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Volumn 256, Issue 1, 1998, Pages 136-141

Studies on the Zn-containing S14 ribosomal protein from Thermus thermophilus

Author keywords

Ribosomal protein; S14; Thermus thermophilus; Zinc finger

Indexed keywords

RIBOSOME PROTEIN; ZINC;

EID: 0032529146     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2560136.x     Document Type: Article
Times cited : (17)

References (38)
  • 1
    • 0029402642 scopus 로고
    • Structure and evolution of mammalian ribosomal proteins
    • Matheson, A. T., Davies, J. E., Dennis, P. P. & Hill, W. E., eds National Research Council Canada, Ottawa
    • Wool, I., Chan, Y.-L. & Glueck, A. (1995) Structure and evolution of mammalian ribosomal proteins in Frontiers in translation. An international conference on the structure and function of the ribosome (Matheson, A. T., Davies, J. E., Dennis, P. P. & Hill, W. E., eds) pp. 933-947, National Research Council Canada, Ottawa.
    • (1995) Frontiers in Translation. An International Conference on the Structure and Function of the Ribosome , pp. 933-947
    • Wool, I.1    Chan, Y.-L.2    Glueck, A.3
  • 3
    • 0031024655 scopus 로고    scopus 로고
    • The RNA binding domain of ribosomal protein L11 is structurally similar to homeodomains
    • Xing, Y., Guha Thakurta, D. & Draper, D. E. (1997) The RNA binding domain of ribosomal protein L11 is structurally similar to homeodomains. Nat. Struct. Biol. 4, 24-27.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 24-27
    • Xing, Y.1    Guha Thakurta, D.2    Draper, D.E.3
  • 4
    • 0031027211 scopus 로고    scopus 로고
    • Alpha-helical protein assembly motifs
    • Kohn, W. D., Mant, C. T. & Hodges, R. S. (1997) Alpha-helical protein assembly motifs, J. Biol. Chem. 272, 2583-2586.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2583-2586
    • Kohn, W.D.1    Mant, C.T.2    Hodges, R.S.3
  • 5
    • 0027168692 scopus 로고
    • Zinc-finger-like motifs in rat ribosomal proteins S27 and S29
    • Chan, Y. L., Suzuki, K., Olvera, J. & Wool, I. G. (1993) Zinc-finger-like motifs in rat ribosomal proteins S27 and S29, Nucleic Acids Res. 21, 649-655.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 649-655
    • Chan, Y.L.1    Suzuki, K.2    Olvera, J.3    Wool, I.G.4
  • 6
    • 0028023941 scopus 로고
    • Complete amino acid sequence of ribosomal protein S14 from B. stearothermophilus and homology studies to other ribosomal proteins
    • Herfurth, E., Briesemeister, U. & Wittmann-Liebold, B. (1994) Complete amino acid sequence of ribosomal protein S14 from B. stearothermophilus and homology studies to other ribosomal proteins, FEBS Lett. 351, 114-118.
    • (1994) FEBS Lett. , vol.351 , pp. 114-118
    • Herfurth, E.1    Briesemeister, U.2    Wittmann-Liebold, B.3
  • 7
    • 0029240402 scopus 로고
    • Studies on S14 protein from Thermus thermophilus possessing zinc-finger like motifs
    • Tsiboli, P. & Choli, T. (1995) Studies on S14 protein from Thermus thermophilus possessing zinc-finger like motifs, Biol. Chem. Hoppe-Seyler 376, 127-130.
    • (1995) Biol. Chem. Hoppe-Seyler , vol.376 , pp. 127-130
    • Tsiboli, P.1    Choli, T.2
  • 8
    • 0029087624 scopus 로고
    • Protein-rRNA binding features and their structural and functional implications in ribosomes as determined by cross-linking studies
    • Urlaub, H., Kruft, V., Bischof, O., Mueller, E. V. & Wittmann-Liebold, B. (1995) Protein-rRNA binding features and their structural and functional implications in ribosomes as determined by cross-linking studies. EMBO J. 14, 4578-4588.
    • (1995) EMBO J. , vol.14 , pp. 4578-4588
    • Urlaub, H.1    Kruft, V.2    Bischof, O.3    Mueller, E.V.4    Wittmann-Liebold, B.5
  • 10
    • 85010439719 scopus 로고
    • A procedure for the isolation of deoxyribonucleic acid from microorganisms
    • Marmur, J. (1961) A procedure for the isolation of deoxyribonucleic acid from microorganisms. J. Mol. Biol. 3, 208-218.
    • (1961) J. Mol. Biol. , vol.3 , pp. 208-218
    • Marmur, J.1
  • 11
    • 77956917564 scopus 로고
    • Boyer, P. D., ed. Academic Press, New York
    • Reid, T. W. & Wilson, I. B. (1971) in The enzymes (Boyer, P. D., ed.) vol. 4, pp. 373-415, Academic Press, New York.
    • (1971) The Enzymes , vol.4 , pp. 373-415
    • Reid, T.W.1    Wilson, I.B.2
  • 12
