메뉴 건너뛰기




Volumn 152, Issue 12, 2006, Pages 3585-3594

Involvement of the arginine repressor in lysine biosynthesis of Thermus thermophilus

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA GALACTOSIDASE; ARGININE; BACTERIAL DNA; BACTERIAL PROTEIN; GLOBAL ARGININE REGULATOR PROTEIN; LYSINE; ORNITHINE; UNCLASSIFIED DRUG;

EID: 33846009421     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.29222-0     Document Type: Article
Times cited : (7)

References (40)
  • 1
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72, 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 2
    • 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
  • 3
    • 2342529094 scopus 로고    scopus 로고
    • Arginine regulation in Thermotoga neapolitana and Thermotoga maritima
    • Charlier, D. (2004). Arginine regulation in Thermotoga neapolitana and Thermotoga maritima. Biochem Soc Trans 32, 310-313.
    • (2004) Biochem Soc Trans , vol.32 , pp. 310-313
    • Charlier, D.1
  • 4
    • 0026742139 scopus 로고
    • Arginine regulon of Escherichia coli K-12. A study of repressor-operator interactions and of in vitro binding affinities versus in vivo repression
    • Charlier, D., Roovers, M., Van Vliet, F., Boyen, A., Cunin, R., Nakamura, Y., Glansdorff, N. & Pierard, A. (11992). Arginine regulon of Escherichia coli K-12. A study of repressor-operator interactions and of in vitro binding affinities versus in vivo repression. J Mol Biol 226, 367-386.
    • (1992) J Mol Biol , vol.226 , pp. 367-386
    • Charlier, D.1    Roovers, M.2    Van Vliet, F.3    Boyen, A.4    Cunin, R.5    Nakamura, Y.6    Glansdorff, N.7    Pierard, A.8
  • 5
    • 0026529106 scopus 로고
    • Purification and initial characterization of AhrC: The regulator of arginine metabolism genes in Bacillus subtilis
    • Czaplewski, L. G., North, A. K., Smith, M. C., Baumberg, S. & Stockley, P. G. (1992). Purification and initial characterization of AhrC: the regulator of arginine metabolism genes in Bacillus subtilis. Mol Microbiol 6, 267-275.
    • (1992) Mol Microbiol , vol.6 , pp. 267-275
    • Czaplewski, L.G.1    North, A.K.2    Smith, M.C.3    Baumberg, S.4    Stockley, P.G.5
  • 6
    • 0014789268 scopus 로고
    • Arginaseless Neurospora: Genetics, physiology, and polyamine synthesis
    • Davis, R. H., Lawless, M. B. & Port, L. A. (1970). Arginaseless Neurospora: genetics, physiology, and polyamine synthesis. J Bacteriol 102, 299-305.
    • (1970) J Bacteriol , vol.102 , pp. 299-305
    • Davis, R.H.1    Lawless, M.B.2    Port, L.A.3
  • 7
    • 0033826224 scopus 로고    scopus 로고
    • Thermostability, oligomerization and DNA-binding properties of the regulatory protein ArgR from the hyperthermophilic bacterium Thermotoga neapolitana
    • Dimova, D., Weigel, P., Takahashi, M., Marc, F., Van Duyne, G. D. & Sakanyan, V. (2000). Thermostability, oligomerization and DNA-binding properties of the regulatory protein ArgR from the hyperthermophilic bacterium Thermotoga neapolitana. Mol Gen Genet 263, 119-130.
    • (2000) Mol Gen Genet , vol.263 , pp. 119-130
    • Dimova, D.1    Weigel, P.2    Takahashi, M.3    Marc, F.4    Van Duyne, G.D.5    Sakanyan, V.6
  • 8
    • 0030791466 scopus 로고    scopus 로고
    • The highly thermostable arginine repressor of Bacillus stearothermophilus: Gene cloning and repressor-operator interactions
    • Dion, M., Charlier, D., Wang, H., Gigot, D., Savchenko, A., Hallet, J. N., Glansdorff, N. & Sakanyan, V. (1997). The highly thermostable arginine repressor of Bacillus stearothermophilus: gene cloning and repressor-operator interactions. Mol Microbiol 25, 385-398.
