메뉴 건너뛰기




Volumn 17, Issue 1, 2008, Pages 159-170

Crystal structure of Mycobacterium tuberculosis LrpA, a leucine-responsive global regulator associated with starvation response

Author keywords

DNA binding; EMSA; HTH motif; lat gene; LrpA; Transcriptional regulator

Indexed keywords

ASPARAGINE; BACTERIAL PROTEIN; LEUCINE; LEUCINE RESPONSIVE REGULATORY PROTEIN; LRPA PROTEIN; UNCLASSIFIED DRUG;

EID: 37549043124     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.073192208     Document Type: Article
Times cited : (22)

References (73)
  • 1
    • 0029990572 scopus 로고    scopus 로고
    • The mechanism of velocity modulated allosteric regulation in D-3-phosphoglycerate dehydrogenase. Cross-linking adjacent regulatory domains with engineered disulfides mimics effector binding
    • Al-Rabiee, R., Lee, E.J., and Grant, G.A. 1996. The mechanism of velocity modulated allosteric regulation in D-3-phosphoglycerate dehydrogenase. Cross-linking adjacent regulatory domains with engineered disulfides mimics effector binding. J. Biol. Chem. 271: 13013-13017.
    • (1996) J. Biol. Chem , vol.271 , pp. 13013-13017
    • Al-Rabiee, R.1    Lee, E.J.2    Grant, G.A.3
  • 2
    • 34447537903 scopus 로고    scopus 로고
    • Curved DNA and prokaryotic promoters: A mechanism for activation of transcription
    • ed. T. Ohyama, Springer, Berlin, Germany
    • Asayama, M. and Ohyama, T. 2005. Curved DNA and prokaryotic promoters: A mechanism for activation of transcription. In DNA conformation and transcription. (ed. T. Ohyama). Springer, Berlin, Germany.
    • (2005) DNA conformation and transcription
    • Asayama, M.1    Ohyama, T.2
  • 3
    • 29244443682 scopus 로고    scopus 로고
    • Transcription and autoregulation of the Rv3134c-devR-devS operon of Mycobacterium tuberculosis
    • Bagchi, G., Chauhan, S., Sharma, D., and Tyagi, J.S. 2005. Transcription and autoregulation of the Rv3134c-devR-devS operon of Mycobacterium tuberculosis. Microbiol. 151: 4045-4053.
    • (2005) Microbiol , vol.151 , pp. 4045-4053
    • Bagchi, G.1    Chauhan, S.2    Sharma, D.3    Tyagi, J.S.4
  • 4
    • 0033894927 scopus 로고    scopus 로고
    • Characterization of LrpC DNA-binding properties and regulation of Bacillus subtilis lrpC gene expression
    • Beloin, C., Exley, R., Mahé, A.L., Zouine, M., Cubasch, S., and Le Hégarat, F. 2000. Characterization of LrpC DNA-binding properties and regulation of Bacillus subtilis lrpC gene expression. J. Bacteriol. 182: 4414-4424.
    • (2000) J. Bacteriol , vol.182 , pp. 4414-4424
    • Beloin, C.1    Exley, R.2    Mahé, A.L.3    Zouine, M.4    Cubasch, S.5    Le Hégarat, F.6
  • 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., and 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
    • 0036270739 scopus 로고    scopus 로고
    • Evaluation of a nutrient starvation model of Mycobacterium tuberculosis persistence by gene and protein expression profiling
    • Betts, J.C., Lukey, P.T., Robb, L.C., McAdam, R.A., and Duncan, K. 2002. Evaluation of a nutrient starvation model of Mycobacterium tuberculosis persistence by gene and protein expression profiling. Mol. Microbiol. 43: 717-731.
    • (2002) Mol. Microbiol , vol.43 , pp. 717-731
    • Betts, J.C.1    Lukey, P.T.2    Robb, L.C.3    McAdam, R.A.4    Duncan, K.5
  • 7
    • 0024571640 scopus 로고
    • The helix-turn-helix DNA binding motif
    • Brennan, R.G. and Matthews, B.W. 1989. The helix-turn-helix DNA binding motif. J. Biol. Chem. 264: 1903-1906.