    • 0003448569 scopus 로고
    • Cold Spring Harbour Laboratory Press, Cold Spring Harbour NY
    • Harlow, D. & Lane, D. (1988) Antibodies, a laboratory manual, Cold Spring Harbour Laboratory Press, Cold Spring Harbour NY.
    • (1988) Antibodies, a Laboratory Manual
    • Harlow, D.1    Lane, D.2
  • 13
    • 0023645045 scopus 로고
    • A family of serine esterases in lytic granules of cytolytic T lymphocytes
    • Masson, D. & Tschopp, J. (1987) A family of serine esterases in lytic granules of cytolytic T lymphocytes. Cell 49, 679-685.
    • (1987) Cell , vol.49 , pp. 679-685
    • Masson, D.1    Tschopp, J.2
  • 14
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T. & Gordon, J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl Acad. Sci. USA 76, 4350-4354.
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 15
    • 0024325490 scopus 로고
    • Blotting of proteins onto Immobilon membranes - In situ characterization and comparison with high performance liquid chromatography
    • Choli, T., Kapp, U. & Wittmann-Liebold B. (1989) Blotting of proteins onto Immobilon membranes - In situ characterization and comparison with high performance liquid chromatography, J. Chromatogr. 476, 59-72.
    • (1989) J. Chromatogr. , vol.476 , pp. 59-72
    • Choli, T.1    Kapp, U.2    Wittmann-Liebold, B.3
  • 16
    • 0029569085 scopus 로고
    • Matrix-assisted laser desorption/ionization of noncovalently bound compounds
    • Woods, A. S., Buchsbaum, J. C., Worrall, T. A., Berg, J. M. & Cotter, R. J. (1995) Matrix-assisted laser desorption/ionization of noncovalently bound compounds, Anal. Chem. 67, 4462-4465.
    • (1995) Anal. Chem. , vol.67 , pp. 4462-4465
    • Woods, A.S.1    Buchsbaum, J.C.2    Worrall, T.A.3    Berg, J.M.4    Cotter, R.J.5
  • 17
    • 0025096109 scopus 로고
    • Sequencc-specific DNA binding by glucocorticoid receptor "zinc-finger peptides"
    • Archer, T. K., Hager, G. L. & Omichinski, J. G. (1990) Sequencc-specific DNA binding by glucocorticoid receptor "zinc-finger peptides", Proc. Natl Acad. Sci. USA 87, 7560-7564.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 7560-7564
    • Archer, T.K.1    Hager, G.L.2    Omichinski, J.G.3
  • 18
    • 15144346859 scopus 로고
    • Zinc-containing binding domains
    • Chapman & Hall, London
    • Travers, A. (1993) Zinc-containing binding domains, in DNA-protein interactions, pp. 64-73, Chapman & Hall, London.
    • (1993) DNA-protein Interactions , pp. 64-73
    • Travers, A.1
  • 19
    • 0028172822 scopus 로고
    • 1H NMR structure and biological studies of the His23→>Cys mutant nucleocapsid protein of HIV-1 indicate that the conformation of the first zinc-finger is critical for virus infectivity
    • Demene, H., Dong, C. Z., Ottmann, M., Rouyez, M. C., Jullian, N., Morellet, N., Mely, Y., Darlix, J. L., Fournie-Zaluski, M. C., Saragosti, S. & Roques, B. P. (1994) 1H NMR structure and biological studies of the His23→>Cys mutant nucleocapsid protein of HIV-1 indicate that the conformation of the first zinc-finger is critical for virus infectivity, Biochemistry 33, 11707-11716.
    • (1994) Biochemistry , vol.33 , pp. 11707-11716
    • Demene, H.1    Dong, C.Z.2    Ottmann, M.3    Rouyez, M.C.4    Jullian, N.5    Morellet, N.6    Mely, Y.7    Darlix, J.L.8    Fournie-Zaluski, M.C.9    Saragosti, S.10    Roques, B.P.11
  • 21
    • 0024344098 scopus 로고
    • RNA-protein interactions in 30S ribosomal subunits: Folding and function of 16S rRNA
    • Stern, S., Powers, T., Changchien, L. M. & Noller, H. E. (1989) RNA-protein interactions in 30S ribosomal subunits: folding and function of 16S rRNA. Science 244, 783-790.
    • (1989) Science , vol.244 , pp. 783-790
    • Stern, S.1    Powers, T.2    Changchien, L.M.3    Noller, H.E.4
  • 23
    • 0024292371 scopus 로고
    • Interactions of proteins S16, S17 and S20 with 16S ribosomal RNA
    • Stern, S., Changchien, L. M., Craven, G. R. & Noller, H. F. (1888) Interactions of proteins S16, S17 and S20 with 16S ribosomal RNA, J. Mol. Biol. 200, 291-299.
    • (1888) J. Mol. Biol. , vol.200 , pp. 291-299
    • Stern, S.1    Changchien, L.M.2    Craven, G.R.3    Noller, H.F.4
  • 24
    • 0027432838 scopus 로고
    • A growth factor-inducible gene encodes a novel nuclear protein with zinc-finger structure
