메뉴 건너뛰기




Volumn 46, Issue 3, 2002, Pages 719-792

Characterization of interaction sites in the Saccharomyces cerevisiae ribosomal stalk components

Author keywords

[No Author keywords available]

Indexed keywords

ACID PROTEIN; AMINO ACID; P0 PROTEIN; P1ALPHA PROTEIN; P1BETA PROTEIN; P2ALPHA PROTEIN; P2BETA PROTEIN; PROTEIN EF 2; RIBOSOME PROTEIN; UNCLASSIFIED DRUG;

EID: 0036439195     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.2002.03179.x     Document Type: Article
Times cited : (33)

References (67)
  • 1
    • 0032568584 scopus 로고    scopus 로고
    • Visualization of elongation factor G on the Escherichia coli 70S ribosome: The mechanism of translocation
    • Agrawal, R.K., Penzek, P., Grassucci, R.A., and Frank, J. (1998) Visualization of elongation factor G on the Escherichia coli 70S ribosome: The mechanism of translocation. Proc Natl Acad Sci USA 95: 6134-6138.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6134-6138
    • Agrawal, R.K.1    Penzek, P.2    Grassucci, R.A.3    Frank, J.4
  • 2
    • 0018269897 scopus 로고
    • Isolation and characterization of the acidic phosphoproteins of 60S ribosomes from Artemia salina and rat liver
    • van Agthoven, A., Kriek, J., Amons, R., and Möller, W. (1978) Isolation and characterization of the acidic phosphoproteins of 60S ribosomes from Artemia salina and rat liver. Eur J Biochem 91: 553-556.
    • (1978) Eur J Biochem , vol.91 , pp. 553-556
    • Van Agthoven, A.1    Kriek, J.2    Amons, R.3    Möller, W.4
  • 3
    • 0029686290 scopus 로고    scopus 로고
    • The large ribosomal subunit stalk as a regulatory element of the eukaryotic translational machinery
    • Ballesta, J.P.G., and Remacha, M. (1996) The large ribosomal subunit stalk as a regulatory element of the eukaryotic translational machinery. Progr Nucleic Acid Res Mol Biol 55: 157-193.
    • (1996) Progr Nucleic Acid Res Mol Biol , vol.55 , pp. 157-193
    • Ballesta, J.P.G.1    Remacha, M.2
  • 5
    • 0030045605 scopus 로고    scopus 로고
    • A protein linkage map of Escherichia coli bacteriophage T7
    • Bartel, P.L., Roecklein, J.A., SenGupta, D., and Fields, S. (1996) A protein linkage map of Escherichia coli bacteriophage T7. Nature Genet 12: 72-77.
    • (1996) Nature Genet , vol.12 , pp. 72-77
    • Bartel, P.L.1    Roecklein, J.A.2    SenGupta, D.3    Fields, S.4
  • 6
    • 0025321217 scopus 로고
    • A gene family for acidic ribosomal proteins in Schizosaccharomyces pombe: Two essential and two nonessential genes
    • Beltrame, M., and Bianchi, M.E. (1990) A gene family for acidic ribosomal proteins in Schizosaccharomyces pombe: Two essential and two nonessential genes. Mol Cell Biol 10: 2341-2348.
    • (1990) Mol Cell Biol , vol.10 , pp. 2341-2348
    • Beltrame, M.1    Bianchi, M.E.2
  • 7
    • 0032570582 scopus 로고    scopus 로고
    • Conformational independence of N-and C-domains in ribosomal protein L7/L12 and in the complex with protein L10
    • Bocharov, E.V., Gudkov, A.T., Budovskaya, E.V., and Arseniev, A.S. (1998) Conformational independence of N-and C-domains in ribosomal protein L7/L12 and in the complex with protein L10. FEBS Lett 423: 347-350.
    • (1998) FEBS Lett , vol.423 , pp. 347-350
    • Bocharov, E.V.1    Gudkov, A.T.2    Budovskaya, E.V.3    Arseniev, A.S.4
  • 8
    • 0025785410 scopus 로고
    • A family of low and high copy replicative, integrative and single-stranded S. cerevisiae/E. coli shuttle vectors
    • Bonneaud, N., Ozier-Kalogeropoulos, O., Li, G., Labouesse, M., Minvielle-Sebastia, L., and Lacroute, F. (1991) A family of low and high copy replicative, integrative and single-stranded S. cerevisiae/E. coli shuttle vectors. Yeast 7: 609-615.