    • (1997) Mol Microbiol , vol.25 , pp. 385-398
    • Dion, M.1    Charlier, D.2    Wang, H.3    Gigot, D.4    Savchenko, A.5    Hallet, J.N.6    Glansdorff, N.7    Sakanyan, V.8
  • 9
    • 0035462375 scopus 로고    scopus 로고
    • Production of recombinant α-galactosidases in Thermus thermophilus
    • Fridjonsson, O. & Mattes, R. (2001). Production of recombinant α-galactosidases in Thermus thermophilus. Appl Environ Microbiol 67, 4192-4198.
    • (2001) Appl Environ Microbiol , vol.67 , pp. 4192-4198
    • Fridjonsson, O.1    Mattes, R.2
  • 10
    • 0036267346 scopus 로고    scopus 로고
    • Thermoadaptation of α-galactosidase AgaB1 in Thermus thermophilus
    • Fridjonsson, O., Watzlawick, H. & Mattes, R. (2002). Thermoadaptation of α-galactosidase AgaB1 in Thermus thermophilus. J Bacteriol 184, 3385-3391.
    • (2002) J Bacteriol , vol.184 , pp. 3385-3391
    • Fridjonsson, O.1    Watzlawick, H.2    Mattes, R.3
  • 11
    • 2342586677 scopus 로고    scopus 로고
    • The genome sequence of the extreme thermophile Thermus thermophilus
    • 17 other authors
    • Henne, A., Bruggemann, H., Raasch, C. & 17 other authors (2004). The genome sequence of the extreme thermophile Thermus thermophilus. Nat Biotechnol 22, 547-553.
    • (2004) Nat Biotechnol , vol.22 , pp. 547-553
    • Henne, A.1    Bruggemann, H.2    Raasch, C.3
  • 12
    • 0028471169 scopus 로고
    • The entire population of Thermus thermophilus cells is always competent at any growth phase
    • Hidaka, Y., Hasegawa, M., Nakahara, T. & Hoshino, T. (1994). The entire population of Thermus thermophilus cells is always competent at any growth phase. Biosci Biotechnol Biochem 58, 1338-1339.
    • (1994) Biosci Biotechnol Biochem , vol.58 , pp. 1338-1339
    • Hidaka, Y.1    Hasegawa, M.2    Nakahara, T.3    Hoshino, T.4
  • 13
    • 0033014075 scopus 로고    scopus 로고
    • Probing activation of the prokaryotic arginine transcriptional regulator using chimeric proteins
    • Holtham, C. A., Jumel, K., Miller, C. M., Harding, S. E., Baumberg, S. & Stockley, P. G. (1999). Probing activation of the prokaryotic arginine transcriptional regulator using chimeric proteins. J Mol Biol 289, 707-727.
    • (1999) J Mol Biol , vol.289 , pp. 707-727
    • Holtham, C.A.1    Jumel, K.2    Miller, C.M.3    Harding, S.E.4    Baumberg, S.5    Stockley, P.G.6
  • 14
    • 0032989249 scopus 로고    scopus 로고
    • Aspartate kinase-independent lysine synthesis in an extremely thermophilic bacterium, Thermus thermophilus: Lysine is synthesized via α-aminoadipic acid not via diaminopimelic acid
    • Kobashi, N., Nishiyama, M. & Tanokura, M. (1999). Aspartate kinase-independent lysine synthesis in an extremely thermophilic bacterium, Thermus thermophilus: lysine is synthesized via α-aminoadipic acid not via diaminopimelic acid. J Bacteriol 181, 1713-1718.
    • (1999) J Bacteriol , vol.181 , pp. 1713-1718
    • Kobashi, N.1    Nishiyama, M.2    Tanokura, M.3
  • 15
    • 0033393823 scopus 로고    scopus 로고
    • The α-aminoadipate pathway for lysine biosynthesis is widely distributed among Thermus strains
    • Kosuge, T. & Hoshino, T. (1999). The α-aminoadipate pathway for lysine biosynthesis is widely distributed among Thermus strains. J Biosci Bioeng 88, 672-675.
    • (1999) J Biosci Bioeng , vol.88 , pp. 672-675
    • Kosuge, T.1    Hoshino, T.2
  • 16
    • 0022448655 scopus 로고
    • Genetic transformation of the extreme thermophile Thermus thermophilus and of other Thermus spp
    • Koyama, Y., Hoshino, T., Tomizuka, N. & Furukawa, K. (1986). Genetic transformation of the extreme thermophile Thermus thermophilus and of other Thermus spp. J Bacteriol 166, 338-340.
