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Volumn 239, Issue 1, 1996, Pages 144-149

Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry

Author keywords

HPLC; Human ribosomal proteins; Matrix assisted laser desorption ionization MS; N terminal and internal amino acid sequencing; Post translational modifications

Indexed keywords

RIBOSOME PROTEIN;

EID: 0029895550     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0144u.x     Document Type: Article
Times cited : (60)

References (40)
  • 2
    • 0027246374 scopus 로고
    • Cloning of the Drosophila ribosomal protein S3: Another multifunctional ribosomal protein with AP endonuclease DNA repair activity
    • Wilson, D. M. Deutsch, W. A. & Kelley, M. R. (1993) Cloning of the Drosophila ribosomal protein S3: another multifunctional ribosomal protein with AP endonuclease DNA repair activity, Nucleic Acids Res. 21, 2516.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 2516
    • Wilson, D.M.1    Deutsch, W.A.2    Kelley, M.R.3
  • 4
    • 0026572661 scopus 로고
    • Elevated expression of the ribosomal protein S2 gene in human tumors
    • Chiao, P. J., Shin, D. M. Sacks, P. G., Hong, W. K. & Tainsky, M. A. (1992) Elevated expression of the ribosomal protein S2 gene in human tumors. Mol. Carcinog. 5, 219 - 231.
    • (1992) Mol. Carcinog. , vol.5 , pp. 219-231
    • Chiao, P.J.1    Shin, D.M.2    Sacks, P.G.3    Hong, W.K.4    Tainsky, M.A.5
  • 5
    • 0025177034 scopus 로고
    • Oncogenic activation of the human trk protooncogene by recombination with the ribosomal large subunit protein L7a
    • Ziemiecki, A., Muller, R. G., Xiao-Chang, F., Hynes, N. E. & Kozma, S. (1990) Oncogenic activation of the human trk protooncogene by recombination with the ribosomal large subunit protein L7a. EMBO J. 9, 191 - 196.
    • (1990) EMBO J. , vol.9 , pp. 191-196
    • Ziemiecki, A.1    Muller, R.G.2    Xiao-Chang, F.3    Hynes, N.E.4    Kozma, S.5
  • 6
    • 0001874236 scopus 로고
    • Structure, function and evolution of mammalian ribosomes
    • (Hill, W. E., Dahlberg, A., Garrett, R. A., Moore, P. B., Schlessinger, D. & Warner, J. R., eds) American Society for Microbiology. Washington DC
    • Wool, I., Endo, Y., Chan, Y. L. & Glück, A. (1990) Structure, function and evolution of mammalian ribosomes, in The ribosome, structure, function and evolution (Hill, W. E., Dahlberg, A., Garrett, R. A., Moore, P. B., Schlessinger, D. & Warner, J. R., eds) pp. 203 - 214, American Society for Microbiology. Washington DC.
    • (1990) The Ribosome, Structure, Function and Evolution , pp. 203-214
    • Wool, I.1    Endo, Y.2    Chan, Y.L.3    Glück, A.4
  • 7
    • 77956760389 scopus 로고
    • Ribosomal proteins: Their structure and spatial arrangement in prokaryotic ribosomes
    • Giri, L., Hill, W. E., Wittmann, H. G. & Wittrnann-Liebold, B. (1984) Ribosomal proteins: their structure and spatial arrangement in prokaryotic ribosomes, Adv. Protein Chem. 36, 1 - 78.
    • (1984) Adv. Protein Chem. , vol.36 , pp. 1-78
    • Giri, L.1    Hill, W.E.2    Wittmann, H.G.3    Wittrnann-Liebold, B.4
  • 8
    • 0001836114 scopus 로고
    • Ribosomal proteins: Their structure and evolution
    • (Hardesly, B. & Kramer, G., eds) Springer-Verlag, New York
    • Wittmann-Liebold, B. (1986) Ribosomal proteins: their structure and evolution, in Structure, function and genatics of ribosomes (Hardesly, B. & Kramer, G., eds) pp. 326 - 361, Springer-Verlag, New York.