    • (1989) J. Biol. Chem , vol.264 , pp. 1903-1906
    • Brennan, R.G.1    Matthews, B.W.2
  • 8
    • 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., and 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
  • 10
    • 13844312836 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis SigD sigma factor controls the expression of ribosome-associated gene products in stationary phase and is required for full virulence
    • Calamita, H., Ko, C., Tyagi, S., Yoshimatsu, T., Morrison, N.E., and Bishai, W.R. 2005. The Mycobacterium tuberculosis SigD sigma factor controls the expression of ribosome-associated gene products in stationary phase and is required for full virulence. Cell. Microbiol. 7: 233-244.
    • (2005) Cell. Microbiol , vol.7 , pp. 233-244
    • Calamita, H.1    Ko, C.2    Tyagi, S.3    Yoshimatsu, T.4    Morrison, N.E.5    Bishai, W.R.6
  • 11
    • 0028111825 scopus 로고
    • The leucine-responsive regulatory protein, a global regulator of metabolism in Escherichia coli
    • Calvo, J.M. and Matthews, R.G. 1994. The leucine-responsive regulatory protein, a global regulator of metabolism in Escherichia coli. Microbiol. Rev. 58: 466-490.
    • (1994) Microbiol. Rev , vol.58 , pp. 466-490
    • Calvo, J.M.1    Matthews, R.G.2
  • 12
    • 0036041669 scopus 로고    scopus 로고
    • Leucine-induced dissociation of Escherichia coli Lrp hexadecamers to octamers
    • Chen, S. and Calvo, J.M. 2002. Leucine-induced dissociation of Escherichia coli Lrp hexadecamers to octamers. J. Mol. Biol. 318: 1031-1042.
    • (2002) J. Mol. Biol , vol.318 , pp. 1031-1042
    • Chen, S.1    Calvo, J.M.2
  • 14
    • 0032536158 scopus 로고    scopus 로고
    • Crystal structure of the cyanobacterial metallothionein repressor SmtB: A model for metalloregulatory proteins
    • Cook, W.J., Kar, S.R., Taylor, K.B., and Hall, L.M. 1998. Crystal structure of the cyanobacterial metallothionein repressor SmtB: A model for metalloregulatory proteins. J. Mol. Biol. 275: 337-346.
    • (1998) J. Mol. Biol , vol.275 , pp. 337-346
    • Cook, W.J.1    Kar, S.R.2    Taylor, K.B.3    Hall, L.M.4
  • 15
    • 0002473587 scopus 로고    scopus 로고
    • Phase combination and cross validation in iterated density-modification calculations
    • Cowtan, K.D. and Main, P. 1996. Phase combination and cross validation in iterated density-modification calculations. Acta Crystallogr. D Biol. Crystallogr. 52: 43-48.
    • (1996) Acta Crystallogr. D Biol. Crystallogr , vol.52 , pp. 43-48
    • Cowtan, K.D.1    Main, P.2
  • 16
    • 0032872798 scopus 로고    scopus 로고
    • Density modification for macromolecular phase improvement
    • Cowtan, K.D. and Zhang, K.Y. 1999. Density modification for macromolecular phase improvement. Prog. Biophys. Mol. Biol. 72: 245-270.
    • (1999) Prog. Biophys. Mol. Biol , vol.72 , pp. 245-270
    • Cowtan, K.D.1    Zhang, K.Y.2
  • 18
    • 0029127850 scopus 로고
    • A consensus sequence for binding of Lrp to DNA
    • Cui, Y., Wang, Q., Stormo, G.D., and Calvo, J.M. 1995. A consensus sequence for binding of Lrp to DNA. J. Bacteriol. 177: 4872-4880.
