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Volumn 71, Issue 4, 2009, Pages 972-988

Ss-LrpB, a transcriptional regulator from Sulfolobus solfataricus, regulates a gene cluster with a pyruvate ferredoxin oxidoreductase-encoding operon and permease genes

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; LEUCINE RESPONSIVE REGULATORY PROTEIN; PERMEASE; PYRUVATE SYNTHASE; SULFOLOBUS SOLFATARICUS LEUCINE RESPONSIVE REGULATORY PROTEIN B; UNCLASSIFIED DRUG;

EID: 60349112392     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2008.06578.x     Document Type: Article
Times cited : (41)

References (67)
  • 1
    • 39449138872 scopus 로고    scopus 로고
    • Conditions for gene disruption by homologous recombination of exogenous DNA into the Sulfolobus solfataricus genome
    • Albers, S.-V. Driessen, A.J.M. (2007) Conditions for gene disruption by homologous recombination of exogenous DNA into the Sulfolobus solfataricus genome. Archaea 2 : 145 149.
    • (2007) Archaea , vol.2 , pp. 145-149
    • Albers, S.-V.1    Driessen, A.J.M.2
  • 2
    • 0033485460 scopus 로고    scopus 로고
    • DNA-binding proteins and evolution of transcription regulation in the archaea
    • Aravind, L. Koonin, E.V. (1999) DNA-binding proteins and evolution of transcription regulation in the archaea. Nucleic Acids Res 27 : 4658 4670.
    • (1999) Nucleic Acids Res , vol.27 , pp. 4658-4670
    • Aravind, L.1    Koonin, E.V.2
  • 3
    • 0027314211 scopus 로고
    • The leucine-responsive regulatory protein: More than a regulator?
    • d'Ari, R., Lin, R.T. Newman, E.B. (1993) The leucine-responsive regulatory protein: more than a regulator? Trends Biochem Sci 18 : 260 263.
    • (1993) Trends Biochem Sci , vol.18 , pp. 260-263
    • D'Ari, R.1    Lin, R.T.2    Newman, E.B.3
  • 4
    • 0035067057 scopus 로고    scopus 로고
    • Mechanism and regulation of transcription in archaea
    • Bell, S.D. Jackson, S.P. (2001) Mechanism and regulation of transcription in archaea. Curr Opin Microbiol 4 : 208 213.
    • (2001) Curr Opin Microbiol , vol.4 , pp. 208-213
    • Bell, S.D.1    Jackson, S.P.2
  • 5
    • 0038136948 scopus 로고    scopus 로고
    • Contribution of DNA conformation and topology in right-handed DNA wrapping by the Bacillus subtilis LrpC protein
    • Beloin, C., Jeusset, J., Révet, B., Mirambaut, G., Le Hégarat, F. Le Cam, E. (2003) Contribution of DNA conformation and topology in right-handed DNA wrapping by the Bacillus subtilis LrpC protein. J Biol Chem 278 : 5333 5342.
    • (2003) J Biol Chem , vol.278 , pp. 5333-5342
    • Beloin, C.1    Jeusset, J.2    Révet, B.3    Mirambaut, G.4    Le Hégarat, F.5    Le Cam, E.6
  • 6
    • 0018800089 scopus 로고
    • A rapid alkaline extraction procedure for screening recombinant plasmid DNA
    • Birnboim, H.C. Doly, J. (1979) A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res 7 : 1513 1523.
    • (1979) Nucleic Acids Res , vol.7 , pp. 1513-1523
    • Birnboim, H.C.1    Doly, J.2
  • 7
    • 0037119358 scopus 로고    scopus 로고
    • The Sulfolobus solfataricus Lrp-like protein LysM regulates lysine biosynthesis in response to lysine availability
    • Brinkman, A.B., Bell, S.D., Lebbink, R.J., de Vos, W.M. van der Oost, J. (2002) The Sulfolobus solfataricus Lrp-like protein LysM regulates lysine biosynthesis in response to lysine availability. J Biol Chem 277 : 29537 29549.
    • (2002) J Biol Chem , vol.277 , pp. 29537-29549
    • Brinkman, A.B.1    Bell, S.D.2    Lebbink, R.J.3    De Vos, W.M.4    Van Der Oost, J.5
  • 9
    • 0015275944 scopus 로고
    • Sulfolobus: A new genus of sulfur-oxidizing bacteria living at low pH and high temperature
    • Brock, T.D., Brock, K.M., Belly, R.T. Weiss, R.L. (1972) Sulfolobus: a new genus of sulfur-oxidizing bacteria living at low pH and high temperature. Arch Mikrobiol 84 : 54 68.