    • (1986) Structure, Function and Genatics of Ribosomes , pp. 326-361
    • Wittmann-Liebold, B.1
  • 9
    • 0021325751 scopus 로고
    • Phosphorylation of hepatic ribosomal protein S6 on 80 and 40S ribosomes. Primary structure of S6 in the region of the major phosphorylation sites for cAMP-dependent protein kinases
    • Wettenhall, R. E. H. & Morgan, F. J. (1984) Phosphorylation of hepatic ribosomal protein S6 on 80 and 40S ribosomes. Primary structure of S6 in the region of the major phosphorylation sites for cAMP-dependent protein kinases. J. Biol. Chem. 259, 2084 - 2091.
    • (1984) J. Biol. Chem. , vol.259 , pp. 2084-2091
    • Wettenhall, R.E.H.1    Morgan, F.J.2
  • 10
    • 0021307322 scopus 로고
    • Differential kinetics of changes in the state of phosphorylation of ribosomal protein S6 and in the rale of protein synthesis in MPC11 cell during tonicity shifts
    • Kruppa, I. & Clemens, M. J. (1984) Differential kinetics of changes in the state of phosphorylation of ribosomal protein S6 and in the rale of protein synthesis in MPC11 cell during tonicity shifts. EMBO J. 3, 95 - 100.
    • (1984) EMBO J. , vol.3 , pp. 95-100
    • Kruppa, I.1    Clemens, M.J.2
  • 11
    • 0016737283 scopus 로고
    • Phosphorylation of ribosome-associated proteins during the mammalian cell cycle. Unique phosphorylation of a specific protein during mitosis
    • Rupp, R. G., Humphrey, R. M. & Shaeffer, J. R. (1976) Phosphorylation of ribosome-associated proteins during the mammalian cell cycle. Unique phosphorylation of a specific protein during mitosis, Biochim. Biophys. Acta 418, 81 - 92.
    • (1976) Biochim. Biophys. Acta , vol.418 , pp. 81-92
    • Rupp, R.G.1    Humphrey, R.M.2    Shaeffer, J.R.3
  • 12
    • 0018178022 scopus 로고
    • Identification of the methylated ribosomal proteins in HeLa cells and the fluctuation of methylation during the cell cycle
    • Chang, F. N., Navickas, I. J., Au, C. & Budzilowicz, C. (1978). Identification of the methylated ribosomal proteins in HeLa cells and the fluctuation of methylation during the cell cycle. Biochim. Biophys. Acta 518, 89 - 94.
    • (1978) Biochim. Biophys. Acta , vol.518 , pp. 89-94
    • Chang, F.N.1    Navickas, I.J.2    Au, C.3    Budzilowicz, C.4
  • 13
    • 0342324801 scopus 로고
    • Amino acid sequence of a 50S ribosomal protein involved in both EFG and EFT dependent GTP-hydrolysis
    • Terhorst, C., Möller, W., Laursen, R. A. & Wittmann-Liebold, B. (1972) Amino acid sequence of a 50S ribosomal protein involved in both EFG and EFT dependent GTP-hydrolysis. FEBS Lett. 28, 325 - 328.
    • (1972) FEBS Lett. , vol.28 , pp. 325-328
    • Terhorst, C.1    Möller, W.2    Laursen, R.A.3    Wittmann-Liebold, B.4
  • 14
    • 0016286071 scopus 로고
    • Acetylation of reticulocyte ribosomal proteins at time of protein biosynthesis
    • Liew, C. C. & Yip, C. C. (1974) Acetylation of reticulocyte ribosomal proteins at time of protein biosynthesis, Proc. Natl Acad. Sci. USA 71, 2988 - 2991.
    • (1974) Proc. Natl Acad. Sci. USA , vol.71 , pp. 2988-2991
    • Liew, C.C.1    Yip, C.C.2
  • 15
    • 0003176633 scopus 로고
    • Purification and identification of E. coli ribosomal proteins
    • (Nomura, M., Tissieres, A. & Lengyel, P., eds) Cold Spring Harbor Press, Long Island NY
    • Wittmann, H. G. (1974) Purification and identification of E. coli ribosomal proteins, in Ribsomes (Nomura, M., Tissieres, A. & Lengyel, P., eds) pp. 93 - 114. Cold Spring Harbor Press, Long Island NY.
    • (1974) Ribsomes , pp. 93-114
    • Wittmann, H.G.1
  • 16
    • 0000114026 scopus 로고
    • Use of cyanate for determining amino-terminal residues in proteins
    • Stark, G. G. (1967) Use of cyanate for determining amino-terminal residues in proteins, Methods Enzymol. 11, 125 - 138.