    • (1995) J. Bacteriol , vol.177 , pp. 4872-4880
    • Cui, Y.1    Wang, Q.2    Stormo, G.D.3    Calvo, J.M.4
  • 19
    • 0043192889 scopus 로고    scopus 로고
    • The role of Rel(Mtb)-mediated adaptation to stationary phase in long-term persistence of Mycobacterium tuberculosis in mice
    • Dahl, J.L., Kraus, C.N., Boshoff, H.I.M., Doan, B., Foley, K., Avarbock, D., Kaplan, G., Mizraji, V., and Barry, C.E. 2003. The role of Rel(Mtb)-mediated adaptation to stationary phase in long-term persistence of Mycobacterium tuberculosis in mice. PNAS 100: 10026-10031.
    • (2003) PNAS , vol.100 , pp. 10026-10031
    • Dahl, J.L.1    Kraus, C.N.2    Boshoff, H.I.M.3    Doan, B.4    Foley, K.5    Avarbock, D.6    Kaplan, G.7    Mizraji, V.8    Barry, C.E.9
  • 20
    • 33846839291 scopus 로고    scopus 로고
    • de los Rios, S. and Perona, J.J. 2006. Structure of the Escherichia coli leucine-responsive regulatory protein Lrp reveals a novel octameric assembly. J. Mol. Biol. 366: 1589-1602.
    • de los Rios, S. and Perona, J.J. 2006. Structure of the Escherichia coli leucine-responsive regulatory protein Lrp reveals a novel octameric assembly. J. Mol. Biol. 366: 1589-1602.
  • 21
    • 0029981245 scopus 로고    scopus 로고
    • A stationary-phase stress-response s factor from Mycobacterium tuberculosis
    • DeMaio, J., Zhang, Y., Ko, C., Young, D.B., and Bishai, W.R. 1996. A stationary-phase stress-response s factor from Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. 93: 2790-2794.
    • (1996) Proc. Natl. Acad. Sci , vol.93 , pp. 2790-2794
    • DeMaio, J.1    Zhang, Y.2    Ko, C.3    Young, D.B.4    Bishai, W.R.5
  • 22
    • 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., and 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
  • 23
    • 0037020177 scopus 로고    scopus 로고
    • A novel ligand-binding domain involved in regulation of amino acid metabolism in prokaryotes
    • Ettema, T.J., Brinkman, A.B., Tani, T.H., Rafferty, J.B., and 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.1    Brinkman, A.B.2    Tani, T.H.3    Rafferty, J.B.4    Van Der Oost, J.5
  • 24
    • 0027609916 scopus 로고
    • SETOR: Hardware lighted three-dimensional solid model representation of macromolecules
    • Evans, S.V. 1993. SETOR: Hardware lighted three-dimensional solid model representation of macromolecules. J. Mol. Graph. 11: 134-138.
    • (1993) J. Mol. Graph , vol.11 , pp. 134-138
    • Evans, S.V.1
  • 25
    • 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
  • 27
    • 0347091999 scopus 로고    scopus 로고
    • Gomez, J.E. and McKinney, J.D. 2004. M. tuberculosis persistence, latency, and drug tolerance. Tuberculosis (Edinb.) 84: 29-44.
    • Gomez, J.E. and McKinney, J.D. 2004. M. tuberculosis persistence, latency, and drug tolerance. Tuberculosis (Edinb.) 84: 29-44.
  • 28
    • 0028624664 scopus 로고
    • Bending and curvature calculations in B-DNA
    • Goodsell, D.S. and Dickerson, R.E. 1994. Bending and curvature calculations in B-DNA. Nucleic Acids Res. 22: 5497-5503.
    • (1994) Nucleic Acids Res , vol.22 , pp. 5497-5503
    • Goodsell, D.S.1    Dickerson, R.E.2
  • 29
    • 33845944628 scopus 로고    scopus 로고
    • The ACT domain: A small molecule binding domain and its role as a common regulatory element
    • Grant, G.A. 2006. The ACT domain: A small molecule binding domain and its role as a common regulatory element. J. Biol. Chem. 281: 33825-33829.