    • (1991) Yeast , vol.7 , pp. 609-615
    • Bonneaud, N.1    Ozier-Kalogeropoulos, O.2    Li, G.3    Labouesse, M.4    Minvielle-Sebastia, L.5    Lacroute, F.6
  • 9
    • 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. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 10
    • 0033610787 scopus 로고    scopus 로고
    • The GTPase center protein L12 is required for correct ribosomal stalk assembly but not for Saccharomyces cerevisiae viability
    • Briones, E., Briones, C., Remacha, M., and Ballesta, J.P.G. (1998) The GTPase center protein L12 is required for correct ribosomal stalk assembly but not for Saccharomyces cerevisiae viability. J Biol Chem 273: 31956-31961.
    • (1998) J Biol Chem , vol.273 , pp. 31956-31961
    • Briones, E.1    Briones, C.2    Remacha, M.3    Ballesta, J.P.G.4
  • 11
    • 0025940629 scopus 로고
    • The two-hybrids system: A method to identify and clone genes for proteins that interact with a protein of interest
    • Chien, C.-T., Bartel, P.L., Sternglatz, R., and Fields, S. (1991) The two-hybrids system: A method to identify and clone genes for proteins that interact with a protein of interest. Proc Natl Acad Sci USA 88: 9578-9582.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 9578-9582
    • Chien, C.-T.1    Bartel, P.L.2    Sternglatz, R.3    Fields, S.4
  • 12
    • 0028568056 scopus 로고
    • Interaction mating reveals binary and ternary connections between Drosophila cell cycle regulators
    • Finley, R.L., Jr, and Brent, R. (1994) Interaction mating reveals binary and ternary connections between Drosophila cell cycle regulators. Proc Natl Acad Sci USA 91: 12980-12984.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12980-12984
    • Finley R.L., Jr.1    Brent, R.2
  • 14
    • 0030963019 scopus 로고    scopus 로고
    • Toward a functional analysis of the yeast genome through exhaustive two-hybrid screens
    • Fromont-Racine, M., Rain, J.C., and Legrain, P. (1997) Toward a functional analysis of the yeast genome through exhaustive two-hybrid screens. Nature Genet 16: 277-282.
    • (1997) Nature Genet , vol.16 , pp. 277-282
    • Fromont-Racine, M.1    Rain, J.C.2    Legrain, P.3
  • 15
    • 0002819495 scopus 로고
    • High efficiency transformation with lithium acetate
    • Johnston, J.R. (ed.). Oxford: IRL Press
    • Gietz, R., and Woods, R. (1994) High efficiency transformation with lithium acetate. In Molecular Genetics of Yeast, a Practical Approach. Johnston, J.R. (ed.). Oxford: IRL Press, pp. 121-134.
    • (1994) Molecular Genetics of Yeast, a Practical Approach , pp. 121-134
    • Gietz, R.1    Woods, R.2
  • 16
    • 18744420805 scopus 로고    scopus 로고
    • Three-dimensional Cryo-EM Localization of EF2 in the Saccharomyces cerevisiae 80S Ribosome at 17.5 Å Resolution
    • Gómez-Lorenzo, M.G., Spahn, C.M.T., Agrawal, R.K., Grassucci, R.A., Penczek, P., Chakraburtty, K., et al. (2000) Three-dimensional Cryo-EM Localization of EF2 in the Saccharomyces cerevisiae 80S Ribosome at 17.5 Å Resolution. EMBO J 19: 2710-2718.
    • (2000) EMBO J , vol.19 , pp. 2710-2718
    • Gómez-Lorenzo, M.G.1    Spahn, C.M.T.2    Agrawal, R.K.3    Grassucci, R.A.4    Penczek, P.5    Chakraburtty, K.6
  • 17
    • 0035827659 scopus 로고    scopus 로고
    • Pivotal role of the p1 n-terminal domain in the assembly of the mammalian ribosomal stalk and in the proteosynthetic activity
    • Gonzalo, P., Lavergne, J.P., and Reboud, J.P. (2001) Pivotal role of the p1 n-terminal domain in the assembly of the mammalian ribosomal stalk and in the proteosynthetic activity. J Biol Chem 276: 19762-19769.