    • (1986) J Bacteriol , vol.166 , pp. 338-340
    • Koyama, Y.1    Hoshino, T.2    Tomizuka, N.3    Furukawa, K.4
  • 17
    • 1142286472 scopus 로고    scopus 로고
    • ArgR and AhrC are both required for regulation of arginine metabolism in Lactococcus lactis
    • Larsen, R., Buist G., Kulpers, O. P. & Kok, J. (2004). ArgR and AhrC are both required for regulation of arginine metabolism in Lactococcus lactis. J Bacteriol 186, 1147-1157.
    • (2004) J Bacteriol , vol.186 , pp. 1147-1157
    • Larsen, R.1    Buist, G.2    Kulpers, O.P.3    Kok, J.4
  • 18
    • 21444458953 scopus 로고    scopus 로고
    • Interaction between ArgR and AhrC controls regulation of arginine metabolism in Lactococcus lactis
    • Larsen, R., Kok, J. & Kulpers, O. P. (2005). Interaction between ArgR and AhrC controls regulation of arginine metabolism in Lactococcus lactis. J Biol Chem 280, 19319-19330.
    • (2005) J Biol Chem , vol.280 , pp. 19319-19330
    • Larsen, R.1    Kok, J.2    Kulpers, O.P.3
  • 19
    • 0033537677 scopus 로고    scopus 로고
    • The dual biosynthetic capability of N-acetylornithine aminotransferase in arginine and lysine biosynthesis
    • Ledwidge, R. & Blanchard, J. S. (1999). The dual biosynthetic capability of N-acetylornithine aminotransferase in arginine and lysine biosynthesis. Biochemistry 38, 3019-3024.
    • (1999) Biochemistry , vol.38 , pp. 3019-3024
    • Ledwidge, R.1    Blanchard, J.S.2
  • 20
    • 0342367772 scopus 로고
    • Isolation of a thermostable enzyme variant by cloning and selection in a thermophile
    • Liao, H., McKenzie, T. & Hageman, R. (1986). Isolation of a thermostable enzyme variant by cloning and selection in a thermophile. Proc Natl Acad Sci U S A 83, 576-580.
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 576-580
    • Liao, H.1    McKenzie, T.2    Hageman, R.3
  • 21
    • 0023431902 scopus 로고
    • Nucleotide sequence of the argR gene of Escherichia coli K-12 and isolation of its product, the arginine repressor
    • Lim, D. B., Oppenheim, J. D., Eckhardt, T. & Maas, W. K. (1987). Nucleotide sequence of the argR gene of Escherichia coli K-12 and isolation of its product, the arginine repressor. Proc Natl Acad Sci U S A 84, 6697-6701.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 6697-6701
    • Lim, D.B.1    Oppenheim, J.D.2    Eckhardt, T.3    Maas, W.K.4
  • 22
    • 1842425623 scopus 로고    scopus 로고
    • Functional analysis of the small subunit of the putative homoaconitase from Pyrococcus horikoshii in the Thermus lysine biosynthetic pathway
    • Lombo, T., Takaya, N., Miyazaki, J., Gotoh, K., Nishiyama, M., Kosuge, T., Nakamura, A. & Hoshino, T. (2004). Functional analysis of the small subunit of the putative homoaconitase from Pyrococcus horikoshii in the Thermus lysine biosynthetic pathway. FEMS Microbiol Lett 233, 315-324.
    • (2004) FEMS Microbiol Lett , vol.233 , pp. 315-324
    • Lombo, T.1    Takaya, N.2    Miyazaki, J.3    Gotoh, K.4    Nishiyama, M.5    Kosuge, T.6    Nakamura, A.7    Hoshino, T.8
  • 23
    • 0026582272 scopus 로고
    • Characterization of the arginine repressor from Salmonella typhimurium and its interactions with the carAB operator
    • Lu, C. D., Houghton, J. E. & Abdelal, A. T. (1992). Characterization of the arginine repressor from Salmonella typhimurium and its interactions with the carAB operator. J Mol Biol 225, 11-24.
    • (1992) J Mol Biol , vol.225 , pp. 11-24
    • Lu, C.D.1    Houghton, J.E.2    Abdelal, A.T.3
  • 24
    • 0031875854 scopus 로고    scopus 로고
    • Development of expression vectors for Thermus thermophilus
    • Masada, H. & Hoshino, T. (1998). Development of expression vectors for Thermus thermophilus. J Ferment Bioeng 86, 121-124.
