메뉴 건너뛰기




Volumn 222, Issue 1, 1998, Pages 125-132

The organization of the leuC, leuD and leuB genes of the extreme thermophile Thermus thermophilus

Author keywords

Complementation analysis; Isopropylmalate dehydrogenase; Isopropylmalate isomerase; Leucine biosynthetic pathway; Sequence analysis

Indexed keywords

ACONITATE HYDRATASE; CYSTEINE; IRON SULFUR PROTEIN; ISOMERASE; LEUCINE; MALATE DEHYDROGENASE; MALIC ACID DERIVATIVE;

EID: 0032487743     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(98)00482-X     Document Type: Article
Times cited : (18)

References (39)
  • 1
    • 0029908683 scopus 로고    scopus 로고
    • Spontaneous tandem sequence duplications reverse the thermal stability of carboxyl-terminal modified 3-isopropylmalate dehydrogenase
    • Akanuma, S., Yamagishi, A., Tanaka, N., Oshima, T., 1996. Spontaneous tandem sequence duplications reverse the thermal stability of carboxyl-terminal modified 3-isopropylmalate dehydrogenase. J. Bacteriol. 178, 6300-6304.
    • (1996) J. Bacteriol. , vol.178 , pp. 6300-6304
    • Akanuma, S.1    Yamagishi, A.2    Tanaka, N.3    Oshima, T.4
  • 2
    • 0027024023 scopus 로고
    • PBluescriptII: Multifunctional cloning and mapping vectors
    • Alting-Mees, M.A., Sorge, J.A., Short, J.M., 1992. pBluescriptII: multifunctional cloning and mapping vectors. Methods Enzymol. 216, 483-495.
    • (1992) Methods Enzymol. , vol.216 , pp. 483-495
    • Alting-Mees, M.A.1    Sorge, J.A.2    Short, J.M.3
  • 3
    • 0031013857 scopus 로고    scopus 로고
    • A novel genetic organization: The leuA-rpoD1 locus in the cyanobacterium Microcystis aerunginosa K-81
    • Asayama, M., Kabasawa, M., Shirai, M., 1997. A novel genetic organization: the leuA-rpoD1 locus in the cyanobacterium Microcystis aerunginosa K-81. Biochim. Biophys. Acta 1350, 15-20.
    • (1997) Biochim. Biophys. Acta , vol.1350 , pp. 15-20
    • Asayama, M.1    Kabasawa, M.2    Shirai, M.3
  • 4
    • 0016687810 scopus 로고
    • Purification of yeast alpha-isopropylmalate isomerase. High ionic strength hydrophobic chromatography
    • Bigelis, R., Umbarger, H.E., 1975. Purification of yeast alpha-isopropylmalate isomerase. High ionic strength hydrophobic chromatography. J. Biol. Chem. 250, 4315-4321.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4315-4321
    • Bigelis, R.1    Umbarger, H.E.2
  • 6
    • 0023504697 scopus 로고
    • Expression of leucine genes from an extremely thermophilic bacterium in Escherichia coli
    • Croft, J.E., Love, D.R., Bergquist, P.L., 1987. Expression of leucine genes from an extremely thermophilic bacterium in Escherichia coli. Mol. Gen. Genet. 210, 490-497.
    • (1987) Mol. Gen. Genet. , vol.210 , pp. 490-497
    • Croft, J.E.1    Love, D.R.2    Bergquist, P.L.3
  • 7
    • 0027251531 scopus 로고
    • Cloning and analysis of the leuB gene of Leptospira interrogans serovar pomona
    • Ding, M., Yelton, D.B., 1993. Cloning and analysis of the leuB gene of Leptospira interrogans serovar pomona. J. Gen. Microbiol. 139, 1093-1103.
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 1093-1103
    • Ding, M.1    Yelton, D.B.2
  • 8
    • 0019781166 scopus 로고
    • Wild-type isopropylmalate isomerase in Salmonella typhimurium is composed of two different subunits
    • Fultz, P.N., Kemper, J., 1981. Wild-type isopropylmalate isomerase in Salmonella typhimurium is composed of two different subunits. J. Bacteriol. 148, 210-219.
    • (1981) J. Bacteriol. , vol.148 , pp. 210-219
    • Fultz, P.N.1    Kemper, J.2
  • 9
    • 0018668988 scopus 로고
    • Leu operon of Salmonella typhimurium is controlled by an attenuation mechanism
    • Gemmill, R.M., Wessler, S.R., Keller, E.B., Calvo, J.M., 1979. leu operon of Salmonella typhimurium is controlled by an attenuation mechanism. Proc. Nat. Acad. Sci. USA 76, 4941-4945.
