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Volumn 24, Issue 4, 1996, Pages 516-519

Purification, crystallization, and preliminary X-ray diffraction studies of tRNA-guanine transglycosylase from Zymomonas mobilis

Author keywords

crystallization; queuosine; transglycosylation; tRNA; X ray diffraction

Indexed keywords

GLYCOSYLTRANSFERASE; GUANINE; TRANSFER RNA;

EID: 0029897830     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(199604)24:4<516::AID-PROT11>3.0.CO;2-O     Document Type: Article
Times cited : (34)

References (23)
  • 2
    • 0027245490 scopus 로고
    • Modification of tRNA as a regulatory device
    • Persson, B.C. Modification of tRNA as a regulatory device. Mol. Microbiol. 8:1011-1016, 1993.
    • (1993) Mol. Microbiol. , vol.8 , pp. 1011-1016
    • Persson, B.C.1
  • 4
    • 0028041249 scopus 로고
    • vacC, a virulence-associated chromosomal locus of Shigella flexneri, is homologous to tgt, a gene encoding tRNA-guanine transglycosylase (Tgt) of Escherichia coli K-12
    • Durand, J.M., Okada, N., Tobe, T., Watarai, M., Fukuda, I., Suzuki, T., Nakata, N., Komatsu, K., Yoshikawa, M., Sasakawa, C. vacC, a virulence-associated chromosomal locus of Shigella flexneri, is homologous to tgt, a gene encoding tRNA-guanine transglycosylase (Tgt) of Escherichia coli K-12. J. Bacteriol. 176:4627-4634, 1994.
    • (1994) J. Bacteriol. , vol.176 , pp. 4627-4634
    • Durand, J.M.1    Okada, N.2    Tobe, T.3    Watarai, M.4    Fukuda, I.5    Suzuki, T.6    Nakata, N.7    Komatsu, K.8    Yoshikawa, M.9    Sasakawa, C.10
  • 5
    • 0021331057 scopus 로고
    • Evidence that the nucleic acid base queuine is incorporated intact into tRNA by animal cells
    • Katze, J.R., Gündüz, U., Smith, D.L., Cheng, C.S., McCloskey, J.A. Evidence that the nucleic acid base queuine is incorporated intact into tRNA by animal cells. Biochemistry 23:1171-1176, 1984.
    • (1984) Biochemistry , vol.23 , pp. 1171-1176
    • Katze, J.R.1    Gündüz, U.2    Smith, D.L.3    Cheng, C.S.4    McCloskey, J.A.5
  • 6
    • 0028908903 scopus 로고
    • Regulation of signalling by receptor tyrosine kinases in HeLa cells involves the q-base
    • Langgut, W. Regulation of signalling by receptor tyrosine kinases in HeLa cells involves the q-base. Biochem. Biophys. Res. Comm. 207:306-311, 1995.
    • (1995) Biochem. Biophys. Res. Comm. , vol.207 , pp. 306-311
    • Langgut, W.1
  • 7
    • 0024789601 scopus 로고
    • Chromatographic analysis of the aminoacyl- TRNAs which are required for translation of codons at and around the ribosomal frameshift sites of HIV,HTLV-1, and BLV
    • Hatfield, D., Feng, Y.X., Lee, B.J., Rein, A., Levin, J.G., Oroszlan, S. Chromatographic analysis of the aminoacyl- tRNAs which are required for translation of codons at and around the ribosomal frameshift sites of HIV,HTLV-1, and BLV. Virology 173:736-742, 1989.
    • (1989) Virology , vol.173 , pp. 736-742
    • Hatfield, D.1    Feng, Y.X.2    Lee, B.J.3    Rein, A.4    Levin, J.G.5    Oroszlan, S.6
  • 8
    • 0028646196 scopus 로고
    • Genes, enzymes and coenzymes of queuosine biosynthesis in procaryotes
    • Slany, R.K., Kersten, H. Genes, enzymes and coenzymes of queuosine biosynthesis in procaryotes. Biochimie 76: 1178-1182, 1994.
    • (1994) Biochimie , vol.76 , pp. 1178-1182
    • Slany, R.K.1    Kersten, H.2
  • 9
    • 0025893685 scopus 로고
    • Structure and organisation of Escherichia coli genes involved in biosynthesis of the deazaguanine derivative queuine, a nutrient factor for eukaryotes
    • Reuter, K., Slany, R., Ullrich, F., Kersten, H. Structure and organisation of Escherichia coli genes involved in biosynthesis of the deazaguanine derivative queuine, a nutrient factor for eukaryotes. J. Bacteriol. 173:2256-2264, 1991.
    • (1991) J. Bacteriol. , vol.173 , pp. 2256-2264
    • Reuter, K.1    Slany, R.2    Ullrich, F.3    Kersten, H.4
  • 10
    • 0018800827 scopus 로고
    • Isolation and characterization of a guanme insertion enzyme, a specific tRNA transglycosylase, from Escherichia coli
    • Okada, N., Nishimura, S. Isolation and characterization of a guanme insertion enzyme, a specific tRNA transglycosylase, from Escherichia coli. J. Biol. Chem. 254:3061-3066, 1979.