    • (1967) Methods Enzymol. , vol.11 , pp. 125-138
    • Stark, G.G.1
  • 17
    • 0024199008 scopus 로고
    • Ribosomal proteins from archaebacteria: High performance liquid chromatographic purification for microsequence analysis
    • Kamp, R. M. & Wittmann-Liebold, B. (1988) Ribosomal proteins from archaebacteria: high performance liquid chromatographic purification for microsequence analysis, in: Methods Enzymol. 164, 542 - 571.
    • (1988) Methods Enzymol. , vol.164 , pp. 542-571
    • Kamp, R.M.1    Wittmann-Liebold, B.2
  • 18
    • 0021765918 scopus 로고
    • Separation of ribosomal proteins from Escherichia coli and rabbit reticulocytes using reverse-phase high-performance liquid chromatography
    • Ferris, R. J., Cowgill, C. A. & Traut, R. R. (1984) Separation of ribosomal proteins from Escherichia coli and rabbit reticulocytes using reverse-phase high-performance liquid chromatography, Biochemistry 23, 3434 - 3442.
    • (1984) Biochemistry , vol.23 , pp. 3434-3442
    • Ferris, R.J.1    Cowgill, C.A.2    Traut, R.R.3
  • 20
    • 0014546343 scopus 로고
    • The ribosomal proteins of Escherichia coli. I. Purification of 30S ribosomal proteins
    • Hardy, S. J. S., Kurland, C. G., Voynow, P. & Mora, G. (1969) The ribosomal proteins of Escherichia coli. I. Purification of 30S ribosomal proteins, Biochemistry 8, 2897 - 2905.
    • (1969) Biochemistry , vol.8 , pp. 2897-2905
    • Hardy, S.J.S.1    Kurland, C.G.2    Voynow, P.3    Mora, G.4
  • 21
    • 84914773142 scopus 로고
    • Two-dimensional polyacrylamide gel electrophoresis of eukaryotic ribosomal proteins
    • (Moldave, K., ed.) Academic Press, New York
    • Sherton, C. C. & Wool. I. G. (1981) Two-dimensional polyacrylamide gel electrophoresis of eukaryotic ribosomal proteins, in RNA and protein synthesis (Moldave, K., ed.) pp. 683 - 703. Academic Press, New York.
    • (1981) RNA and Protein Synthesis , pp. 683-703
    • Sherton, C.C.1    Wool, I.G.2
  • 22
    • 0018292212 scopus 로고
    • Spot position of rat liver ribosomal proteins by four different two-dimensional electrophoreses in polyacrylamide gel
    • Madjar, J.-J., Arpin, M., Buisson, M. & Reboud, J.-P. (1979) Spot position of rat liver ribosomal proteins by four different two-dimensional electrophoreses in polyacrylamide gel, Mol. & Gen. Genet. 171, 121 - 134.
    • (1979) Mol. & Gen. Genet. , vol.171 , pp. 121-134
    • Madjar, J.-J.1    Arpin, M.2    Buisson, M.3    Reboud, J.-P.4
  • 23
    • 0024280221 scopus 로고
    • Extended N-terminal sequencing of proteins of archeabacterial ribosomes blotted from two-dimensional gels onto glass fiber and polyvinylidene difluoride membrane
    • Walsh, M. J., McDougall, J. & Wittmann-Liebold, B. (1988) Extended N-terminal sequencing of proteins of archeabacterial ribosomes blotted from two-dimensional gels onto glass fiber and polyvinylidene difluoride membrane. Biochemistry 27, 6867 - 6876.
    • (1988) Biochemistry , vol.27 , pp. 6867-6876
    • Walsh, M.J.1    McDougall, J.2    Wittmann-Liebold, B.3
  • 24
    • 0026580898 scopus 로고
    • Internal protein sequence analysis: Enzymatic digestion for less than 10 μg of protein bound to polyvinylidene difluoride or nitrocellulose membranes
    • Fernandez, J., DeMott, M., Atherton, D. & Mische, S. M. (1992) Internal protein sequence analysis: enzymatic digestion for less than 10 μg of protein bound to polyvinylidene difluoride or nitrocellulose membranes, Anal. Biochem. 201, 255 - 264.