    • (1972) Arch Mikrobiol , vol.84 , pp. 54-68
    • Brock, T.D.1    Brock, K.M.2    Belly, R.T.3    Weiss, R.L.4
  • 11
    • 0023425411 scopus 로고
    • Missing contact probing of DNA-protein interactions
    • Brunelle, A. Schleif, R.F. (1987) Missing contact probing of DNA-protein interactions. Proc Nat Acad Sci USA 84 : 6673 6676.
    • (1987) Proc Nat Acad Sci USA , vol.84 , pp. 6673-6676
    • Brunelle, A.1    Schleif, R.F.2
  • 12
    • 0036034720 scopus 로고    scopus 로고
    • High resolution contact probing of the Lrp-like DNA-binding protein Ss-Lrp from the hyperthermoacidophilic crenarchaeote Sulfolobus solfataricus P2
    • Enoru-Eta, J., Gigot, D., Glansdorff, N. Charlier, D. (2002) High resolution contact probing of the Lrp-like DNA-binding protein Ss-Lrp from the hyperthermoacidophilic crenarchaeote Sulfolobus solfataricus P2. Mol Microbiol 45 : 1541 1555.
    • (2002) Mol Microbiol , vol.45 , pp. 1541-1555
    • Enoru-Eta, J.1    Gigot, D.2    Glansdorff, N.3    Charlier, D.4
  • 13
    • 0034044849 scopus 로고    scopus 로고
    • Purification and characterization of Sa-Lrp, a DNA-binding protein from the extreme thermoacidophilic archaeon Sulfolobus acidocaldarius homologous to the bacterial global transcriptional regulator Lrp
    • Enoru-Eta, J., Gigot, D., Thia-Toong, T.-L., Glansdorff, N. Charlier, D. (2000) Purification and characterization of Sa-Lrp, a DNA-binding protein from the extreme thermoacidophilic archaeon Sulfolobus acidocaldarius homologous to the bacterial global transcriptional regulator Lrp. J Bacteriol 182 : 3661 3672.
    • (2000) J Bacteriol , vol.182 , pp. 3661-3672
    • Enoru-Eta, J.1    Gigot, D.2    Thia-Toong, T.-L.3    Glansdorff, N.4    Charlier, D.5
  • 14
    • 0037020177 scopus 로고    scopus 로고
    • A novel ligand-binding domain involved in regulation of amino acid metabolism in prokaryotes
    • Ettema, T.J.G., Brinkman, A.B., Tani, T.H., Rafferty, J.B. van der Oost, J. (2002) A novel ligand-binding domain involved in regulation of amino acid metabolism in prokaryotes. J Biol Chem 277 : 37464 37468.
    • (2002) J Biol Chem , vol.277 , pp. 37464-37468
    • Ettema, T.J.G.1    Brinkman, A.B.2    Tani, T.H.3    Rafferty, J.B.4    Van Der Oost, J.5
  • 15
    • 0037140949 scopus 로고    scopus 로고
    • Substrate recognition by 2-oxoacid: Ferredoxin oxidoreductase from Sulfolobus sp. strain 7
    • Fukuda, E. Wakagi, T. (2002) Substrate recognition by 2-oxoacid: ferredoxin oxidoreductase from Sulfolobus sp. strain 7. Biochim Biophys Acta 1597 : 74 80.
    • (2002) Biochim Biophys Acta , vol.1597 , pp. 74-80
    • Fukuda, E.1    Wakagi, T.2
  • 16
    • 20344386725 scopus 로고    scopus 로고
    • Archaeal transcription and its regulators
    • Geiduschek, E.P. Ouhammouch, M. (2005) Archaeal transcription and its regulators. Mol Microbiol 56 : 1397 1407.
    • (2005) Mol Microbiol , vol.56 , pp. 1397-1407
    • Geiduschek, E.P.1    Ouhammouch, M.2
  • 17
    • 0001572474 scopus 로고
    • Topography of cotransducible arginine mutations in Escherichia coli K12
    • Glansdorff, N. (1965) Topography of cotransducible arginine mutations in Escherichia coli K12. Genetics 51 : 167 179.
    • (1965) Genetics , vol.51 , pp. 167-179
    • Glansdorff, N.1
  • 18
    • 0024351039 scopus 로고
    • Phenotypic charcaterization of the archaebacterial genus Sulfolobus: Comparison of five wild-type strains
    • Grogan, D.W. (1989) Phenotypic charcaterization of the archaebacterial genus Sulfolobus: comparison of five wild-type strains. J Bacteriol 171 : 6710 6719.
