viollier, P. H., Minas, W., Dale, G. E., Folcher, M., and Thompson, C. J. (2001) Role of acid metabolism in Streptomyces coelicolor morphological development and antibiotic biosynthesis. J. Bacteriol. 183, 3184-3192
    • (2001) J. Bacteriol , vol.183 , pp. 3184-3192
    • Viollier, P.H.1    Minas, W.2    Dale, G.E.3    Folcher, M.4    Thompson, C.J.5
  • 73
    • 0347091999 scopus 로고    scopus 로고
    • M tuberculosis persistence, latency, and drug tolerance
    • Gomez, J. E., and McKinney, J. D. (2004) M. tuberculosis persistence, latency, and drug tolerance. Tuberculosis 84, 29-44
    • (2004) Tuberculosis , vol.84 , pp. 29-44
    • Gomez, J.E.1    McKinney, J.D.2
  • 74
    • 4644273704 scopus 로고    scopus 로고
    • The high-mobility group A-type protein CarD of the bacterium Myxococcus xanthus as a transcription factor for several distinct vegetative genes
    • Galbis-Martínez, M., Fontes, M., and Murillo, F. J. (2004) The high-mobility group A-type protein CarD of the bacterium Myxococcus xanthus as a transcription factor for several distinct vegetative genes. Genetics 167, 1585-1595
    • (2004) Genetics , vol.167 , pp. 1585-1595
    • Galbis-Martínez, M.1    Fontes, M.2    Murillo, F.J.3
  • 75
    • 0037610124 scopus 로고    scopus 로고
    • The Stigmatella aurantiaca homolog of Myxococcus xanthus high-mobility-group A-type transcription factor CarD: In- sights into the functional modules of CarD and their distribution in bacteria
    • Cayuela, M. L., Elías-Arnanz, M., Peñalver-Mellado, M., Padmanabhan, S., and Murillo, F. J. (2003) The Stigmatella aurantiaca homolog of Myxococcus xanthus high-mobility-group A-type transcription factor CarD: in- sights into the functional modules of CarD and their distribution in bacteria. J. Bacteriol. 185, 3527-3537
    • (2003) J. Bacteriol , vol.185 , pp. 3527-3537
    • Cayuela, M.L.1    Elías-Arnanz, M.2    Peñalver-Mellado, M.3    Padmanabhan, S.4    Murillo, F.J.5
  • 77
    • 0035962921 scopus 로고    scopus 로고
    • HMGI/Y proteins: Flexible regulators of transcription and chromatin structure
    • Reeves, R., and Beckerbauer, L. (2001) HMGI/Y proteins: flexible regulators of transcription and chromatin structure. Biochim. Biophys. Acta 1519, 13-29
    • (2001) Biochim. Biophys. Acta , vol.1519 , pp. 13-29
    • Reeves, R.1    Beckerbauer, L.2
  • 78
    • 0033039345 scopus 로고    scopus 로고
    • Purification and assays for high mobility group HMG-I(Y) protein function
    • Reeves, R., and Nissen, M. S. (1999) Purification and assays for high mobility group HMG-I(Y) protein function. Methods Enzymol. 304, 155-188
    • (1999) Methods Enzymol , vol.304 , pp. 155-188
    • Reeves, R.1    Nissen, M.S.2
  • 79
    • 0034653531 scopus 로고    scopus 로고
    • The role of high-mobility group I(Y) proteins in expression of IL-2 and T cell proliferation
    • Himes, S. R., Reeves, R., Attema, J., Nissen, M., Li, Y., and Shannon, M. F. (2000) The role of high-mobility group I(Y) proteins in expression of IL-2 and T cell proliferation. J. Immunol. 164, 3157-3168
    • (2000) J. Immunol , vol.164 , pp. 3157-3168
    • Himes, S.R.1    Reeves, R.2    Attema, J.3    Nissen, M.4    Li, Y.5    Shannon, M.F.6
  • 81
    • 31544466852 scopus 로고    scopus 로고
    • Characterization of tetracycline resistance mediated by the efflux pump Tap from Mycobacterium fortuitum
    • Ramón-García, S., Martín, C., Aínsa, J. A., and De Rossi, E. (2006) Characterization of tetracycline resistance mediated by the efflux pump Tap from Mycobacterium fortuitum. J. Antimicrob. Chemother. 57, 252-259
    • (2006) J. Antimicrob. Chemother , vol.57 , pp. 252-259
    • Ramón-García, S.1    Martín, C.2    Aínsa, J.A.3    De Rossi, E.4
  • 82
    • 0031793411 scopus 로고    scopus 로고
    • Molecular cloning and characterization of Tap, a putative multidrug efflux pump present in Mycobacterium fortuitum and Mycobacterium tuberculosis
    • Aínsa, J. A., Blokpoel, M. C., Otal, I., Young, D. B., De Smet, K. A., and Martín, C. (1998) Molecular cloning and characterization of Tap, a putative multidrug efflux pump present in Mycobacterium fortuitum and Mycobacterium tuberculosis. J. Bacteriol. 180, 5836-5843
    • (1998) J. Bacteriol , vol.180 , pp. 5836-5843
    • Aínsa, J.A.1    Blokpoel, M.C.2    Otal, I.3    Young, D.B.4    De Smet, K.A.5    Martín, C.6
  • 83
    • 0029128756 scopus 로고
    • A novel transformation of polychlorinated biphenyls by Rhodococcus sp. strain RHA1
    • Seto, M., Kimbara, K., Shimura, M., Hatta, T., Fukuda, M., and Yano, K. (1995) A novel transformation of polychlorinated biphenyls by Rhodococcus sp. strain RHA1. Appl. Environ. Microbiol. 61, 3353-3358
    • (1995) Appl. Environ. Microbiol , vol.61 , pp. 3353-3358
    • Seto, M.1    Kimbara, K.2    Shimura, M.3    Hatta, T.4    Fukuda, M.5    Yano, K.6


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