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Volumn 247, Issue 1, 1997, Pages 59-65

Interaction of N-tosyl-L-phenylalanylchloromethane with Thermus thermophilus elongation factor Tu

Author keywords

Affinity labeling; Aminoacyl tRNA; Elongation factor Tu; GTPase; Translation

Indexed keywords

ELONGATION FACTOR TU; TOSYLPHENYLALANYL CHLOROMETHYL KETONE;

EID: 0030839061     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.t01-1-00059.x     Document Type: Article
Times cited : (2)

References (31)
  • 2
    • 0026051404 scopus 로고
    • Overproduction of the Thermus thermophilus elongation factor Tu in Escherichia coli
    • Ahmadian, M. R., Kreutzer, R. & Sprinzl, M. (1991) Overproduction of the Thermus thermophilus elongation factor Tu in Escherichia coli, Biochimie (Paris) 73, 1037-1043.
    • (1991) Biochimie (Paris) , vol.73 , pp. 1037-1043
    • Ahmadian, M.R.1    Kreutzer, R.2    Sprinzl, M.3
  • 3
    • 0026726745 scopus 로고
    • Site-directed mutagenesis of elongation factor Tu
    • Anborgh, P. H., Parmeggiani, A. & Jonák, J. (1992) Site-directed mutagenesis of elongation factor Tu. Eur. J. Biochem. 208, 251-257.
    • (1992) Eur. J. Biochem. , vol.208 , pp. 251-257
    • Anborgh, P.H.1    Parmeggiani, A.2    Jonák, J.3
  • 5
    • 0029670027 scopus 로고    scopus 로고
    • Elongation factor Ts from Thermus thermophilus. Overproduction in Escherichia coli, quaternary structure and interaction with elongation factor Tu
    • Blank, J., Nock, S., Kreutzer, R. & Sprinzl, M. (1996) Elongation factor Ts from Thermus thermophilus. Overproduction in Escherichia coli, quaternary structure and interaction with elongation factor Tu, Eur. J. Biochem. 236, 222-227.
    • (1996) Eur. J. Biochem. , vol.236 , pp. 222-227
    • Blank, J.1    Nock, S.2    Kreutzer, R.3    Sprinzl, M.4
  • 7
    • 0001030631 scopus 로고
    • Regulation of ribosomal RNA promoters with a synthetic lac operator
    • Brosius, J. & Holy, A. (1984) Regulation of ribosomal RNA promoters with a synthetic lac operator. Proc. Natl Acad. Sci. USA 81, 6929-6933.
    • (1984) Proc. Natl Acad. Sci. USA , vol.81 , pp. 6929-6933
    • Brosius, J.1    Holy, A.2
  • 8
    • 0027169358 scopus 로고
    • Role of the 1-72 base pair in tRNAs for the activity of Escherichia coli peptidyl-tRNA hydrolase
    • Dutka, S., Meinnel, T., Lazennec, C., Mechulam, Y. & Blanquet, S. (1993) Role of the 1-72 base pair in tRNAs for the activity of Escherichia coli peptidyl-tRNA hydrolase, Nucleic Acids Res. 21, 4025-4030.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 4025-4030
    • Dutka, S.1    Meinnel, T.2    Lazennec, C.3    Mechulam, Y.4    Blanquet, S.5
  • 10
    • 0028219577 scopus 로고
    • Effector region of the translation elongation factor EF-Tu · GTP complex stabilizes an orthoester acid intermediate structure of aminoacyl-tRNA in a ternary complex
    • Förster, C., Limmer, S., Zeidler, W. & Sprinzl, M. (1994) Effector region of the translation elongation factor EF-Tu · GTP complex stabilizes an orthoester acid intermediate structure of aminoacyl-tRNA in a ternary complex, Proc. Natl Acad. Sci. USA 91, 4254-4257.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 4254-4257
    • Förster, C.1    Limmer, S.2    Zeidler, W.3    Sprinzl, M.4
  • 11
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coll with plasmids
    • Hanahan, D. (1983) Studies on transformation of Escherichia coll with plasmids, J. Mol. Biol. 166, 557-580.