    • (1989) J Bacteriol , vol.171 , pp. 6710-6719
    • Grogan, D.W.1
  • 19
    • 37249018447 scopus 로고    scopus 로고
    • Transcription factor e is a part of transcription elongation complexes
    • Grünberg, S., Bartlett, M.S., Naji, S. Thomm, M. (2007) Transcription factor E is a part of transcription elongation complexes. J Biol Chem 282 : 35482 35490.
    • (2007) J Biol Chem , vol.282 , pp. 35482-35490
    • Grünberg, S.1    Bartlett, M.S.2    Naji, S.3    Thomm, M.4
  • 20
    • 22144453950 scopus 로고    scopus 로고
    • Effect of low sulfate concentrations on lactate oxidation and isotope fractionation during sulfate reduction by Archaeoglobus fulgidus strain
    • Habicht, K.S., Salling, L., Thamdrup, B. Canfield, D.E. (2005) Effect of low sulfate concentrations on lactate oxidation and isotope fractionation during sulfate reduction by Archaeoglobus fulgidus strain. Z Appl Environ Microbiol 71 : 3770 3777.
    • (2005) Z Appl Environ Microbiol , vol.71 , pp. 3770-3777
    • Habicht, K.S.1    Salling, L.2    Thamdrup, B.3    Canfield, D.E.4
  • 21
    • 0023684064 scopus 로고
    • A general method of in vitro preparation and specific mutagenesis of DNA fragments: Study of protein and DNA interactions
    • Higuchi, R., Krummel, B. Saiki, R.K. (1988) A general method of in vitro preparation and specific mutagenesis of DNA fragments: study of protein and DNA interactions. Nucleic Acids Res 16 : 7351 7367.
    • (1988) Nucleic Acids Res , vol.16 , pp. 7351-7367
    • Higuchi, R.1    Krummel, B.2    Saiki, R.K.3
  • 22
    • 0037174983 scopus 로고    scopus 로고
    • Global gene expression profiling in Escherichia coli K12
    • Hung, S., Baldi, P. Hatfield, G.W. (2002) Global gene expression profiling in Escherichia coli K12. J Biol Chem 277 : 40309 40323.
    • (2002) J Biol Chem , vol.277 , pp. 40309-40323
    • Hung, S.1    Baldi, P.2    Hatfield, G.W.3
  • 23
    • 0033591426 scopus 로고    scopus 로고
    • An Lrp-type transcriptional regulator from Agrobacterium tumefaciens condenses more than 100 nucleotides of DNA into globular nucleoprotein complexes
    • Jafri, S., Evoy, S., Cho, K., Craighead, H.G. Winans, S.C. (1999) An Lrp-type transcriptional regulator from Agrobacterium tumefaciens condenses more than 100 nucleotides of DNA into globular nucleoprotein complexes. J Mol Biol 288 : 811 824.
    • (1999) J Mol Biol , vol.288 , pp. 811-824
    • Jafri, S.1    Evoy, S.2    Cho, K.3    Craighead, H.G.4    Winans, S.C.5
  • 24
    • 38849111724 scopus 로고    scopus 로고
    • Transcription regulation by feast/famine regulatory proteins, FFRPs, in archaea and eubacteria
    • Kawashima, T., Aramaki, H., Oyamada, T., Makino, K., Yamada, M., Okamura, H., et al. (2008) Transcription regulation by feast/famine regulatory proteins, FFRPs, in archaea and eubacteria. Biol Pharm Bull 31 : 173 186.
    • (2008) Biol Pharm Bull , vol.31 , pp. 173-186
    • Kawashima, T.1    Aramaki, H.2    Oyamada, T.3    Makino, K.4    Yamada, M.5    Okamura, H.6
  • 25
    • 0028853504 scopus 로고
    • Expression of the putA gene encoding proline dehydrogenase from Rhodobacter capsulatus is independent of NtrC regulation but requires an Lrp-like activator protein
    • Keuntje, B., Masepohl, B. Klipp, W. (1995) Expression of the putA gene encoding proline dehydrogenase from Rhodobacter capsulatus is independent of NtrC regulation but requires an Lrp-like activator protein. J Bacteriol 177 : 6432 6439.
    • (1995) J Bacteriol , vol.177 , pp. 6432-6439
    • Keuntje, B.1    Masepohl, B.2    Klipp, W.3
  • 26
    • 0031458333 scopus 로고    scopus 로고
    • The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus
    • Klenk, H.P., Clayton, R.A., Tomb, J.F., White, O., Nelson, K.E., Ketchum, K.A., et al. (1997) The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus. Nature 390 : 364 370.