    • (2006) J. Biol. Chem , vol.281 , pp. 33825-33829
    • Grant, G.A.1
  • 30
    • 0029670622 scopus 로고    scopus 로고
    • A model for the regulation of D-3-phosphoglycerate dehydrogenase, a Vmax-type allosteric enzyme
    • Grant, G.A., Schuller, D.J., and Banaszak, L.J. 1996. A model for the regulation of D-3-phosphoglycerate dehydrogenase, a Vmax-type allosteric enzyme. Protein Sci. 5: 34-41.
    • (1996) Protein Sci , vol.5 , pp. 34-41
    • Grant, G.A.1    Schuller, D.J.2    Banaszak, L.J.3
  • 31
    • 0031058883 scopus 로고    scopus 로고
    • Phase determination from multi-wavelength anomalous diffraction measurements
    • Hendickson, W.A. and Ogata, C.M. 1997. Phase determination from multi-wavelength anomalous diffraction measurements. Methods Enzymol. 276: 307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Hendickson, W.A.1    Ogata, C.M.2
  • 32
    • 0028871926 scopus 로고
    • DALI: A network tool for protein structure comparison
    • Holm, L. and Sander, C. 1995. DALI: A network tool for protein structure comparison. Trends Biochem. Sci. 20: 478-480.
    • (1995) Trends Biochem. Sci , vol.20 , pp. 478-480
    • Holm, L.1    Sander, C.2
  • 33
    • 0034628901 scopus 로고    scopus 로고
    • Computational identification of cis-regulatory elements associated with groups of functionally related genes in Saccharomyces cerevisiae
    • Hughes, J.D., Estep, P.W., Tavazoie, S., and Church, G.M. 2000. Computational identification of cis-regulatory elements associated with groups of functionally related genes in Saccharomyces cerevisiae. J. Mol. Biol. 296: 1205-1214.
    • (2000) J. Mol. Biol , vol.296 , pp. 1205-1214
    • Hughes, J.D.1    Estep, P.W.2    Tavazoie, S.3    Church, G.M.4
  • 34
    • 0348014440 scopus 로고    scopus 로고
    • The TEXTAL system: Artificial intelligence techniques for automated protein model building
    • Ioerger, T.R. and Sacchettini, J.C. 2003. The TEXTAL system: Artificial intelligence techniques for automated protein model building. Methods Enzymol. 374: 244-270.
    • (2003) Methods Enzymol , vol.374 , pp. 244-270
    • Ioerger, T.R.1    Sacchettini, J.C.2
  • 36
    • 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., and Suzuki, M. 2004. The archaeal feast/famine regulatory protein: Potential roles of its assembly forms for regulating transcription. Proc. Natl. Acad. Sci. 101: 2840-2845.
    • (2004) Proc. Natl. Acad. Sci , vol.101 , pp. 2840-2845
    • Koike, H.1    Ishijima, S.A.2    Clowney, L.3    Suzuki, M.4
  • 37
    • 0022342556 scopus 로고
    • AsnC: An autogenously regulated activator of asparagine synthetase A transcription in Escherichia coli
    • Kolling, R. and 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
    • Kolling, R.1    Lother, H.2
  • 38
    • 0001759947 scopus 로고    scopus 로고
    • Crystal structure of the Escherichia coli rob transcription factor complexed to DNA
    • Kwon, H.J., Bennik, M.H., Demple, B., and Ellenberger, T. 2000. Crystal structure of the Escherichia coli rob transcription factor complexed to DNA. Nat. Struct. Biol. 7: 424-430.
    • (2000) Nat. Struct. Biol , vol.7 , pp. 424-430
    • Kwon, H.J.1    Bennik, M.H.2    Demple, B.3    Ellenberger, T.4
  • 39
    • 10544251055 scopus 로고    scopus 로고
    • Effects of nutrition and growth rate on Lrp levels in Escherichia coli
    • Landgraf, J.R., Wu, J., and Calvo, J.M. 1996. Effects of nutrition and growth rate on Lrp levels in Escherichia coli. J. Bacteriol. 1996: 6930-6936.