    • (2001) J Biol Chem , vol.276 , pp. 19762-19769
    • Gonzalo, P.1    Lavergne, J.P.2    Reboud, J.P.3
  • 18
    • 0035980142 scopus 로고    scopus 로고
    • Asymetric interactions between the acidic P1 and P2 proteins in the Saccharomyces cerevisiae ribosomal stalk
    • Guarinos, E., Remacha, M., and Ballesta, J.P.G. (2001) Asymetric interactions between the acidic P1 and P2 proteins in the Saccharomyces cerevisiae ribosomal stalk. J Biol Chem 276: 32474-32479.
    • (2001) J Biol Chem , vol.276 , pp. 32474-32479
    • Guarinos, E.1    Remacha, M.2    Ballesta, J.P.G.3
  • 19
    • 0030941216 scopus 로고    scopus 로고
    • The L7/L12 ribosomal domain of the ribosome: Structural and functional studies
    • Gudkov, A.T. (1997) The L7/L12 ribosomal domain of the ribosome: Structural and functional studies. FEBS Lett 407: 253-256.
    • (1997) FEBS Lett , vol.407 , pp. 253-256
    • Gudkov, A.T.1
  • 20
    • 0000075317 scopus 로고
    • Techniques for transformation of E. coli
    • Glover, D.M. (ed.). Oxford: IRL Press
    • Hanahan, D. (1985) Techniques for transformation of E. coli. In DNA Cloning: A Practical Approach. Glover, D.M. (ed.). Oxford: IRL Press, pp. 109-136.
    • (1985) DNA Cloning: A Practical Approach , pp. 109-136
    • Hanahan, D.1
  • 21
    • 0025938044 scopus 로고
    • DMSO-enhanced whole cell yeast transformation
    • Hill, H., Donald, I.G., and Griffiths, D.E. (1991) DMSO-enhanced whole cell yeast transformation. Nucleic Acids Res 19: 5791.
    • (1991) Nucleic Acids Res , vol.19 , pp. 5791
    • Hill, H.1    Donald, I.G.2    Griffiths, D.E.3
  • 22
    • 0033974688 scopus 로고    scopus 로고
    • Towards a protei-protein interaction map of the budding yeast: A comprehensive system to examine two-hybrid interactions in all possible combinations between the yeast proteins
    • Ito, T., Tashiro, K., Muta, S., Ozawa, R., Chiba, T., Nishizawa, M., et al. (2000) Towards a protei-protein interaction map of the budding yeast: A comprehensive system to examine two-hybrid interactions in all possible combinations between the yeast proteins. Proc Natl Acad Sci USA 97: 1143-1147.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 1143-1147
    • Ito, T.1    Tashiro, K.2    Muta, S.3    Ozawa, R.4    Chiba, T.5    Nishizawa, M.6
  • 23
    • 0035836765 scopus 로고    scopus 로고
    • A comprehensive two-hybrid analysis to explore the yeast protein interactome
    • Ito, T., Chiba, T., Ozawa, R., Yoshida, M., Hattori, M., and Sakaki, Y. (2001) A comprehensive two-hybrid analysis to explore the yeast protein interactome. Proc Natl Acad Sci USA 98: 4569-4574.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 4569-4574
    • Ito, T.1    Chiba, T.2    Ozawa, R.3    Yoshida, M.4    Hattori, M.5    Sakaki, Y.6
  • 24
    • 0021765649 scopus 로고
    • Acidic proteins of the large ribosomal subunit in Saccharomyces cerevisiae. Effect of phosphorylation
    • Juan-Vidales, F., Saenz-Robles, M.T., and Ballesta, J.P.G. (1984) Acidic proteins of the large ribosomal subunit in Saccharomyces cerevisiae. Effect of phosphorylation. Biochemistry 23: 390-396.