    • (1997) Nature , vol.390 , pp. 364-370
    • Klenk, H.P.1    Clayton, R.A.2    Tomb, J.F.3    White, O.4    Nelson, K.E.5    Ketchum, K.A.6
  • 27
    • 1542267826 scopus 로고    scopus 로고
    • The archaeal feast/famine regulatory protein: Potential roles of its assembly forms for regulating transcription
    • Koike, H., Ishijima, S.A., Clowney, L. Suzuki, M. (2004) The archaeal feast/famine regulatory protein: potential roles of its assembly forms for regulating transcription. Proc Natl Acad Sci USA 101 : 2840 2845.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 2840-2845
    • Koike, H.1    Ishijima, S.A.2    Clowney, L.3    Suzuki, M.4
  • 28
    • 0022342556 scopus 로고
    • AsnC: An autogenously regulated activator of asparagine synthetase A transcription in Escherichia coli
    • Kölling, R. Lother, H. (1985) AsnC: an autogenously regulated activator of asparagine synthetase A transcription in Escherichia coli. J Bacteriol 164 : 310 315.
    • (1985) J Bacteriol , vol.164 , pp. 310-315
    • Kölling, R.1    Lother, H.2
  • 29
    • 49249119063 scopus 로고    scopus 로고
    • Crystal structure of glutamine receptor protein from Sulfolobus tokodaii strain 7 in complex with its effector 1-glutamine: Implications of effector binding in molecular association and DNA binding
    • Kumarevel, T., Nakano, N., Ponnuraj, K., Gopinath, S.C.B., Sakamoto, K., Shinkai, A., et al. (2008) Crystal structure of glutamine receptor protein from Sulfolobus tokodaii strain 7 in complex with its effector 1-glutamine: implications of effector binding in molecular association and DNA binding. Nucleic Acids Res 36 : 4808 4820.
    • (2008) Nucleic Acids Res , vol.36 , pp. 4808-4820
    • Kumarevel, T.1    Nakano, N.2    Ponnuraj, K.3    Gopinath, S.C.B.4    Sakamoto, K.5    Shinkai, A.6
  • 31
    • 0034749172 scopus 로고    scopus 로고
    • Sugar utilization in the hyperthermophilic, sulfate-reducing archaeon Archaeoglobus fulgidus strain 7324: Starch degradation to acetate and CO2 via a modified Embden-Meyerhof pathway and acetyl-CoA synthetase (ADP-forming)
    • Labes, A. Schönheit, P. (2001) Sugar utilization in the hyperthermophilic, sulfate-reducing archaeon Archaeoglobus fulgidus strain 7324: starch degradation to acetate and CO2 via a modified Embden-Meyerhof pathway and acetyl-CoA synthetase (ADP-forming). Arch Microbiol 176 : 329 338.
    • (2001) Arch Microbiol , vol.176 , pp. 329-338
    • Labes, A.1    Schönheit, P.2
  • 32
    • 0035282970 scopus 로고    scopus 로고
    • Crystal structure of the Lrp-like transcriptional regulator from the archaeon Pyrococcus furiosus
    • Leonard, P.M., Smits, S.H.J., Sedelnikova, S.E., Brinkman, A.B., de Vos, W.M., van der Oost, J., et al. (2001) Crystal structure of the Lrp-like transcriptional regulator from the archaeon Pyrococcus furiosus. EMBO J 20 : 990 997.
    • (2001) EMBO J , vol.20 , pp. 990-997
    • Leonard, P.M.1    Smits, S.H.J.2    Sedelnikova, S.E.3    Brinkman, A.B.4    De Vos, W.M.5    Van Der Oost, J.6
  • 33
    • 0033598826 scopus 로고    scopus 로고
    • The structural basis for the oriented assembly of a TBP/TFB/promoter complex
    • Littlefield, O., Korkhin, Y. Sigler, P.B. (1999) The structural basis for the oriented assembly of a TBP/TFB/promoter complex. Proc Natl Acad Sci USA 96 : 13668 13673.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 13668-13673
    • Littlefield, O.1    Korkhin, Y.2    Sigler, P.B.3
  • 34
    • 0028936476 scopus 로고
    • Characterization of BkdR-DNA binding in the expression of the bkd operon of Pseudomonas putida
    • Madhusudhan, K.T., Huang, N. Sokatch, J.R. (1995) Characterization of BkdR-DNA binding in the expression of the bkd operon of Pseudomonas putida. J Bacteriol 177 : 636 641.