    • (1979) Proc. Nat. Acad. Sci. USA , vol.76 , pp. 4941-4945
    • Gemmill, R.M.1    Wessler, S.R.2    Keller, E.B.3    Calvo, J.M.4
  • 10
    • 0026781514 scopus 로고
    • Branched-chain amino acid biosynthesis genes in Lactococcus lactis subsp. lactis
    • Godon, J.J., Chopin, M.C., Ehrlich, S.D., 1992. Branched-chain amino acid biosynthesis genes in Lactococcus lactis subsp. lactis. J. Bacteriol. 174, 6580-6589.
    • (1992) J. Bacteriol. , vol.174 , pp. 6580-6589
    • Godon, J.J.1    Chopin, M.C.2    Ehrlich, S.D.3
  • 11
    • 0025865421 scopus 로고
    • Homology between IRE-BP, a regulatory RNA-binding protein, aconitase, and isopropylmalate isomerase
    • Hentze, M.W., Argos, P., 1991. Homology between IRE-BP, a regulatory RNA-binding protein, aconitase, and isopropylmalate isomerase. Nucleic Acids Res. 19, 1739-1740.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 1739-1740
    • Hentze, M.W.1    Argos, P.2
  • 12
    • 0027293814 scopus 로고
    • Molecular cloning and sequence analysis of crtB gene of Thermus thermophilus HB27, an extreme thermophile producing carotenoid pigments
    • Hoshino, T., Fujii, R., Nakahara, T., 1993. Molecular cloning and sequence analysis of crtB gene of Thermus thermophilus HB27, an extreme thermophile producing carotenoid pigments. Appl. Environ. Microbiol. 59, 3150-3153.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 3150-3153
    • Hoshino, T.1    Fujii, R.2    Nakahara, T.3
  • 13
    • 0021326794 scopus 로고
    • High guanine plus cytosine content in the third letter of codons of an extreme thermophile. DNA sequence of the isopropylmalate dehydrogenase of Thermus thermophilus
    • Kagawa, Y., Nojima, H., Nukiwa, N., Ishizuka, M., Nakajima, T., Yasuhara, T., Tanaka, T., Oshima, T., 1984. High guanine plus cytosine content in the third letter of codons of an extreme thermophile. DNA sequence of the isopropylmalate dehydrogenase of Thermus thermophilus. J. Biol. Chem. 259, 2956-2960.
    • (1984) J. Biol. Chem. , vol.259 , pp. 2956-2960
    • Kagawa, Y.1    Nojima, H.2    Nukiwa, N.3    Ishizuka, M.4    Nakajima, T.5    Yasuhara, T.6    Tanaka, T.7    Oshima, T.8
  • 14
    • 0025761731 scopus 로고
    • Molecular cloning and nucleotide sequence of 3-isopropylmalate dehydrogenase gene (leuB) from an extreme thermophile, Thermus aquaticus YT-1
    • Tokyo
    • Kirino, H., Oshima, T., 1991. Molecular cloning and nucleotide sequence of 3-isopropylmalate dehydrogenase gene (leuB) from an extreme thermophile, Thermus aquaticus YT-1. J. Biochem. (Tokyo) 109, 852-857.
    • (1991) J. Biochem. , vol.109 , pp. 852-857
    • Kirino, H.1    Oshima, T.2
  • 15
    • 0028091179 scopus 로고
    • Hydrophobic interaction at the subunit interface contributes to the thermostability of 3-isopropylmalate dehydrogenase from an extreme thermophile, Thermus thermophilus
    • Kirino, H., Aoki, M., Aoshima, M., Hayashi, Y., Ohba, M., Yamagishi, A., Wakagi, T., Oshima, T., 1994. Hydrophobic interaction at the subunit interface contributes to the thermostability of 3-isopropylmalate dehydrogenase from an extreme thermophile, Thermus thermophilus. Eur. J. Biochem. 220, 275-281.
    • (1994) Eur. J. Biochem. , vol.220 , pp. 275-281
    • Kirino, H.1    Aoki, M.2    Aoshima, M.3    Hayashi, Y.4    Ohba, M.5    Yamagishi, A.6    Wakagi, T.7    Oshima, T.8
  • 16
    • 0028170967 scopus 로고
    • Molecular cloning and sequence analysis of the proBA operon from an extremely thermophilic eubacterium Thermus thermophilus
    • Kosuge, T., Tabata, K., Hoshino, T., 1994. Molecular cloning and sequence analysis of the proBA operon from an extremely thermophilic eubacterium Thermus thermophilus. FEMS Microbiol. Lett. 123, 55-61.
    • (1994) FEMS Microbiol. Lett. , vol.123 , pp. 55-61
    • Kosuge, T.1    Tabata, K.2    Hoshino, T.3
  • 17