    • (1984) Biochemistry , vol.23 , pp. 390-396
    • Juan-Vidales, F.1    Saenz-Robles, M.T.2    Ballesta, J.P.G.3
  • 25
    • 0027229973 scopus 로고
    • A multifunctional prokaryotic protein expression system: Overproduction, affinity purification, and selective detection
    • Kroll, D.J., Abdel-Malek Abdel-Hafiz, H., Marcell, T., Simpson, S., Chen, C.Y., Gutierrez-Hartmann, A., et al. (1993) A multifunctional prokaryotic protein expression system: Overproduction, affinity purification, and selective detection. DNA Cell Biol 12: 441-453.
    • (1993) DNA Cell Biol , vol.12 , pp. 441-453
    • Kroll, D.J.1    Abdel-Malek Abdel-Hafiz, H.2    Marcell, T.3    Simpson, S.4    Chen, C.Y.5    Gutierrez-Hartmann, A.6
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 0023664506 scopus 로고
    • Role of acidic phosphoproteins in the partial reconstitution of the active 60S ribosomal subunit
    • Lavergne, J.-P., Conquet, F., Reboud, J.P., and Reboud, A.-M. (1987) Role of acidic phosphoproteins in the partial reconstitution of the active 60S ribosomal subunit. FEBS Lett 216: 83-88.
    • (1987) FEBS Lett , vol.216 , pp. 83-88
    • Lavergne, J.-P.1    Conquet, F.2    Reboud, J.P.3    Reboud, A.-M.4
  • 28
    • 0029608909 scopus 로고
    • Ribosomal proteins and elongation factors
    • Liljas, A., and Garber, M. (1995) Ribosomal proteins and elongation factors. Curr Opin Struct Biol 5: 721-727.
    • (1995) Curr Opin Struct Biol , vol.5 , pp. 721-727
    • Liljas, A.1    Garber, M.2
  • 29
    • 0020490682 scopus 로고
    • The activity of the acidic phophoproteins from the 80S rat liver ribosome
    • MacConnell, W.P., and Kaplan, N.O. (1982) The activity of the acidic phophoproteins from the 80S rat liver ribosome. J Biol Chem 257: 5359-5366.
    • (1982) J Biol Chem , vol.257 , pp. 5359-5366
    • MacConnell, W.P.1    Kaplan, N.O.2
  • 30
    • 0001115404 scopus 로고
    • On the structure, function and dynamics of L7/12 from Escherichia coli ribosomes
    • Hardesty, B., and Kramer, G. (eds). New York: Springer-Verlag
    • Möller, W., and Maassen, J.A. (1986) On the structure, function and dynamics of L7/12 from Escherichia coli ribosomes. In Structure, Function and Genetics of Ribosomes. Hardesty, B., and Kramer, G. (eds). New York: Springer-Verlag, pp. 309-325.
    • (1986) Structure, Function and Genetics of Ribosomes , pp. 309-325
    • Möller, W.1    Maassen, J.A.2
  • 31
    • 0026016509 scopus 로고
    • The conserved GTPase center and variable V9 from Saccharomyces cerevisiae 26S rRNA can be replaced by their equivalent from other prokaryotes or eukaryotes without detectable loss of ribosomal function
    • Musters, W., Gonzalves, P.M., Boon, K., Raué, H.A., van Heerikhuizen, H., and Planta, R.J. (1991) The conserved GTPase center and variable V9 from Saccharomyces cerevisiae 26S rRNA can be replaced by their equivalent from other prokaryotes or eukaryotes without detectable loss of ribosomal function. Proc Natl Acad Sci USA 88: 1469-1473.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 1469-1473
    • Musters, W.1    Gonzalves, P.M.2    Boon, K.3    Raué, H.A.4    Van Heerikhuizen, H.5    Planta, R.J.6
  • 32
    • 0025014843 scopus 로고
    • A family of genes encode the multiple forms of the Saccharomyces cerevisiae ribosomal proteins equivalent to the Escherichia coli L12 protein and a single form of the L10-equivalent ribosomal protein
    • Newton, C.H., Shimmin, L.C., Yee, J., and Dennis, P.P. (1990) A family of genes encode the multiple forms of the Saccharomyces cerevisiae ribosomal proteins equivalent to the Escherichia coli L12 protein and a single form of the L10-equivalent ribosomal protein. J Bacteriol 172: 579-588.