    • (1995) J Bacteriol , vol.177 , pp. 636-641
    • Madhusudhan, K.T.1    Huang, N.2    Sokatch, J.R.3
  • 35
    • 0027227336 scopus 로고
    • The bkdr gene of Pseudomonas putida is required for expression of the bkd operon and encodes a protein related to Lrp of Escherichia coli
    • Madhusudhan, K.T., Lorenz, D. Sokatch, J.R. (1993) The bkdr gene of Pseudomonas putida is required for expression of the bkd operon and encodes a protein related to Lrp of Escherichia coli. J Bacteriol 175 : 3934 3940.
    • (1993) J Bacteriol , vol.175 , pp. 3934-3940
    • Madhusudhan, K.T.1    Lorenz, D.2    Sokatch, J.R.3
  • 36
    • 0018846636 scopus 로고
    • Sequencing end-labeled DNA with base-specific chemical cleavages
    • Maxam, A.M. Gilbert, W. (1980) Sequencing end-labeled DNA with base-specific chemical cleavages. Methods Enzymol 65 : 499 560.
    • (1980) Methods Enzymol , vol.65 , pp. 499-560
    • Maxam, A.M.1    Gilbert, W.2
  • 37
    • 0032985667 scopus 로고    scopus 로고
    • An Lrp-like protein of the hyperthermophilic archaeon Sulfolobus solfataricus which binds its own promoter
    • Napoli, A., van der Oost, J., Sensen, C., Charlebois, R., Rossi, M. Ciaramella, M. (1999) An Lrp-like protein of the hyperthermophilic archaeon Sulfolobus solfataricus which binds its own promoter. J Bacteriol 181 : 1474 1480.
    • (1999) J Bacteriol , vol.181 , pp. 1474-1480
    • Napoli, A.1    Van Der Oost, J.2    Sensen, C.3    Charlebois, R.4    Rossi, M.5    Ciaramella, M.6
  • 38
    • 0035815657 scopus 로고    scopus 로고
    • A novel member of the Bacterial-Archaeal regulator family is a nonspecific DNA-binding protein and induces positive supercoiling
    • Napoli, A., Kvaratskelia, M., White, M.F., Rossi, M. Ciaramella, M. (2001) A novel member of the Bacterial-Archaeal regulator family is a nonspecific DNA-binding protein and induces positive supercoiling. J Biol Chem 276 : 10745 10752.
    • (2001) J Biol Chem , vol.276 , pp. 10745-10752
    • Napoli, A.1    Kvaratskelia, M.2    White, M.F.3    Rossi, M.4    Ciaramella, M.5
  • 40
    • 35148829988 scopus 로고    scopus 로고
    • A structural code for discriminating between transcription signals revealed by the feast/famine regulatory protein DM1 in complex with ligands
    • Okamura, H., Yokoyama, K., Koike, H., Yamada, M., Shimowasa, A., Kabasawa, M., et al. (2007) A structural code for discriminating between transcription signals revealed by the feast/famine regulatory protein DM1 in complex with ligands. Structure 15 : 1325 1338.
    • (2007) Structure , vol.15 , pp. 1325-1338
    • Okamura, H.1    Yokoyama, K.2    Koike, H.3    Yamada, M.4    Shimowasa, A.5    Kabasawa, M.6
  • 41
    • 1942535726 scopus 로고    scopus 로고
    • Transcriptional regulation in Archaea
    • Ouhammouch, M. (2004) Transcriptional regulation in Archaea. Curr Opin Genet Dev 14 : 133 138.
    • (2004) Curr Opin Genet Dev , vol.14 , pp. 133-138
    • Ouhammouch, M.1
  • 42
    • 27344457589 scopus 로고    scopus 로고
    • An expanding family of archaeal transcriptional activators
    • Ouhammouch, M. Geiduschek, E.P. (2005) An expanding family of archaeal transcriptional activators. Proc Natl Acad Sci USA 102 : 15423 15428.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 15423-15428
    • Ouhammouch, M.1    Geiduschek, E.P.2
  • 44
    • 6344272907 scopus 로고    scopus 로고
    • Ss-LrpB, a novel Lrp-like regulator of Sulfolobus solfataricus P2, binds cooperatively to three conserved targets in its own control region
    • Peeters, E., Thia-Toong, T.L., Gigot, D., Maes, D. Charlier, D. (2004) Ss-LrpB, a novel Lrp-like regulator of Sulfolobus solfataricus P2, binds cooperatively to three conserved targets in its own control region. Mol Microbiol 54 : 321 336.