    • Fernandez-Pol. J. A. (1993) A growth factor-inducible gene encodes a novel nuclear protein with zinc-finger structure. J. Biol. Chem. 268, 21198-21204.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21198-21204
    • Fernandez-Pol, J.A.1
  • 25
    • 0027652056 scopus 로고
    • Entamoeba histolytica: The EHZc3 cDNA clone encodes a zinc-binding protein
    • Zhang, Y. (1993) Entamoeba histolytica: the EHZc3 cDNA clone encodes a zinc-binding protein, Exp. Parasitol. 77, 118-120.
    • (1993) Exp. Parasitol. , vol.77 , pp. 118-120
    • Zhang, Y.1
  • 29
    • 0024449327 scopus 로고
    • Cloning and analysis of the spc ribosomal protein operon of Bacillus subtilis: Comparison with the spc operon of Escherichia coli
    • Henkin, T. M., Moon, S. H., Mattheakis, L. C. & Nomura, M. (1989) Cloning and analysis of the spc ribosomal protein operon of Bacillus subtilis: comparison with the spc operon of Escherichia coli, Nucleic Acids Res. 17, 7469-7486.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 7469-7486
    • Henkin, T.M.1    Moon, S.H.2    Mattheakis, L.C.3    Nomura, M.4
  • 31
    • 0024962387 scopus 로고
    • Organization and structure of the Methanococcus transcriptional unit homologous to the E. coli "spectinomycin operon". Implications for the evolutionary relationship of 70S and 80S ribosomes
    • Auer, J., Spicker, G. & Boeck, A. (1989) Organization and structure of the Methanococcus transcriptional unit homologous to the E. coli "spectinomycin operon". Implications for the evolutionary relationship of 70S and 80S ribosomes, J. Mol. Biol. 209, 21-28.
    • (1989) J. Mol. Biol. , vol.209 , pp. 21-28
    • Auer, J.1    Spicker, G.2    Boeck, A.3
  • 32
    • 0023484179 scopus 로고
    • The ribosomal protein gene cluster of Mycoplasma capricolum
    • Ohkubo, S., Muto, A., Kawauchi, Y., Yamao, F. & Osawa, S. (1987)The ribosomal protein gene cluster of Mycoplasma capricolum, Mol. Gen. Genet. 210, 314-322.
    • (1987) Mol. Gen. Genet. , vol.210 , pp. 314-322
    • Ohkubo, S.1    Muto, A.2    Kawauchi, Y.3    Yamao, F.4    Osawa, S.5
  • 33
  • 34
    • 0024296971 scopus 로고
    • Ribosomal protein S14 genes in broad bean mitochondrial DNA
    • Wahleithner, J. A. & Wolstenholme, D. R. (1988) Ribosomal protein S14 genes in broad bean mitochondrial DNA, Nucleic Acids Res. 16, 6897-6913.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 6897-6913
    • Wahleithner, J.A.1    Wolstenholme, D.R.2
  • 35
    • 0024284693 scopus 로고
    • Sequence of the chloroplast psbF gene encoding the photosystem II 10 kDa phosphoprotein from Oryza sativa
    • Coté. J. C. & Wu, R. (1988) Sequence of the chloroplast psbF gene encoding the photosystem II 10 kDa phosphoprotein from Oryza sativa. Nucleic Acids Res. 16, 10384.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 10384
    • Coté, J.C.1    Wu, R.2
  • 36
    • 0023138080 scopus 로고
    • Structure and expression of the S. cerevisiae CRY1 gene: A highly con-served ribosomal protein gene
    • Larkin, J. C., Thompson, J. R. & Woolford, J. L. Jr (1987) Structure and expression of the S. cerevisiae CRY1 gene: a highly con-served ribosomal protein gene, Mol. Cell. Biol. 7, 1764-1775.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 1764-1775
    • Larkin, J.C.1    Thompson, J.R.2    Woolford Jr., J.L.3
  • 37
    • 0025915261 scopus 로고
    • Organization and nucleotide sequence of ten ribosomal protein genes from the region equivalent to the spectinomycin operon in the archaebacterium Halobacteriuin marismortui
    • Scholzen, T. & Arndt, E. (1991) Organization and nucleotide sequence of ten ribosomal protein genes from the region equivalent to the spectinomycin operon in the archaebacterium Halobacteriuin marismortui, Mol. Gen. Genet. 228, 70-80.
    • (1991) Mol. Gen. Genet. , vol.228 , pp. 70-80
    • Scholzen, T.1    Arndt, E.2
  • 38
    • 0029020135 scopus 로고
    • Cloning, sequencing and expression of the L5, L21, L27a, L28, S5, S9, S10, S29 human ribosomal protein mRNAs
    • Frigerio, J. M., Dagorn, J. C. & Iovanna, J. L. (1995) Cloning, sequencing and expression of the L5, L21, L27a, L28, S5, S9, S10, S29 human ribosomal protein mRNAs. Biochim. Biophys. Acta 1262, 64-68.
    • (1995) Biochim. Biophys. Acta , vol.1262 , pp. 64-68
    • Frigerio, J.M.1    Dagorn, J.C.2    Iovanna, J.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.