    • 0025297256 scopus 로고
    • Cloning and sequence analysis of tryptophan synthetase genes of an extreme thermophile, Thermus thermophilus HB27: Plasmid transfer from replica-plated Escherichia coli recombinant colonies to competent T. thermophilus cells
    • Koyama, Y., Furukawa, K., Cloning and sequence analysis of tryptophan synthetase genes of an extreme thermophile, Thermus thermophilus HB27: plasmid transfer from replica-plated Escherichia coli recombinant colonies to competent T. thermophilus cells. 1990. J. Bacteriol. 172, 3490-3495.
    • (1990) Bacteriol. , vol.172 , pp. 3490-3495
    • Koyama, Y.1    Furukawa, K.2
  • 18
    • 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
  • 19
    • 2642699794 scopus 로고
    • Rapid and efficient site-specific mutagensis without phenotypic selection
    • Kunkel, T.A., 1985. Rapid and efficient site-specific mutagensis without phenotypic selection. Proc. Nat. Acad. Sci. USA 82, 488-492.
    • (1985) Proc. Nat. Acad. Sci. USA , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 20
    • 0030928486 scopus 로고    scopus 로고
    • Characterization and mutagensis of the leucine biosynthetic genes of Azotobacter vinelandii: An analysis of the rarity of amino acid auxotrophs
    • Manna, A.C., Das, H.K., 1997. Characterization and mutagensis of the leucine biosynthetic genes of Azotobacter vinelandii: an analysis of the rarity of amino acid auxotrophs. Mol. Gen. Genet. 254, 207-217.
    • (1997) Mol. Gen. Genet. , vol.254 , pp. 207-217
    • Manna, A.C.1    Das, H.K.2
  • 21
    • 0345139390 scopus 로고
    • Genetic fine structure of the leucine operon in Salmonella
    • Margolin, P., 1963. Genetic fine structure of the leucine operon in Salmonella. Genetics 48, 441-457.
    • (1963) Genetics , vol.48 , pp. 441-457
    • Margolin, P.1
  • 23
    • 0018962052 scopus 로고
    • Cloning and expression of the leucine gene from Thermus thermophilus in Escherichia coli
    • Nagahari, K., Koshikawa, T., Sakaguchi, K., 1980. Cloning and expression of the leucine gene from Thermus thermophilus in Escherichia coli. Gene 10, 137-145.
    • (1980) Gene , vol.10 , pp. 137-145
    • Nagahari, K.1    Koshikawa, T.2    Sakaguchi, K.3
  • 24
    • 0025729531 scopus 로고
    • Methionyl-tRNA synthetase gene from an extreme thermophile, Thermus thermophilus HB8. Molecular cloning, primary-structure analysis, expression in Escherichia coli, and site-directed mutagenesis
    • Nureki, O., Muramatsu, T., Suzuki, K., Kohda, D., Matsuzawa, H., Ohta, T., Miyazawa, T., Yokoyama, S., Methionyl-tRNA synthetase gene from an extreme thermophile, Thermus thermophilus HB8. Molecular cloning, primary-structure analysis, expression in Escherichia coli, and site-directed mutagenesis. 1991. J. Biol. Chem. 266, 3268-3277.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3268-3277
    • Nureki, O.1    Muramatsu, T.2    Suzuki, K.3    Kohda, D.4    Matsuzawa, H.5    Ohta, T.6    Miyazawa, T.7    Yokoyama, S.8
  • 25
    • 0019253694 scopus 로고
    • Translational coupling during expression of the tryptophan operon of Escherichia coli
    • Oppenheim, D.S., Yanofsky, C., 1980. Translational coupling during expression of the tryptophan operon of Escherichia coli. Genetics 95, 785-795.
    • (1980) Genetics , vol.95 , pp. 785-795
    • Oppenheim, D.S.1    Yanofsky, C.2
  • 26
    • 0026517563 scopus 로고
    • The aconitase of Escherichia coli. Nucleotide sequence of the aconitase gene and amino acid sequence similarity with mitochondrial aconitases, the iron-responsive-element-binding protein and isopropylmalate isomerases
    • Prodromou, C., Artymiuk, P. J., Guest, J.R., The aconitase of Escherichia coli. Nucleotide sequence of the aconitase gene and amino acid sequence similarity with mitochondrial aconitases, the iron-responsive-element-binding protein and isopropylmalate isomerases. 1992. Eur. J. Biochem. 204, 599-609.