    • (1998) J Ferment Bioeng , vol.86 , pp. 121-124
    • Masada, H.1    Hoshino, T.2
  • 25
    • 0034891272 scopus 로고    scopus 로고
    • Functional and evolutionary relationship between arginine biosynthesis and prokaryotic lysine biosynthesis through α-aminoadipate
    • Miyazaki, J., Kobashi, N., Nishiyama, M. & Yamane, H. (2001). Functional and evolutionary relationship between arginine biosynthesis and prokaryotic lysine biosynthesis through α-aminoadipate. J Bacteriol 183, 5067-5073.
    • (2001) J Bacteriol , vol.183 , pp. 5067-5073
    • Miyazaki, J.1    Kobashi, N.2    Nishiyama, M.3    Yamane, H.4
  • 26
    • 0037070156 scopus 로고    scopus 로고
    • Characterization of a lysK gene as an argE homolog in Thermus thermophilus HB27
    • Miyazaki, J., Kobashi, N., Fujii, T., Nishiyama, M. & Yamane, H. (2002). Characterization of a lysK gene as an argE homolog in Thermus thermophilus HB27. FEBS Lett 512, 269-274.
    • (2002) FEBS Lett , vol.512 , pp. 269-274
    • Miyazaki, J.1    Kobashi, N.2    Fujii, T.3    Nishiyama, M.4    Yamane, H.5
  • 27
    • 0037449765 scopus 로고    scopus 로고
    • Characterization of homoisocitrate dehydrogenase involved in lysine biosynthesis of an extremely thermophilic bacterium, Thermus thermophilus HB27, and evolutionary implication of β-decarboxylating dehydrogenase
    • Miyazaki, J., Kobashi, N., Nishiyama, M. & Yamane, H. (2003). Characterization of homoisocitrate dehydrogenase involved in lysine biosynthesis of an extremely thermophilic bacterium, Thermus thermophilus HB27, and evolutionary implication of β-decarboxylating dehydrogenase. J Biol Chem 278, 1864-1871.
    • (2003) J Biol Chem , vol.278 , pp. 1864-1871
    • Miyazaki, J.1    Kobashi, N.2    Nishiyama, M.3    Yamane, H.4
  • 28
    • 4344635690 scopus 로고    scopus 로고
    • α-Aminoadipate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus
    • Miyazaki, T., Miyazaki, J., Yamane, H. & Nishiyama, M. (2004). α-Aminoadipate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus. Microbiology 150, 2327-2334.
    • (2004) Microbiology , vol.150 , pp. 2327-2334
    • Miyazaki, T.1    Miyazaki, J.2    Yamane, H.3    Nishiyama, M.4
  • 29
    • 0042736857 scopus 로고    scopus 로고
    • Hyperthermophilic Thermotoga arginine repressor binding to full-length cognate and heterologous arginine operators and to half-site targets
    • Morin, A., Huysveld, N., Braun, F., Dimova, D., Sakanyan, V. & Charlier, D. (2003). Hyperthermophilic Thermotoga arginine repressor binding to full-length cognate and heterologous arginine operators and to half-site targets. J Mol Biol 332, 537-553.
    • (2003) J Mol Biol , vol.332 , pp. 537-553
    • Morin, A.1    Huysveld, N.2    Braun, F.3    Dimova, D.4    Sakanyan, V.5    Charlier, D.6
  • 30
    • 27644459857 scopus 로고    scopus 로고
    • In vivo directed evolution for thermostabilization of Escherichia coli hygromycin B phosphotransferase and the use of the gene as a selection marker in the host-vector system of Thermus thermophilus
    • Nakamura, A., Takakura, Y., Kobayashi, H. & Hoshino, T. (2005). In vivo directed evolution for thermostabilization of Escherichia coli hygromycin B phosphotransferase and the use of the gene as a selection marker in the host-vector system of Thermus thermophilus. J Biosci Bioeng 100, 158-163.