    • (1983) J. Mol. Biol. , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 12
    • 0020674810 scopus 로고
    • New ribose-modified fluorescent analogs of adenine and guanine nucleotides available as substrates for various enzymes
    • Hiratsuka, T, (1983) New ribose-modified fluorescent analogs of adenine and guanine nucleotides available as substrates for various enzymes. Biochim. Biophys. Acta 742, 496-508.
    • (1983) Biochim. Biophys. Acta , vol.742 , pp. 496-508
    • Hiratsuka, T.1
  • 13
    • 0016680771 scopus 로고
    • Separation of transfer ribonucleic acid by sepharose chromatography using reverse salt gradients
    • Holmes, W. M., Hurd, R. E., Reid, B. R., Rimerman, R. A. & Hatfield, G. W. (1975) Separation of transfer ribonucleic acid by sepharose chromatography using reverse salt gradients. Proc. Natl Acad. Sci. USA 72, 1068-1071.
    • (1975) Proc. Natl Acad. Sci. USA , vol.72 , pp. 1068-1071
    • Holmes, W.M.1    Hurd, R.E.2    Reid, B.R.3    Rimerman, R.A.4    Hatfield, G.W.5
  • 15
    • 0020425992 scopus 로고
    • N-tosylL-phenylalanylchloromethane reacts with cysteine 81 in the molecule of elongation factor Tufrom Escherichia coli
    • Jonák, J., Petersen, T. E., Clark, B. F. C. & Rychlík, I. (1982) N-tosylL-phenylalanylchloromethane reacts with cysteine 81 in the molecule of elongation factor Tufrom Escherichia coli, FEBS Lett. 150, 485-488.
    • (1982) FEBS Lett. , vol.150 , pp. 485-488
    • Jonák, J.1    Petersen, T.E.2    Clark, B.F.C.3    Rychlík, I.4
  • 16
    • 0022443825 scopus 로고
    • Structural homology between elongation factors EF-Tu from Bacillus stearothermophilus and Escherichia coli in the binding site for aminoacyltRNA
    • Jonák, J., Pokorná, K., Meloun, B. & Karas, K. (1986) Structural homology between elongation factors EF-Tu from Bacillus stearothermophilus and Escherichia coli in the binding site for aminoacyltRNA, Eur. J. Biochem. 154, 355-362.
    • (1986) Eur. J. Biochem. , vol.154 , pp. 355-362
    • Jonák, J.1    Pokorná, K.2    Meloun, B.3    Karas, K.4
  • 17
    • 0027917990 scopus 로고
    • The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation
    • Kjeldgaard, M., Nissen, P., Thirup, S. & Nyborg, J. (1943) The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation. Structure (Lond.) 1, 35-50.
    • (1943) Structure (Lond.) , vol.1 , pp. 35-50
    • Kjeldgaard, M.1    Nissen, P.2    Thirup, S.3    Nyborg, J.4
  • 18
    • 0026509493 scopus 로고
    • Nucleotide binding and GTP hydrolysis hy elongation factor Tu from Thermus thermophilus as monitored by proton NMR
    • Limmer, S., Reiser, C. O. A., Schirmer, N. K., Grillenbeck, N. W. & Sprinzl, M. (1992) Nucleotide binding and GTP hydrolysis hy elongation factor Tu from Thermus thermophilus as monitored by proton NMR, Biochemistry 31, 2970-2977.
    • (1992) Biochemistry , vol.31 , pp. 2970-2977
    • Limmer, S.1    Reiser, C.O.A.2    Schirmer, N.K.3    Grillenbeck, N.W.4    Sprinzl, M.5
  • 19
    • 45949127274 scopus 로고
    • 13C NMR of enzymes
    • (Emsley, J. W., Feeney, J. & Sutcliffe, L. M., eds) Pergamon Press, New York
    • 13C NMR of enzymes, in Progress in nuclear magnetic resonance spectroscopy, vol. 17 (Emsley, J. W., Feeney, J. & Sutcliffe, L. M., eds) pp. 1-59, Pergamon Press, New York.
    • (1986) Progress in Nuclear Magnetic Resonance Spectroscopy , vol.17 , pp. 1-59
    • Multhouse, J.P.G.1
  • 21
    • 0024971344 scopus 로고
    • Interaction of elongation factor Tu from Escherichia coli with aminoacyl-tRNA carrying a fluorescent reporter group on the 3′ terminus
