메뉴 건너뛰기




Volumn 18, Issue 3, 2000, Pages 257-261

Extremely thermostable elongation factor G from Aquifex aeolicus: Cloning, expression, purification, and characterization in a heterologous translation system

Author keywords

[No Author keywords available]

Indexed keywords

CLONE; FUS GENE; GENE OVEREXPRESSION; HYDROLYSIS; MOLECULAR CLONING; PROMOTER REGION; PROTEIN DENATURATION; PROTEIN ISOLATION; PROTEIN PURIFICATION; PROTEIN SYNTHESIS; RIBOSOME; RNA TRANSLATION; THERMOSTABILITY; TRANSLATION FACTOR G;

EID: 0034006565     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.1999.1178     Document Type: Article
Times cited : (5)

References (25)
  • 2
    • 0018152620 scopus 로고
    • Studies on polypeptide-chain-elongation factors from an extreme thermophile, Thermus thermophilus HB8
    • Nakamura S., Ochta S., Arai K., Arai N., Oshima T., Kaziro Y. Studies on polypeptide-chain-elongation factors from an extreme thermophile, Thermus thermophilus HB8. Eur. J. Biochem. 92:1978;533-543.
    • (1978) Eur. J. Biochem. , vol.92 , pp. 533-543
    • Nakamura, S.1    Ochta, S.2    Arai, K.3    Arai, N.4    Oshima, T.5    Kaziro, Y.6
  • 4
    • 0027179878 scopus 로고
    • Crystal structure of active elongation factor Tu reveals major domain rearrangements
    • Berchtold H., Reshetnikova L., Reiser C. O. A., Shirmer N. K., Hilgenfeld R. Crystal structure of active elongation factor Tu reveals major domain rearrangements. Nature. 365:1993;126-132.
    • (1993) Nature , vol.365 , pp. 126-132
    • Berchtold, H.1    Reshetnikova, L.2    Reiser, C.O.A.3    Shirmer, N.K.4    Hilgenfeld, R.5
  • 6
    • 0029608909 scopus 로고
    • Ribosomal proteins and elongation factors
    • Liljas A., Garber M. Ribosomal proteins and elongation factors. Curr. Opin. Struct. Biol. 5:1995;721-727.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 721-727
    • Liljas, A.1    Garber, M.2
  • 7
    • 0033607003 scopus 로고    scopus 로고
    • Placement of protein and RNA structures into a 5 A-resolution map of the 50S ribosomal subunit
    • Ban N., Nissen P., Hansen J., Capel M., Moore P. B., Steitz T. A. Placement of protein and RNA structures into a 5 A-resolution map of the 50S ribosomal subunit. Nature. 400:1998;841-847.
    • (1998) Nature , vol.400 , pp. 841-847
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Capel, M.4    Moore, P.B.5    Steitz, T.A.6
  • 8
    • 0029379602 scopus 로고
    • Overexpression and purification of T. thermophilus elongation factors G, Tu, and Ts in E. coli
    • Blank J., Grillenbeck N. W., Kreutzer R., Sprinzl M. Overexpression and purification of T. thermophilus elongation factors G, Tu, and Ts in E. coli. Protein Expression Purific. 6:1995;637-645.
    • (1995) Protein Expression Purific , vol.6 , pp. 637-645
    • Blank, J.1    Grillenbeck, N.W.2    Kreutzer, R.3    Sprinzl, M.4
  • 9
    • 0032176794 scopus 로고    scopus 로고
    • Increased functional activity of elongation factor G with G16V mutation in the GTP-binding domain
    • Martemyanov K. A., Liljas A., Gudkov A. T. Increased functional activity of elongation factor G with G16V mutation in the GTP-binding domain. Biochemistry (Moscow). 63:1998;116-120.
    • (1998) Biochemistry (Moscow) , vol.63 , pp. 116-120
    • Martemyanov, K.A.1    Liljas, A.2    Gudkov, A.T.3
  • 10
    • 0031668779 scopus 로고    scopus 로고
    • An intact conformation of the tip of elongation factor G domain IV is functionally important
    • Martemyanov K. A., Yarunin A. S., Liljas A., Gudkov A. T. An intact conformation of the tip of elongation factor G domain IV is functionally important. FEBS Lett. 434:1998;205-208.
    • (1998) FEBS Lett. , vol.434 , pp. 205-208
    • Martemyanov, K.A.1    Yarunin, A.S.2    Liljas, A.3    Gudkov, A.T.4
  • 12
    • 0030914069 scopus 로고    scopus 로고
    • Cloning and expression of superoxide dismutase from Aquifex pyrophilus, a hyperthermophilic bacterium
    • Lim J. H., Yu Y. G., Han Y. S., Cho S., Ahn B. Y., Kim S. H., Cho Y. Cloning and expression of superoxide dismutase from Aquifex pyrophilus, a hyperthermophilic bacterium. FEBS Lett. 406:1997;142-146.
    • (1997) FEBS Lett. , vol.406 , pp. 142-146
    • Lim, J.H.1    Yu, Y.G.2    Han, Y.S.3    Cho, S.4    Ahn, B.Y.5    Kim, S.H.6    Cho, Y.7
  • 13
    • 0033119154 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of glutamate racemase from Aquifex pyrophilus, a hyperthermophilic bacterium
    • Hwang K. Y., Cho C. S., Kim S. S., Baek K., Kim S. H., Yu Y. G., Cho Y. Crystallization and preliminary X-ray analysis of glutamate racemase from Aquifex pyrophilus, a hyperthermophilic bacterium. Acta Crystallogr. D Biol. Crystallogr. 55:1999;927-928.