    • (1996) J. Bacteriol , vol.1996 , pp. 6930-6936
    • Landgraf, J.R.1    Wu, J.2    Calvo, J.M.3
  • 41
    • 0009365006 scopus 로고
    • The influence of foodstuffs upon the respiratory metabolism and growth of human tubercle bacilli
    • Loebel, R.O., Shorr, E., and Richardson, H.B. 1933a. The influence of foodstuffs upon the respiratory metabolism and growth of human tubercle bacilli. J. Bacteriol. 26: 139-166.
    • (1933) J. Bacteriol , vol.26 , pp. 139-166
    • Loebel, R.O.1    Shorr, E.2    Richardson, H.B.3
  • 42
    • 0000226712 scopus 로고
    • The influence of adverse conditions upon the respiratory metabolism and growth of human tubercle bacilli
    • Loebel, R.O., Shorr, E., and Richardson, H.B. 1933b. The influence of adverse conditions upon the respiratory metabolism and growth of human tubercle bacilli. J. Bacteriol. 26: 167-200.
    • (1933) J. Bacteriol , vol.26 , pp. 167-200
    • Loebel, R.O.1    Shorr, E.2    Richardson, H.B.3
  • 43
    • 0027439293 scopus 로고
    • Precursor flux control through targeted chromosomal insertion of the lysine epsilon-aminotransferase (lat) gene in cephamycin C biosynthesis
    • Malmberg, L.H., Hu, W.S., and Sherman, D.H. 1993. Precursor flux control through targeted chromosomal insertion of the lysine epsilon-aminotransferase (lat) gene in cephamycin C biosynthesis. J. Bacteriol. 175: 6916-6924.
    • (1993) J. Bacteriol , vol.175 , pp. 6916-6924
    • Malmberg, L.H.1    Hu, W.S.2    Sherman, D.H.3
  • 44
    • 0030447842 scopus 로고    scopus 로고
    • Lrp is a direct repressor of the dad operon in Escherichia coli
    • Mathew, E., Zhi, J., and Freundlich, M. 1996. Lrp is a direct repressor of the dad operon in Escherichia coli. J. Bacteriol. 178: 7234-7240.
    • (1996) J. Bacteriol , vol.178 , pp. 7234-7240
    • Mathew, E.1    Zhi, J.2    Freundlich, M.3
  • 45
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews, B.W. 1968. Solvent content of protein crystals. J. Mol. Biol. 33: 491-497.
    • (1968) J. Mol. Biol , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 46
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit - a versatile program for manipulating atomic coordinates and electron density
    • McRee, D.E. 1999. XtalView/Xfit - a versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 125: 156-165.
    • (1999) J. Struct. Biol , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 48
    • 0024961628 scopus 로고
    • Structure of the amino-terminal domain of phage 434 repressor at 2.0 Å resolution
    • Mondragon, A., Subbiah, S., Almo, S.C., Drottar, M., and Harrison, S.C. 1989. Structure of the amino-terminal domain of phage 434 repressor at 2.0 Å resolution. J. Mol. Biol. 205: 189-200.
    • (1989) J. Mol. Biol , vol.205 , pp. 189-200
    • Mondragon, A.1    Subbiah, S.2    Almo, S.C.3    Drottar, M.4    Harrison, S.C.5
  • 49
    • 0001291140 scopus 로고    scopus 로고
    • A powerful non-homology method for the prediction of operons in prokaryotes
    • Moreno-Hagelsieb, G. and Collado-Vides, X. 2002. A powerful non-homology method for the prediction of operons in prokaryotes. Bioinformatics 18(Suppl. 1):S329-S336.
    • (2002) Bioinformatics , vol.18 , Issue.SUPPL. 1
    • Moreno-Hagelsieb, G.1    Collado-Vides, X.2
  • 51
  • 52
    • 0029144601 scopus 로고
    • Gibbs motif sampling: Detection of bacterial outer membrane protein repeats
    • Neuwald, A.F., Liu, J.S., and Lawrence, C.E. 1995. Gibbs motif sampling: Detection of bacterial outer membrane protein repeats. Protein Sci. 4: 1618-1632.