    • (2004) Mol Microbiol , vol.54 , pp. 321-336
    • Peeters, E.1    Thia-Toong, T.L.2    Gigot, D.3    Maes, D.4    Charlier, D.5
  • 45
    • 33744954870 scopus 로고    scopus 로고
    • Ss-LrpB from Sulfolobus solfataricus condenses about 100 base pairs of its own operator DNA into globular nucleoprotein complexes
    • Peeters, E., Willaert, R., Maes, D. Charlier, D. (2006) Ss-LrpB from Sulfolobus solfataricus condenses about 100 base pairs of its own operator DNA into globular nucleoprotein complexes. J Biol Chem 281 : 11721 11728.
    • (2006) J Biol Chem , vol.281 , pp. 11721-11728
    • Peeters, E.1    Willaert, R.2    Maes, D.3    Charlier, D.4
  • 46
    • 33846913874 scopus 로고    scopus 로고
    • Analysis of the DNA-binding sequence specificity of the archaeal transcriptional regulator Ss-LrpB from Sulfolobus solfataricus by systematic mutagenesis and high resolution contact probing
    • Peeters, E., Wartel, C., Maes, D. Charlier, D. (2007) Analysis of the DNA-binding sequence specificity of the archaeal transcriptional regulator Ss-LrpB from Sulfolobus solfataricus by systematic mutagenesis and high resolution contact probing. Nucleic Acids Res 35 : 623 633.
    • (2007) Nucleic Acids Res , vol.35 , pp. 623-633
    • Peeters, E.1    Wartel, C.2    Maes, D.3    Charlier, D.4
  • 47
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in real-time RT-PCR
    • Pfaffl, M.W. (2001) A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res 29 : e45.
    • (2001) Nucleic Acids Res , vol.29
    • Pfaffl, M.W.1
  • 48
    • 33745004429 scopus 로고    scopus 로고
    • Mutations and rearrangements in the genome of Sulfolobus solfataricus P2
    • Redder, P. Garrett, R.A. (2006) Mutations and rearrangements in the genome of Sulfolobus solfataricus P2. J Bacteriol 188 : 4198 4206.
    • (2006) J Bacteriol , vol.188 , pp. 4198-4206
    • Redder, P.1    Garrett, R.A.2
  • 49
    • 37549043124 scopus 로고    scopus 로고
    • Crystal structure of Mycobacterium tuberculosis LrpA, a leucine-responsive global regulator associated with starvation response
    • Reddy, M.C., Gokulan, K., Jacobs, W.R. Ioerger, T.R. Sacchettini, J.C. (2008) Crystal structure of Mycobacterium tuberculosis LrpA, a leucine-responsive global regulator associated with starvation response. Protein Sci 17 : 159 170.
    • (2008) Protein Sci , vol.17 , pp. 159-170
    • Reddy, M.C.1    Gokulan, K.2    Jacobs, W.R.3    Ioerger, T.R.4    Sacchettini, J.C.5
  • 50
    • 34347225934 scopus 로고    scopus 로고
    • The structure and transcriptional analysis of a global regulator from Neisseria meningitidis
    • Ren, J., Sainsbury, S., Combs, S.E., Capper, R.G., Jordan, P.W., Berrow, N.S., et al. (2007) The structure and transcriptional analysis of a global regulator from Neisseria meningitidis. J Biol Chem 282 : 14655 14664.
    • (2007) J Biol Chem , vol.282 , pp. 14655-14664
    • Ren, J.1    Sainsbury, S.2    Combs, S.E.3    Capper, R.G.4    Jordan, P.W.5    Berrow, N.S.6
  • 51
    • 33846839291 scopus 로고    scopus 로고
    • Structure of the Escherichia coli leucine-responsive regulatory protein Lrp reveals a novel octameric assembly
    • de los Rios, S. Perona, J.J. (2007) Structure of the Escherichia coli leucine-responsive regulatory protein Lrp reveals a novel octameric assembly. J Mol Biol 366 : 1589 1602.
    • (2007) J Mol Biol , vol.366 , pp. 1589-1602
    • De Los Rios, S.1    Perona, J.J.2
  • 52
    • 0347285395 scopus 로고    scopus 로고
    • Occurrence and characterization of mercury resistance in the hyperthermophilic archaeon Sulfolobus solfataricus by use of gene disruption
    • Schelert, J., Dixit, V., Hoang, V., Simbahan, J., Drozda, M. Blum, P. (2004) Occurrence and characterization of mercury resistance in the hyperthermophilic archaeon Sulfolobus solfataricus by use of gene disruption. J Bacteriol 186 : 427 437.