    • Ott, G., Faulhammer, H. G. & Sprinzl, M. (1989) Interaction of elongation factor Tu from Escherichia coli with aminoacyl-tRNA carrying a fluorescent reporter group on the 3′ terminus, Eur. J. Biochem. 184, 345-352.
    • (1989) Eur. J. Biochem. , vol.184 , pp. 345-352
    • Ott, G.1    Faulhammer, H.G.2    Sprinzl, M.3
  • 22
    • 0025019432 scopus 로고
    • The influence of different modifications of elongation factor Tu from Escherichia coli on ternary complex formation investigated by fluorescence spectroscopy
    • Ott, G., Jonák, J., Abrahams, I. P. & Sprinzl, M. (1990) The influence of different modifications of elongation factor Tu from Escherichia coli on ternary complex formation investigated by fluorescence spectroscopy. Nucleic Acids Res. 18, 437-441.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 437-441
    • Ott, G.1    Jonák, J.2    Abrahams, I.P.3    Sprinzl, M.4
  • 23
    • 0024844439 scopus 로고
    • Identification of the N-tosyl-L-phenylalanyl chloromethylketone modification site in Thermus thermophilus elongation factor Tu
    • Peter, M. E., Brockmöller, J., Jonák, J. & Sprinzl, M. (1989) Identification of the N-tosyl-L-phenylalanyl chloromethylketone modification site in Thermus thermophilus elongation factor Tu, FEBS Lett. 257, 219-222.
    • (1989) FEBS Lett. , vol.257 , pp. 219-222
    • Peter, M.E.1    Brockmöller, J.2    Jonák, J.3    Sprinzl, M.4
  • 26
    • 0001244705 scopus 로고
    • Direct evidence for the presence of histidine in the active center of chymotrypsin
    • Schoellmann, G. & Shaw, E. (1963) Direct evidence for the presence of histidine in the active center of chymotrypsin. Biochemistry 2, 252-255.
    • (1963) Biochemistry , vol.2 , pp. 252-255
    • Schoellmann, G.1    Shaw, E.2
  • 27
    • 0017382439 scopus 로고
    • Specificity of elongation factor Tu from Escherichia coli with respect to attachment of the amino acid to the 2′ or 3′-hydroxyl group of the terminal adenosine of tRNA
    • Sprinzl, M., Kucharzewski, M., Hobbs, J. B. & Cramer, F. (1977) Specificity of elongation factor Tu from Escherichia coli with respect to attachment of the amino acid to the 2′ or 3′-hydroxyl group of the terminal adenosine of tRNA, Eur. J. Biochem. 78, 55-61.
    • (1977) Eur. J. Biochem. , vol.78 , pp. 55-61
    • Sprinzl, M.1    Kucharzewski, M.2    Hobbs, J.B.3    Cramer, F.4
  • 28
    • 0028238349 scopus 로고
    • Elongation factor Tu: A regulatory GTPase with an integrated effector
    • Sprinzl, M. (1994) Elongation factor Tu: a regulatory GTPase with an integrated effector. Trends Biochem. Sci. 19, 245-250.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 245-250
    • Sprinzl, M.1
  • 30
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13-mp18 and pUC19 vectors
    • Yanisch-Perron, C., Vieira, J. & Messing, J. (1985) Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13-mp18 and pUC19 vectors. Gene (Amst.) 33, 103-119.
    • (1985) Gene (Amst.) , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 31
    • 0345195532 scopus 로고
    • Isolation of transfer RNA
    • (Cantoni, G. L. & Davies, D. R., eds) Harper & Row, New York
    • Zubay, G. (1966) Isolation of transfer RNA. in Procedures in nucleic acid research (Cantoni, G. L. & Davies, D. R., eds) pp. 455-460. Harper & Row, New York.
    • (1966) Procedures in Nucleic Acid Research , pp. 455-460
    • Zubay, G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.