    • (1995) Protein Sci , vol.4 , pp. 1618-1632
    • Neuwald, A.F.1    Liu, J.S.2    Lawrence, C.E.3
  • 53
    • 0028845957 scopus 로고
    • Differential binding of Lrp to two sets of pap DNA binding sites mediated by Pap I regulates Pap phase variation in Escherichia coli
    • Nou, X., Braaten, B., Kaltenbach, L., and Low, D.A. 1995. Differential binding of Lrp to two sets of pap DNA binding sites mediated by Pap I regulates Pap phase variation in Escherichia coli. EMBO J. 14: 5785-5797.
    • (1995) EMBO J , vol.14 , pp. 5785-5797
    • Nou, X.1    Braaten, B.2    Kaltenbach, L.3    Low, D.A.4
  • 54
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. and Minor, W. (1997). Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276: 307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 55
    • 27344457589 scopus 로고    scopus 로고
    • An expanding family of archaeal transcriptional activators
    • Ouhammouch, M. and Geiduschek, E.P. 2005. An expanding family of archaeal transcriptional activators. Proc. Natl. Acad. Sci. 102: 15423-15428.
    • (2005) Proc. Natl. Acad. Sci , vol.102 , pp. 15423-15428
    • Ouhammouch, M.1    Geiduschek, E.P.2
  • 56
    • 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., and 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
  • 57
    • 0027537042 scopus 로고
    • Mutations affecting the ability of Escherichia coli Lrp to bind DNA, activate transcription, or respond to leucine
    • Platko, J.V. and Calvo, J.M. 1993. Mutations affecting the ability of Escherichia coli Lrp to bind DNA, activate transcription, or respond to leucine. J. Bacteriol. 175: 1110-1117.
    • (1993) J. Bacteriol , vol.175 , pp. 1110-1117
    • Platko, J.V.1    Calvo, J.M.2
  • 58
    • 4544346067 scopus 로고    scopus 로고
    • Transcription regulation by the Mycobacterium tuberculosis alternative s factor SigD and its role in virulence
    • Raman, S., Hazra, R., Dascher, C.C., and Husson, R.N. 2004. Transcription regulation by the Mycobacterium tuberculosis alternative s factor SigD and its role in virulence. J. Bacteriol. 186: 6605-6616.
    • (2004) J. Bacteriol , vol.186 , pp. 6605-6616
    • Raman, S.1    Hazra, R.2    Dascher, C.C.3    Husson, R.N.4
  • 59
    • 37549022003 scopus 로고
    • Structure solution by iterative peaklist optimization and tangent expansion in space group P1
    • Sheldrick, G.M. and Gould, R.O. 1995. Structure solution by iterative peaklist optimization and tangent expansion in space group P1. Acta Crystallogr. B51: 432-446.
    • (1995) Acta Crystallogr , vol.B51 , pp. 432-446
    • Sheldrick, G.M.1    Gould, R.O.2
  • 60
    • 16644370432 scopus 로고    scopus 로고
    • Cloning, expression, purification and crystallization of a transcriptional regulatory protein (Rv3291c) from Mycobacterium tuberculosis H37Rv
    • Shrivastava, T., Kumar, S., and Ramachandran, R. 2004. Cloning, expression, purification and crystallization of a transcriptional regulatory protein (Rv3291c) from Mycobacterium tuberculosis H37Rv. Acta Crystallogr. D Biol. Crystallogr. 60: 1874-1876.
    • (2004) Acta Crystallogr. D Biol. Crystallogr , vol.60 , pp. 1874-1876
    • Shrivastava, T.1    Kumar, S.2    Ramachandran, R.3
  • 61
    • 1042302417 scopus 로고    scopus 로고
    • Structure and function of the feast/famine regulatory proteins, FFRPs
    • Suzuki, M. 2003. Structure and function of the feast/famine regulatory proteins, FFRPs. Proc. Jpn. Acad. 79B: 274-289.