    • (1990) J Bacteriol , vol.172 , pp. 579-588
    • Newton, C.H.1    Shimmin, L.C.2    Yee, J.3    Dennis, P.P.4
  • 33
    • 0034669118 scopus 로고    scopus 로고
    • Phosphorylation and N-end region of the yeast ribosomal protein P1 mediate its degradation, which is prevented by protein P2
    • Nusspaumer, G., Remacha, M., and Ballesta, J.P.G. (2000) Phosphorylation and N-end region of the yeast ribosomal protein P1 mediate its degradation, which is prevented by protein P2. EMBO J 19: 6075-6084.
    • (2000) EMBO J , vol.19 , pp. 6075-6084
    • Nusspaumer, G.1    Remacha, M.2    Ballesta, J.P.G.3
  • 34
    • 0017121519 scopus 로고
    • The ribosomal protein L8 is a complex of L7/L12 and L10
    • Pettersson, I., Hardy, S.J., and Liljas, A. (1976) The ribosomal protein L8 is a complex of L7/L12 and L10. FEBS Lett 64: 135-138.
    • (1976) FEBS Lett , vol.64 , pp. 135-138
    • Pettersson, I.1    Hardy, S.J.2    Liljas, A.3
  • 35
    • 0023952119 scopus 로고
    • Independent genes coding for three acidic proteins of the large ribosomal subunit from Saccharomyces cerevisae
    • Remacha, M., Saenz-Robles, M.T., Vilella, M.D., and Ballesta, J.P.G. (1988) Independent genes coding for three acidic proteins of the large ribosomal subunit from Saccharomyces cerevisae. J Biol Chem 263: 9094-9101.
    • (1988) J Biol Chem , vol.263 , pp. 9094-9101
    • Remacha, M.1    Saenz-Robles, M.T.2    Vilella, M.D.3    Ballesta, J.P.G.4
  • 36
    • 0025266702 scopus 로고
    • Disruption of single-copy genes encoding acidic ribosomal proteins in Saccharomyces cerevisiae
    • Remacha, M., Santos, C., and Ballesta, J.P.G. (1990) Disruption of single-copy genes encoding acidic ribosomal proteins in Saccharomyces cerevisiae. Mol Cell Biol 10: 2182-2190.
    • (1990) Mol Cell Biol , vol.10 , pp. 2182-2190
    • Remacha, M.1    Santos, C.2    Ballesta, J.P.G.3
  • 37
    • 0026651735 scopus 로고
    • Stable binding of the eukaryotic acidic phosphoproteins to the ribosome is not an absolute requirement forin vivo protein synthesis
    • Remacha, M., Santos, C., Bermejo, B., Naranda, T., and Ballesta, J.P.G. (1992) Stable binding of the eukaryotic acidic phosphoproteins to the ribosome is not an absolute requirement forin vivo protein synthesis. J Biol Chem 267: 12061-12067.
    • (1992) J Biol Chem , vol.267 , pp. 12061-12067
    • Remacha, M.1    Santos, C.2    Bermejo, B.3    Naranda, T.4    Ballesta, J.P.G.5
  • 38
    • 0028981381 scopus 로고
    • Ribosomal acidic phosphoproteins P1 and P2 are not required for cell viability but regulate the pattern of protein expression inSaccharomyces cerevisiae
    • Remacha, M., Jimenez-Diaz, A., Bermejo, B., Rodriguez-Gabriel, M.A., Guarinos, E., and Ballesta, J.P.G. (1995) Ribosomal acidic phosphoproteins P1 and P2 are not required for cell viability but regulate the pattern of protein expression inSaccharomyces cerevisiae. Mol Cell Biol 15: 4754-4762.
    • (1995) Mol Cell Biol , vol.15 , pp. 4754-4762
    • Remacha, M.1    Jimenez-Diaz, A.2    Bermejo, B.3    Rodriguez-Gabriel, M.A.4    Guarinos, E.5    Ballesta, J.P.G.6
  • 39
    • 0017715736 scopus 로고
    • Exchange of ribosomal proteins among the ribosomes of Escherichia coli
    • Robertson, W.R., Dowsett, S.J., and Hardy, S.J. (1977) Exchange of ribosomal proteins among the ribosomes of Escherichia coli. Mol Gen Genet 157: 205-214.