    • (2004) J Bacteriol , vol.186 , pp. 427-437
    • Schelert, J.1    Dixit, V.2    Hoang, V.3    Simbahan, J.4    Drozda, M.5    Blum, P.6
  • 53
    • 0035079430 scopus 로고    scopus 로고
    • 2-keto acid oxidoreductases from Pyrococcus furiosus and Thermococcus litoralis
    • Schut, G.J., Menon, A.L. Adams, M.W. (2001) 2-keto acid oxidoreductases from Pyrococcus furiosus and Thermococcus litoralis. Methods Enzymol 331 : 144 158.
    • (2001) Methods Enzymol , vol.331 , pp. 144-158
    • Schut, G.J.1    Menon, A.L.2    Adams, M.W.3
  • 55
    • 37549028005 scopus 로고    scopus 로고
    • Mechanistic insights from the crystal structures of a feast/famine regulatory protein from Mycobacterium tuberculosis H37Rv
    • Shrivastrava, T. Ramachandran, R. (2007) Mechanistic insights from the crystal structures of a feast/famine regulatory protein from Mycobacterium tuberculosis H37Rv. Nucleic Acids Res 35 : 7324 7335.
    • (2007) Nucleic Acids Res , vol.35 , pp. 7324-7335
    • Shrivastrava, T.1    Ramachandran, R.2
  • 56
    • 33645062395 scopus 로고    scopus 로고
    • Reconstruction of central carbon metabolism in Sulfolobus solfataricus using a two-dimensional gel electrophoresis map, stable isotope labelling and DNA microarray analysis
    • Snijders, A.P., Walther, J., Peter, S., Kinnman, I., de Vos, M.G., van de Werken, H.J., et al. (2006) Reconstruction of central carbon metabolism in Sulfolobus solfataricus using a two-dimensional gel electrophoresis map, stable isotope labelling and DNA microarray analysis. Proteomics 6 : 1518 1529.
    • (2006) Proteomics , vol.6 , pp. 1518-1529
    • Snijders, A.P.1    Walther, J.2    Peter, S.3    Kinnman, I.4    De Vos, M.G.5    Van De Werken, H.J.6
  • 57
    • 34247498903 scopus 로고    scopus 로고
    • Flagellar motility and structure in the hyperthermoacidophilic archaeon Sulfolobus solfataricus
    • Szabo, Z., Sani, M., Groeneveld, M., Zolghadr, B., Schelert, J., Albers, S.-V., et al. (2007) Flagellar motility and structure in the hyperthermoacidophilic archaeon Sulfolobus solfataricus. J Bacteriol 189 : 4305 4309.
    • (2007) J Bacteriol , vol.189 , pp. 4305-4309
    • Szabo, Z.1    Sani, M.2    Groeneveld, M.3    Zolghadr, B.4    Schelert, J.5    Albers, S.-V.6
  • 58
    • 0037109068 scopus 로고    scopus 로고
    • Adaptation to famine: A family of stationary-phase genes revealed by microarray analysis
    • Tani, T.H., Khodursky, A., Blumenthal, R.M., Brown, P.O. Matthews, R.G. (2002) Adaptation to famine: a family of stationary-phase genes revealed by microarray analysis. Proc Natl Acad Sci USA 99 : 13471 13476.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 13471-13476
    • Tani, T.H.1    Khodursky, A.2    Blumenthal, R.M.3    Brown, P.O.4    Matthews, R.G.5
  • 59
    • 0343340048 scopus 로고    scopus 로고
    • Bacillus subtilis LrpC is a sequence-independent DNA-binding and DNA-bending protein which bridges DNA
    • Tapias, A., Lopez, G. Ayora, S. (2000) Bacillus subtilis LrpC is a sequence-independent DNA-binding and DNA-bending protein which bridges DNA. Nucleic Acids Res 28 : 552 559.
    • (2000) Nucleic Acids Res , vol.28 , pp. 552-559
    • Tapias, A.1    Lopez, G.2    Ayora, S.3
  • 60
    • 33645525801 scopus 로고    scopus 로고
    • Structural insight into gene transcriptional regulation and effector binding by the Lrp/AsnC family
    • Thaw, P., Sedelnikova, S.E., Muranova, T., Wiese, S., Ayora, S., Alonso, J.C., et al. (2006) Structural insight into gene transcriptional regulation and effector binding by the Lrp/AsnC family. Nucleic Acids Res 34 : 1439 1449.