    • (1992) Anal. Biochem. , vol.201 , pp. 255-264
    • Fernandez, J.1    DeMott, M.2    Atherton, D.3    Mische, S.M.4
  • 25
    • 0021647719 scopus 로고
    • Application of high performance liquid chromatographic techniques to the separation of ribosomal proteins of different organisins
    • Kamp, R. M., Bosserhoff, A., Kamp, D. & Wittmann-Liebold. B. (1984) Application of high performance liquid chromatographic techniques to the separation of ribosomal proteins of different organisins, J. Chromatogr. 317, 181 - 192.
    • (1984) J. Chromatogr. , vol.317 , pp. 181-192
    • Kamp, R.M.1    Bosserhoff, A.2    Kamp, D.3    Wittmann-Liebold, B.4
  • 26
    • 0024289037 scopus 로고
    • Laser desorption ionization of proteins with molecular masses exceeding 10000 daltons
    • Karas, M. & Hillenkamp, F. (1988) Laser desorption ionization of proteins with molecular masses exceeding 10000 daltons. Anal. Chem. 60, 2299 - 2301.
    • (1988) Anal. Chem. , vol.60 , pp. 2299-2301
    • Karas, M.1    Hillenkamp, F.2
  • 27
    • 0028843017 scopus 로고
    • MALDI-MS for C-terminal sequence determination of peptides and proteins degraded by earboxypeptidase Y and P
    • Thiede, B., Wittmann-Liebold, B., Bienert, M. & Krause, E. (1995) MALDI-MS for C-terminal sequence determination of peptides and proteins degraded by earboxypeptidase Y and P. FEBS Lett. 357, 65 - 69.
    • (1995) FEBS Lett. , vol.357 , pp. 65-69
    • Thiede, B.1    Wittmann-Liebold, B.2    Bienert, M.3    Krause, E.4
  • 28
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparison
    • Person, W. R. & Lipiman, D. J. (1988) Improved tools for biological sequence comparison, Proc. Natl Acad. Sci. USA 85, 2444 - 2448.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 2444-2448
    • Person, W.R.1    Lipiman, D.J.2
  • 29
    • 0014757386 scopus 로고
    • A general method applicable to the search for similarities in the amino acid sequence of two proteins
    • Needleman, S. B. & Wunsch, C. D. (1970) A general method applicable to the search for similarities in the amino acid sequence of two proteins, J. Mol. Biol. 48, 443 - 453.
    • (1970) J. Mol. Biol. , vol.48 , pp. 443-453
    • Needleman, S.B.1    Wunsch, C.D.2
  • 30
    • 0003074704 scopus 로고
    • Sequence comparison and evolution of ribosomal proteins and their genes
    • (Hill, W. E., Dalilberg, A., Garrett, R. A., Moore, P. B., Schlessinger, D. & Warner, J. R., eds) American Society for Microbiology, Washington, DC
    • Wittmann-Liebold, B., Köpke, A. K. E., Arndt, E., Krömer, W., Hatakeyama, T. & Wittmann, H. G. (1990) Sequence comparison and evolution of ribosomal proteins and their genes. in The ribosome, structure, funtion and evolution (Hill, W. E., Dalilberg, A., Garrett, R. A., Moore, P. B., Schlessinger, D. & Warner, J. R., eds) pp. 598 - 616, American Society for Microbiology, Washington, DC.
    • (1990) The Ribosome, Structure, Funtion and Evolution , pp. 598-616
    • Wittmann-Liebold, B.1    Köpke, A.K.E.2    Arndt, E.3    Krömer, W.4    Hatakeyama, T.5    Wittmann, H.G.6
  • 31
    • 0028882951 scopus 로고
    • Cartography of ribosomal proteins of the 30S subunit from the halophilic Haloarcula marismortui and complete sequence analysis of protein HS26
    • Engemann, S., Nölle, R., Herfurth, E., Briesemeister, U., Grelle, G. & Witttmann-Liebold, B. (1995) Cartography of ribosomal proteins of the 30S subunit from the halophilic Haloarcula marismortui and complete sequence analysis of protein HS26, Eur. J. Biochem. 214, 24 - 31.
    • (1995) Eur. J. Biochem. , vol.214 , pp. 24-31
    • Engemann, S.1    Nölle, R.2    Herfurth, E.3    Briesemeister, U.4    Grelle, G.5    Witttmann-Liebold, B.6
  • 32
    • 0014836418 scopus 로고
    • Two-dimensional polyacrylamide gel electrophoresis for fingerprinting of ribosomal proteins
    • Kaltschmidt, E. & Wittmann, H. G. (1970) Two-dimensional polyacrylamide gel electrophoresis for fingerprinting of ribosomal proteins, Anal. Biochem. 36, 401 - 412.