    • (2005) J Biosci Bioeng , vol.100 , pp. 158-163
    • Nakamura, A.1    Takakura, Y.2    Kobayashi, H.3    Hoshino, T.4
  • 32
    • 0033404080 scopus 로고    scopus 로고
    • A prokaryotic gene cluster involved in synthesis of lysine through the amino adipate pathway: A key to the evolution of amino acid biosynthesis
    • Nishida, H., Nishiyama, M., Kobashi, N., Kosuge, T., Hoshino, T. & Yamane, H. (1999). A prokaryotic gene cluster involved in synthesis of lysine through the amino adipate pathway: a key to the evolution of amino acid biosynthesis. Genome Res 9, 1175-1183.
    • (1999) Genome Res , vol.9 , pp. 1175-1183
    • Nishida, H.1    Nishiyama, M.2    Kobashi, N.3    Kosuge, T.4    Hoshino, T.5    Yamane, H.6
  • 34
    • 0033819383 scopus 로고    scopus 로고
    • Organization and expression of a Thermus thermophilus arginine duster: Presence of unidentified open reading frames and absence of a Shine-Dalgarno sequence
    • Sanchez, R., Roovers, M. & Glansdorff, N. (2000). Organization and expression of a Thermus thermophilus arginine duster: presence of unidentified open reading frames and absence of a Shine-Dalgarno sequence. J Bacteriol 182, 5911-5915.
    • (2000) J Bacteriol , vol.182 , pp. 5911-5915
    • Sanchez, R.1    Roovers, M.2    Glansdorff, N.3
  • 35
    • 0028053275 scopus 로고
    • Explanation for different types of regulation of arginine biosynthesis in Escherichia coli B and Escherichia coli K12 caused by a difference between their arginine repressors
    • Tian, G., Lim, D., Oppenheim, J. D. & Maas, W. K. (1994). Explanation for different types of regulation of arginine biosynthesis in Escherichia coli B and Escherichia coli K12 caused by a difference between their arginine repressors. J Mol Biol 235, 221-230.
    • (1994) J Mol Biol , vol.235 , pp. 221-230
    • Tian, G.1    Lim, D.2    Oppenheim, J.D.3    Maas, W.K.4
  • 36
  • 37
    • 0029670095 scopus 로고    scopus 로고
    • Structure of the oligomerization and L-arginine binding domain of the arginine repressor of Escherichia coli
    • Van Duyne, G. D., Ghosh, G., Maas, W. K. & Sigler, P. B. (1996). Structure of the oligomerization and L-arginine binding domain of the arginine repressor of Escherichia coli. J Mol Biol 256, 377-391.
    • (1996) J Mol Biol , vol.256 , pp. 377-391
    • Van Duyne, G.D.1    Ghosh, G.2    Maas, W.K.3    Sigler, P.B.4
  • 38
    • 0025300402 scopus 로고
    • Towards a natural system of organisms: Proposal for the domains Archaea, Bacteria, and Eucarya
    • Woese, C. R., Kandler, O. & Wheelis, M. L. (1990). Towards a natural system of organisms: proposal for the domains Archaea, Bacteria, and Eucarya. Proc Natl Acad Sci U S A 87, 4576-4579.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 4576-4579
    • Woese, C.R.1    Kandler, O.2    Wheelis, M.L.3
  • 39
    • 0037014672 scopus 로고    scopus 로고
    • Characterization of bacterial homocitrate synthase involved in lysine biosynthesis
    • Wulandari, A. P., Miyazaki, J., Kobashi, N., Nishiyama, M., Hoshino, T. & Yamane, H. (2002). Characterization of bacterial homocitrate synthase involved in lysine biosynthesis. FEBS Lett 522, 35-40.
    • (2002) FEBS Lett , vol.522 , pp. 35-40
    • Wulandari, A.P.1    Miyazaki, J.2    Kobashi, N.3    Nishiyama, M.4    Hoshino, T.5    Yamane, H.6
  • 40
    • 0037436334 scopus 로고    scopus 로고
    • Regulation of arginine biosynthesis in the psychropiezophilic bacterium Moritella profunda: In vivo repressibility and in vitro repressor-operator contact probing
    • Xu, Y., Sun, Y., Huysveld, N., Gigot, D., Glansdorff, N. & Charlier, D. (2003). Regulation of arginine biosynthesis in the psychropiezophilic bacterium Moritella profunda: in vivo repressibility and in vitro repressor-operator contact probing. J Mol Biol 326, 353-369.
    • (2003) J Mol Biol , vol.326 , pp. 353-369
    • Xu, Y.1    Sun, Y.2    Huysveld, N.3    Gigot, D.4    Glansdorff, N.5    Charlier, D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.