    • (1977) Mol Gen Genet , vol.157 , pp. 205-214
    • Robertson, W.R.1    Dowsett, S.J.2    Hardy, S.J.3
  • 40
    • 0040016327 scopus 로고    scopus 로고
    • The RNA interacting domain but not the protein interacting domain is highly conserved in ribosomal protein P0
    • Rodriguez-Gabriel, M.A., Remacha, M., and Ballesta, J.P.G. (2000) The RNA interacting domain but not the protein interacting domain is highly conserved in ribosomal protein P0. J Biol Chem 275: 2130-2136.
    • (2000) J Biol Chem , vol.275 , pp. 2130-2136
    • Rodriguez-Gabriel, M.A.1    Remacha, M.2    Ballesta, J.P.G.3
  • 43
    • 0018507922 scopus 로고
    • Acidic ribosomal proteins from eukaryotic cells. Effect on ribosomal functions
    • Sanchez-Madrid, F., Reyes, R., Conde, P., and Ballesta, J.P.G. (1979)) Acidic ribosomal proteins from eukaryotic cells. Effect on ribosomal functions. Eur J Biochem 98: 409-416.
    • (1979) Eur J Biochem , vol.98 , pp. 409-416
    • Sanchez-Madrid, F.1    Reyes, R.2    Conde, P.3    Ballesta, J.P.G.4
  • 44
    • 0029135319 scopus 로고
    • The highly conserved protein P0 carboxyl end is essential for ribosome activity only in the absence of proteins P1 and P2
    • Santos, C., and Ballesta, J.P.G. (1995) The highly conserved protein P0 carboxyl end is essential for ribosome activity only in the absence of proteins P1 and P2. J Biol Chem 270: 20608-20614.
    • (1995) J Biol Chem , vol.270 , pp. 20608-20614
    • Santos, C.1    Ballesta, J.P.G.2
  • 45
    • 0002623943 scopus 로고
    • Control of ribosome biosynthesis in plant cell cultures under heat shock conditions. II. Ribosomal proteins
    • Scharf, K.-D., and Nover, L. (1987) Control of ribosome biosynthesis in plant cell cultures under heat shock conditions. II. Ribosomal proteins. Biochim Biophys Acta 909: 44-57.
    • (1987) Biochim Biophys Acta , vol.909 , pp. 44-57
    • Scharf, K.-D.1    Nover, L.2
  • 47
    • 0037096782 scopus 로고    scopus 로고
    • Interaction among silkworm ribosomal proteins P1, P2 and P0 required for functional protein binding to the GTPase-associated domain of 28S rRNA
    • Shimizu, T., Nakagaki, M., Nishi, Y., Kobayashi, Y., Hachimori, A., and Uchiumi, T. (2002) Interaction among silkworm ribosomal proteins P1, P2 and P0 required for functional protein binding to the GTPase-associated domain of 28S rRNA. Nucleic Acids Res 30: 2620-2627.
    • (2002) Nucleic Acids Res , vol.30 , pp. 2620-2627
    • Shimizu, T.1    Nakagaki, M.2    Nishi, Y.3    Kobayashi, Y.4    Hachimori, A.5    Uchiumi, T.6
  • 48
    • 0024448354 scopus 로고
    • Sequence alignment and evolutionary comparison of the L10 equivalent and L12 equivalent ribosomal proteins from archaebacterial, eubacterial and eukaryotes
    • Shimmin, L.C., Ramirez, G., Matheson, A.T., and Dennis, P.P. (1989) Sequence alignment and evolutionary comparison of the L10 equivalent and L12 equivalent ribosomal proteins from archaebacterial, eubacterial and eukaryotes. J Mol Evol 29: 448-462.
    • (1989) J Mol Evol , vol.29 , pp. 448-462
    • Shimmin, L.C.1    Ramirez, G.2    Matheson, A.T.3    Dennis, P.P.4
  • 51
    • 0016787665 scopus 로고
    • Copies of proteins L7 and L12 and heterogeneity of the large subunit ofEscherichia coli ribosome
    • Subramanian, A.R. (1975) Copies of proteins L7 and L12 and heterogeneity of the large subunit ofEscherichia coli ribosome. J Mol Biol 95: 1-8.