    • (1999) Acta Crystallogr. D Biol. Crystallogr. , vol.55 , pp. 927-928
    • Hwang, K.Y.1    Cho, C.S.2    Kim, S.S.3    Baek, K.4    Kim, S.H.5    Yu, Y.G.6    Cho, Y.7
  • 14
    • 0033534477 scopus 로고    scopus 로고
    • Extremely thermostable serine-type protease from Aquifex pyrophilus. Molecular cloning, expression, and characterization
    • Choi I. G., Bang W. G., Kim S. H., Yu Y. G. Extremely thermostable serine-type protease from Aquifex pyrophilus. Molecular cloning, expression, and characterization. J. Biol. Chem. 274:1999;881-888.
    • (1999) J. Biol. Chem. , vol.274 , pp. 881-888
    • Choi, I.G.1    Bang, W.G.2    Kim, S.H.3    Yu, Y.G.4
  • 16
    • 0029036255 scopus 로고
    • A superior host strain for the over-expression of cloned genes using the T7 promoter vectors
    • Doherty A. J., Ashford S. R., Brannigan J. A., Wigley D. B. A superior host strain for the over-expression of cloned genes using the T7 promoter vectors. Nucleic Acids Res. 23:1995;2074-2075.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 2074-2075
    • Doherty, A.J.1    Ashford, S.R.2    Brannigan, J.A.3    Wigley, D.B.4
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 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. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 19
    • 0018156514 scopus 로고
    • Studies on polypeptide-chain-elongation factors from an extreme thermophile, Thermus thermophilus HB8
    • Arai K., Arai N., Nakamura S., Oshima T., Kaziro Y. Studies on polypeptide-chain-elongation factors from an extreme thermophile, Thermus thermophilus HB8. Eur. J. Biochem. 92:1978;521-531.
    • (1978) Eur. J. Biochem. , vol.92 , pp. 521-531
    • Arai, K.1    Arai, N.2    Nakamura, S.3    Oshima, T.4    Kaziro, Y.5
  • 20
    • 0014802782 scopus 로고
    • Analysis of orthophosphate-pyrophosphate mixtures resulting from weak pyrophosphatase activities
    • Panusz H. T., Graczyk G., Wilmanska D., Skazynski J. Analysis of orthophosphate-pyrophosphate mixtures resulting from weak pyrophosphatase activities. Anal. Biochem. 35:1970;494-504.
    • (1970) Anal. Biochem. , vol.35 , pp. 494-504
    • Panusz, H.T.1    Graczyk, G.2    Wilmanska, D.3    Skazynski, J.4
  • 21
    • 0019881232 scopus 로고
    • Elongation factor Tu can reduce translation errors in poly(U)-directed cell-free systems
    • Gavrilova L. P., Perminova I. N., Spirin A. S. Elongation factor Tu can reduce translation errors in poly(U)-directed cell-free systems. J. Mol. Biol. 149:1981;69-78.
    • (1981) J. Mol. Biol. , vol.149 , pp. 69-78
    • Gavrilova, L.P.1    Perminova, I.N.2    Spirin, A.S.3
  • 23
    • 0018064450 scopus 로고
    • Studies on polypeptide-chain-elongation factors from an extreme thermopile, T. thermopilus HB8. Purification and some properties of the purified factors
    • Arai K., Ota Y., Arai N., Nakamura S., Henneke C., Oshima T., Kaziro Y. Studies on polypeptide-chain-elongation factors from an extreme thermopile, T. thermopilus HB8. Purification and some properties of the purified factors. Eur. J. Biochem. 92:1978;509-519.
    • (1978) Eur. J. Biochem. , vol.92 , pp. 509-519
    • Arai, K.1    Ota, Y.2    Arai, N.3    Nakamura, S.4    Henneke, C.5    Oshima, T.6    Kaziro, Y.7
  • 24
    • 0029587036 scopus 로고
    • Arrangement and nucleotide sequence of the gene (fus) encoding elongation factor G (EF-G) from the hyperthermophilic bacterium Aquifex pyrophilus: Phylogenetic depth of hyperthermophilic bacteria inferred from analysis of the EF-G/fus sequences
    • Bocchetta M., Ceccarelli E., Creti R., Sanangelantoni A. M., Tiboni O., Cammarano P. Arrangement and nucleotide sequence of the gene (fus) encoding elongation factor G (EF-G) from the hyperthermophilic bacterium Aquifex pyrophilus: Phylogenetic depth of hyperthermophilic bacteria inferred from analysis of the EF-G/fus sequences. J. Mol. Evol. 41:1995;803-812.
    • (1995) J. Mol. Evol. , vol.41 , pp. 803-812
    • Bocchetta, M.1    Ceccarelli, E.2    Creti, R.3    Sanangelantoni, A.M.4    Tiboni, O.5    Cammarano, P.6
  • 25
    • 0033555252 scopus 로고    scopus 로고
    • Refined crystal structure of a superoxide dismutase from the hyperthermophilic archaeon Sulfolobus acidocaldarius at 2.2 A resolution
    • Knapp S., Kardinahl S., Hellgren N., Tibbelin G., Schafer G., Ladenstein R. Refined crystal structure of a superoxide dismutase from the hyperthermophilic archaeon Sulfolobus acidocaldarius at 2.2 A resolution. J. Mol. Biol. 285:1999;689-702.
    • (1999) J. Mol. Biol. , vol.285 , pp. 689-702
    • Knapp, S.1    Kardinahl, S.2    Hellgren, N.3    Tibbelin, G.4    Schafer, G.5    Ladenstein, R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.