    • (2003) Proc. Jpn. Acad , vol.79 B , pp. 274-289
    • Suzuki, M.1
  • 62
    • 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., and Matthews, R.G. 2002. Adaptation to famine: A family of stationary-phase genes revealed by microarray analysis. Proc. Natl. Acad. Sci. 99: 13471-13476.
    • (2002) Proc. Natl. Acad. Sci , vol.99 , pp. 13471-13476
    • Tani, T.H.1    Khodursky, A.2    Blumenthal, R.M.3    Brown, P.O.4    Matthews, R.G.5
  • 63
    • 0343340048 scopus 로고    scopus 로고
    • Bacillus subtilis LrpC is a sequence-independent DNA-binding and DNA-bending protein which bridges DNA
    • Tapias, A., López, G., and 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    López, G.2    Ayora, S.3
  • 66
    • 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, J.D., Higgins, D.G., and Gibson, T.J. 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
    • 3042838120 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis gene expression during adaptation to stationary phase and low-oxygen dormancy
    • Voskuil, M.I., Visconti, K.C., and Schoolnik, G.K. 2004. Mycobacterium tuberculosis gene expression during adaptation to stationary phase and low-oxygen dormancy. Tuberculosis (Edinb.) 84: 218-227.
    • (2004) Tuberculosis (Edinb.) , vol.84 , pp. 218-227
    • Voskuil, M.I.1    Visconti, K.C.2    Schoolnik, G.K.3
  • 69
    • 0027461910 scopus 로고
    • Lrp, a global regulatory protein of Escherichia coli, binds co-operatively to multiple sites and activates transcription of ilvIH
    • Wang, Q. and Calvo, J.M. 1993. Lrp, a global regulatory protein of Escherichia coli, binds co-operatively to multiple sites and activates transcription of ilvIH. J. Mol. Biol. 229: 306-318.
    • (1993) J. Mol. Biol , vol.229 , pp. 306-318
    • Wang, Q.1    Calvo, J.M.2
  • 70
    • 0028598544 scopus 로고
    • Sequence determinants of DNA bending in the ilvlH promoter and regulatory region of Escherichia coli
    • Wang, Q., Albert, F.G., Fitzgerald, D.J., Calvo, J.M., and Anderson, J.N. 1994. Sequence determinants of DNA bending in the ilvlH promoter and regulatory region of Escherichia coli. Nucleic Acids Res. 22: 5753-5760.
    • (1994) Nucleic Acids Res , vol.22 , pp. 5753-5760
    • Wang, Q.1    Albert, F.G.2    Fitzgerald, D.J.3    Calvo, J.M.4    Anderson, J.N.5
  • 71
    • 0029976980 scopus 로고    scopus 로고
    • An in vitro model for sequential study of shiftdown of Mycobacterium tuberculosis through two stages of non-replicating persistence
    • Wayne, L.G. and Hayes, L.G. 1996. An in vitro model for sequential study of shiftdown of Mycobacterium tuberculosis through two stages of non-replicating persistence. Infect. Immun. 64: 2062-2069.
    • (1996) Infect. Immun , vol.64 , pp. 2062-2069
    • Wayne, L.G.1    Hayes, L.G.2
  • 72
    • 0034780485 scopus 로고    scopus 로고
    • Nonreplicating persistence of Mycobacterium tuberculosis
    • Wayne, L.G. and Sohaskey, C.D. 2001. Nonreplicating persistence of Mycobacterium tuberculosis. Annu. Rev. Microbiol. 55: 139-163.
    • (2001) Annu. Rev. Microbiol , vol.55 , pp. 139-163
    • Wayne, L.G.1    Sohaskey, C.D.2
  • 73
    • 0032859398 scopus 로고    scopus 로고
    • Mutations enhancing amino acid catabolism confer a growth advantage in stationary phase
    • Zinser, E.R. and Kolter, R. 1999. Mutations enhancing amino acid catabolism confer a growth advantage in stationary phase. J. Bacteriol. 181: 5800-5807.
    • (1999) J. Bacteriol , vol.181 , pp. 5800-5807
    • Zinser, E.R.1    Kolter, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.