    • (1979) J. Biol. Chem. , vol.254 , pp. 3061-3066
    • Okada, N.1    Nishimura, S.2
  • 12
    • 0027300858 scopus 로고
    • tRNA-guanine transglycosylase from Escherichia coli: Gross tRNA structural requirements for recognition
    • Curnow, A.W., Kung, F.L., Koch, K.A., Garcia, G.A. tRNA-guanine transglycosylase from Escherichia coli: Gross tRNA structural requirements for recognition. Biochemistry 32:5239-5246, 1993.
    • (1993) Biochemistry , vol.32 , pp. 5239-5246
    • Curnow, A.W.1    Kung, F.L.2    Koch, K.A.3    Garcia, G.A.4
  • 13
    • 0028595685 scopus 로고
    • A UGU sequence in the anticodon loop is a minimum requirement for recognition by Escherichia coli tRNA-guanine transglycosylase
    • Nakanishi, S., Ueda, T., Hori, H., Yamazaki, N., Okada, N., Watanabe, K. A UGU sequence in the anticodon loop is a minimum requirement for recognition by Escherichia coli tRNA-guanine transglycosylase. J. Biol. Chem. 269: 32221-32225, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32221-32225
    • Nakanishi, S.1    Ueda, T.2    Hori, H.3    Yamazaki, N.4    Okada, N.5    Watanabe, K.6
  • 14
    • 0029112199 scopus 로고
    • Sequence analysis and overexpression of the Zymomonas mobilis gene encoding tRNA-guanine transglycosylase; purification and biochemical characterization of the enzyme
    • Reuter, K., Ficner, R. Sequence analysis and overexpression of the Zymomonas mobilis gene encoding tRNA-guanine transglycosylase; purification and biochemical characterization of the enzyme. J. Bacteriol. 177:5284-5288, 1995.
    • (1995) J. Bacteriol. , vol.177 , pp. 5284-5288
    • Reuter, K.1    Ficner, R.2
  • 15
    • 0027280419 scopus 로고
    • tRNA-guanine transglycosylase from Escherichia coli. Overexpression, purification and quaternary structure
    • Garcia, G.A., Koch, K.A., Chong, S. tRNA-guanine transglycosylase from Escherichia coli. Overexpression, purification and quaternary structure. J. Mol. Biol. 231:489-497, 1993.
    • (1993) J. Mol. Biol. , vol.231 , pp. 489-497
    • Garcia, G.A.1    Koch, K.A.2    Chong, S.3
  • 16
    • 85022452739 scopus 로고
    • tRNA-guanine transglycosylase from Escherichia coli is a zinc metalloprotein. Site-directed mutagenesis studies to identify the zinc ligands
    • Chong, S., Curnow, A.W., Huston, T.J., Garcia, G.A. tRNA-guanine transglycosylase from Escherichia coli is a zinc metalloprotein. Site-directed mutagenesis studies to identify the zinc ligands. Biochemistry 34:3694-3701, 1995.
    • (1995) Biochemistry , vol.34 , pp. 3694-3701
    • Chong, S.1    Curnow, A.W.2    Huston, T.J.3    Garcia, G.A.4
  • 17
    • 0028246537 scopus 로고
    • Serine 90 is required for enzymic activity by tRNA- Guanine transglycosylase from Escherichia coli
    • Reuter, K., Chong, S., Ullrich, F., Kersten, H., Garcia, G.A. Serine 90 is required for enzymic activity by tRNA- guanine transglycosylase from Escherichia coli. Biochemistry 33:7041-7046, 1994.
    • (1994) Biochemistry , vol.33 , pp. 7041-7046
    • Reuter, K.1    Chong, S.2    Ullrich, F.3    Kersten, H.4    Garcia, G.A.5
  • 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. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal. Biochem. 72:248, 1976.
    • (1976) Anal. Biochem. , vol.72 , pp. 248
    • Bradford, M.1
  • 19
    • 85046526624 scopus 로고
    • Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector
    • Kabsch, W. Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector. J. Appl. Crystallogr. 21:916-924, 1988.
    • (1988) J. Appl. Crystallogr. , vol.21 , pp. 916-924
    • Kabsch, W.1
  • 20
    • 0000085607 scopus 로고
    • Crystallization experiments with 2-enoyl-CoA hydratase, using an automated "fast-screening" crystallization protocol
    • Zeelen, J.P., Hiltunen, J.K., Ceska, T.A., Wierenga, R.K. Crystallization experiments with 2-enoyl-CoA hydratase, using an automated "fast-screening" crystallization protocol. Acta Crystalogr. D50:443-447, 1994.
    • (1994) Acta Crystalogr. , vol.D50 , pp. 443-447
    • Zeelen, J.P.1    Hiltunen, J.K.2    Ceska, T.A.3    Wierenga, R.K.4
  • 23
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews, B.W. Solvent content of protein crystals. J. Mol. Biol. 33:491-497, 1968.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.