    • (1992) Eur. J. Biochem. , vol.204 , pp. 599-609
    • Prodromou, C.1    Artymiuk, P.J.2    Guest, J.R.3
  • 27
    • 0017855941 scopus 로고
    • Structural features of normal and complemented forms of Neurospora isopropylmalate isomerase
    • Reichenbecher, V.J., Gross, S.R., 1978. Structural features of normal and complemented forms of Neurospora isopropylmalate isomerase. J. Bacteriol. 133, 802-810.
    • (1978) J. Bacteriol. , vol.133 , pp. 802-810
    • Reichenbecher, V.J.1    Gross, S.R.2
  • 30
    • 0015591150 scopus 로고
    • Genetic fine structure of the leucine operon of Escherichia coli K-12
    • Somers, J.M., Amzallag, A., Middleton, R.B., 1973. Genetic fine structure of the leucine operon of Escherichia coli K-12. J. Bacteriol. 113, 1268-1272.
    • (1973) J. Bacteriol. , vol.113 , pp. 1268-1272
    • Somers, J.M.1    Amzallag, A.2    Middleton, R.B.3
  • 31
    • 0030794064 scopus 로고
    • Screening of a mutant plasmid with high expression efficiency of GC-rich leuB gene of an extreme thermophile, Thermus thermophilus, in Escherichia coli
    • Tokyo
    • Suzuki, T., Tanaka, Y., Ishida, M., Ishizuka, M., Yamagishi, A., Oshima, T., 1977. Screening of a mutant plasmid with high expression efficiency of GC-rich leuB gene of an extreme thermophile, Thermus thermophilus, in Escherichia coli. J. Biochem. (Tokyo) 121, 1031-1034.
    • (1977) J. Biochem. , vol.121 , pp. 1031-1034
    • Suzuki, T.1    Tanaka, Y.2    Ishida, M.3    Ishizuka, M.4    Yamagishi, A.5    Oshima, T.6
  • 33
    • 0029154808 scopus 로고
    • Screening of stable proteins in an extreme thermophile, Thermus thermophilus
    • Tamakoshi, M., Yamagishi, A., Oshima, T., 1995. Screening of stable proteins in an extreme thermophile, Thermus thermophilus. Mol. Microbiol. 16, 1031-1036.
    • (1995) Mol. Microbiol. , vol.16 , pp. 1031-1036
    • Tamakoshi, M.1    Yamagishi, A.2    Oshima, T.3
  • 35
    • 0019510613 scopus 로고
    • Cloning of 3-isopropylmalate dehydrogenase gene of an extreme thermophile and partial purification of the gene product
    • Tokyo
    • Tanaka, T., Kawano, N., Oshima, T., 1981. Cloning of 3-isopropylmalate dehydrogenase gene of an extreme thermophile and partial purification of the gene product. J. Biochem. (Tokyo) 89, 677-682.
    • (1981) J. Biochem. , vol.89 , pp. 677-682
    • Tanaka, T.1    Kawano, N.2    Oshima, T.3
  • 36
    • 0023634094 scopus 로고
    • Production of single-stranded plasmid DNA
    • Vieira, J., Messing, J., 1987. Production of single-stranded plasmid DNA. Methods Enzymol. 153, 3-11.
    • (1987) Methods Enzymol. , vol.153 , pp. 3-11
    • Vieira, J.1    Messing, J.2
  • 37
    • 0023644668 scopus 로고
    • Thermal destruction processes in proteins involving cystine residues
    • Volkin, D.B., Klibanov, A.M., 1987. Thermal destruction processes in proteins involving cystine residues. J. Biol. Chem. 262, 2945-2950.
    • (1987) J. Biol. Chem. , vol.262 , pp. 2945-2950
    • Volkin, D.B.1    Klibanov, A.M.2
  • 38
    • 0015805577 scopus 로고
    • Genetic studies of leucine biosynthesis in Bacillus subtilis
    • Ward, J.J., Zahler, S.A., 1973. Genetic studies of leucine biosynthesis in Bacillus subtilis. J. Bacteriol. 116, 719-726.
    • (1973) J. Bacteriol. , vol.116 , pp. 719-726
    • Ward, J.J.1    Zahler, S.A.2
  • 39
    • 0019376173 scopus 로고
    • Control of leu operon expression in Escherichia coli by a transcription attenuation mechanism
    • Wessler, S.R., Calvo, J.M., 1981. Control of leu operon expression in Escherichia coli by a transcription attenuation mechanism. J. Mol. Biol. 149, 579-597.
    • (1981) J. Mol. Biol. , vol.149 , pp. 579-597
    • Wessler, S.R.1    Calvo, J.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.