    • (1970) Anal. Biochem. , vol.36 , pp. 401-412
    • Kaltschmidt, E.1    Wittmann, H.G.2
  • 33
    • 0026072648 scopus 로고
    • Isolation of ribosomal subunits containing intact rRNA from human placenta: Estimation of functional activity of 80S ribosomes
    • Matasova, N. B., Myltseva, S. V., Zenkova, M. A., Graifer, D. M., Vladimirov, S. N. & Karpova, G. G. (1991) Isolation of ribosomal subunits containing intact rRNA from human placenta: estimation of functional activity of 80S ribosomes, Anal. Biochem. 198, 219 - 223.
    • (1991) Anal. Biochem. , vol.198 , pp. 219-223
    • Matasova, N.B.1    Myltseva, S.V.2    Zenkova, M.A.3    Graifer, D.M.4    Vladimirov, S.N.5    Karpova, G.G.6
  • 34
    • 0025757141 scopus 로고
    • Rig encodes ribosomal protein S15. The primary structure of mammalian ribosomal protein S15
    • Kitakawa, M., Takasawa, S., Kikuchi, N., Itoh, T., Teraoka, H., Yamamoto, H. & Okamoto, H. (1991 ) Rig encodes ribosomal protein S15. The primary structure of mammalian ribosomal protein S15. FEBS Lett. 283, 210 - 214.
    • (1991) FEBS Lett. , vol.283 , pp. 210-214
    • Kitakawa, M.1    Takasawa, S.2    Kikuchi, N.3    Itoh, T.4    Teraoka, H.5    Yamamoto, H.6    Okamoto, H.7
  • 36
    • 0025231247 scopus 로고
    • The primary structure of rat ribosomal protein S24
    • Chan, Y.-L., Paz, V., Olvera, J. & Wool, I. G. (1990) The primary structure of rat ribosomal protein S24, FEBS Lett. 262, 253 - 255.
    • (1990) FEBS Lett. , vol.262 , pp. 253-255
    • Chan, Y.-L.1    Paz, V.2    Olvera, J.3    Wool, I.G.4
  • 37
    • 0025062790 scopus 로고
    • A cDNA encoding human ribosomal protein S24
    • Brown, S. J., Jewell, A., Maki, C. G. & Roufa, D. J. (1990) A cDNA encoding human ribosomal protein S24, Gene (Amst.) 91, 293 - 296.
    • (1990) Gene (Amst.) , vol.91 , pp. 293-296
    • Brown, S.J.1    Jewell, A.2    Maki, C.G.3    Roufa, D.J.4
  • 38
    • 0028243177 scopus 로고
    • Molecular characterization of the mouse ribosomal protein S24 multigene family - A uniquely expressed intron-containing gene with cell-specific expression of three alternatively spliced mRNAs
    • Xu, L., He, G. P., Li, A. & Ro, H. S. (1994) Molecular characterization of the mouse ribosomal protein S24 multigene family - a uniquely expressed intron-containing gene with cell-specific expression of three alternatively spliced mRNAs. Nucleic Acids Res. 22. 646 - 655.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 646-655
    • Xu, L.1    He, G.P.2    Li, A.3    Ro, H.S.4
  • 39
    • 0028287515 scopus 로고
    • Putative nuclear localization signals (NLS) in protein transcription factors
    • Boulikas, T. (1994) Putative nuclear localization signals (NLS) in protein transcription factors, J. Cell. Biochem. 55, 32 - 58.
    • (1994) J. Cell. Biochem. , vol.55 , pp. 32-58
    • Boulikas, T.1
  • 40
    • 0028085454 scopus 로고
    • Alternative splicing introduces a nuclear localization signal that targets multifunctional CaM kinase to the nucleus
    • Srinivasan, M., Edman, C. F. & Schulman, H. (1994) Alternative splicing introduces a nuclear localization signal that targets multifunctional CaM kinase to the nucleus, J. Cell Biol. 126, 839 - 852.
    • (1994) J. Cell Biol. , vol.126 , pp. 839-852
    • Srinivasan, M.1    Edman, C.F.2    Schulman, H.3


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