    • (2006) Nucleic Acids Res , vol.34 , pp. 1439-1449
    • Thaw, P.1    Sedelnikova, S.E.2    Muranova, T.3    Wiese, S.4    Ayora, S.5    Alonso, J.C.6
  • 61
    • 12544256546 scopus 로고    scopus 로고
    • Divergent transcriptional and translational signals in Archaea
    • Torarinsson, E., Klenk, H.-P. Garrett, R.A. (2005) Divergent transcriptional and translational signals in Archaea. Environ Microbiol 7 : 47 54.
    • (2005) Environ Microbiol , vol.7 , pp. 47-54
    • Torarinsson, E.1    Klenk, H.-P.2    Garrett, R.A.3
  • 62
    • 0032502998 scopus 로고    scopus 로고
    • The arginine repressor of Escherichia coli K-12 makes direct contacts to minor and major groove determinants of the operators
    • Wang, H., Glansdorff, N. Charlier, D. (1998) The arginine repressor of Escherichia coli K-12 makes direct contacts to minor and major groove determinants of the operators. J Mol Biol 277 : 805 824.
    • (1998) J Mol Biol , vol.277 , pp. 805-824
    • Wang, H.1    Glansdorff, N.2    Charlier, D.3
  • 63
    • 3242879355 scopus 로고    scopus 로고
    • PredictRegulon: A web server for the prediction of the regulatory protein binding sites and operons in prokaryote genomes
    • Yellaboina, S., Seshadri, J., Senthil Kumar, M. Ranjan, A. (2004) PredictRegulon: a web server for the prediction of the regulatory protein binding sites and operons in prokaryote genomes. Nucleic Acids Res 32 : W318 W320.
    • (2004) Nucleic Acids Res , vol.32
    • Yellaboina, S.1    Seshadri, J.2    Senthil Kumar, M.3    Ranjan, A.4
  • 64
    • 33644890216 scopus 로고    scopus 로고
    • Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp, AsnC and related archaeal transcription factors
    • Yokoyama, K., Ishijima, S.A., Clowney, L., Koike, H., Aramaki, H., Tanaka, C., et al. (2006) Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp, AsnC and related archaeal transcription factors. FEMS Microbiol Rev 30 : 89 106.
    • (2006) FEMS Microbiol Rev , vol.30 , pp. 89-106
    • Yokoyama, K.1    Ishijima, S.A.2    Clowney, L.3    Koike, H.4    Aramaki, H.5    Tanaka, C.6
  • 65
    • 36749036126 scopus 로고    scopus 로고
    • Feast/famine regulation by transcription factor FL11 for the survival of the hyperthermophilic archaeon Pyrococcus OT3
    • Yokoyama, K., Ishijima, S.A., Koike, H., Kurihara, C., Shimowasa, A., Kabasawa, M., et al. (2007) Feast/famine regulation by transcription factor FL11 for the survival of the hyperthermophilic archaeon Pyrococcus OT3. Structure 15 : 1542 1554.
    • (2007) Structure , vol.15 , pp. 1542-1554
    • Yokoyama, K.1    Ishijima, S.A.2    Koike, H.3    Kurihara, C.4    Shimowasa, A.5    Kabasawa, M.6
  • 66
    • 0029784085 scopus 로고    scopus 로고
    • 2-oxoacid: Ferredoxin oxidoreductase from the thermoacidophilic archaeon, Sulfolobus sp. strain 7
    • Zhang, Q., Iwasaki, T., Wakagi, T. Oshima, T. (1996) 2-oxoacid: ferredoxin oxidoreductase from the thermoacidophilic archaeon, Sulfolobus sp. strain 7. J Biochem 120 : 587 599.
    • (1996) J Biochem , vol.120 , pp. 587-599
    • Zhang, Q.1    Iwasaki, T.2    Wakagi, T.3    Oshima, T.4
  • 67
    • 34247515309 scopus 로고    scopus 로고
    • Identification of a system required for the functional surface localization of sugar binding proteins with class III signal peptides in Sulfolobus solfataricus
    • Zolghadr, B., Weber, S., Szabo, Z., Driessen, A.J. Albers, S.-V. (2007) Identification of a system required for the functional surface localization of sugar binding proteins with class III signal peptides in Sulfolobus solfataricus. Mol Microbiol 64 : 795 806.
    • (2007) Mol Microbiol , vol.64 , pp. 795-806
    • Zolghadr, B.1    Weber, S.2    Szabo, Z.3    Driessen, A.J.4    Albers, S.-V.5


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