    • (1975) J Mol Biol , vol.95 , pp. 1-8
    • Subramanian, A.R.1
  • 52
    • 0032478087 scopus 로고    scopus 로고
    • Evolutionary analyses of the 12-kDa acidic ribosomal P-proteins reveal a distinct protein of higher plant ribosomes
    • Szick, K., Springer, M., and Bailey-Serres, J. (1998) Evolutionary analyses of the 12-kDa acidic ribosomal P-proteins reveal a distinct protein of higher plant ribosomes. Proc Natl Acad Sci USA 95: 2378-2383.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 2378-2383
    • Szick, K.1    Springer, M.2    Bailey-Serres, J.3
  • 53
    • 0034237451 scopus 로고    scopus 로고
    • Analysis of the protein-protein interactions between the human acidic ribosomal P-proteins: Evaluation by the two hybrid system
    • Tchorzewski, M., Boldyreff, B., Issinger, O., and Grankowski, N. (2000) Analysis of the protein-protein interactions between the human acidic ribosomal P-proteins: Evaluation by the two hybrid system. Int J Biochem Cell Biol 32: 737-746.
    • (2000) Int J Biochem Cell Biol , vol.32 , pp. 737-746
    • Tchorzewski, M.1    Boldyreff, B.2    Issinger, O.3    Grankowski, N.4
  • 54
    • 0027480627 scopus 로고
    • Replacement of the L11 binding region within E. coli 23S ribosomal RNA with its homologue from yeast: In vivo and in vitro analysis of hybrid ribosomes altered in the GTPase centre
    • Thompson, J., Muster, W., Cundliffe, E., and Dahlberg, A.E. (1993) Replacement of the L11 binding region within E. coli 23S ribosomal RNA with its homologue from yeast: In vivo and in vitro analysis of hybrid ribosomes altered in the GTPase centre. EMBO J 12: 1499-1504.
    • (1993) EMBO J , vol.12 , pp. 1499-1504
    • Thompson, J.1    Muster, W.2    Cundliffe, E.3    Dahlberg, A.E.4
  • 55
    • 0020479805 scopus 로고
    • Monoclonal antibodies against eukaryotic ribosomes. Use to characterize a ribosomal protein not previously identified and genetically related to the acidic phosphoproteins P1/P2
    • Towbin, G., Siegmann, M., and Gordon, J. (1982) Monoclonal antibodies against eukaryotic ribosomes. Use to characterize a ribosomal protein not previously identified and genetically related to the acidic phosphoproteins P1/P2. J Biol Chem 257: 12709-12715.
    • (1982) J Biol Chem , vol.257 , pp. 12709-12715
    • Towbin, G.1    Siegmann, M.2    Gordon, J.3
  • 56
    • 0022369647 scopus 로고
    • Evidence for the exchangeability of acidic ribosomal proteins on cytoplasmic ribosomes in regenerating rat liver
    • Tsurugi, K., and Ogata, K. (1985) Evidence for the exchangeability of acidic ribosomal proteins on cytoplasmic ribosomes in regenerating rat liver. J Biochem 98: 1427-1431.
    • (1985) J Biochem , vol.98 , pp. 1427-1431
    • Tsurugi, K.1    Ogata, K.2
  • 57
    • 0026703192 scopus 로고
    • Direct evidence for interaction of the conserved GTPase domain within 28S RNA with mammalian ribosomal acidic phosphoproteins and L12
    • Uchiumi, T., and Kominami, R. (1992) Direct evidence for interaction of the conserved GTPase domain within 28S RNA with mammalian ribosomal acidic phosphoproteins and L12. J Biol Chem 267: 19179-19185.
    • (1992) J Biol Chem , vol.267 , pp. 19179-19185
    • Uchiumi, T.1    Kominami, R.2
  • 58
    • 0022701927 scopus 로고
    • Cross-linking of elongation factor 2 to rat liver ribosomal proteins by 2-iminothiolane
    • Uchiumi, T., Kikuchi, M., Terao, K., Iwasaki, K., and Ogata, K. (1986) Cross-linking of elongation factor 2 to rat liver ribosomal proteins by 2-iminothiolane. Eur J Biochem 156: 37-48.
    • (1986) Eur J Biochem , vol.156 , pp. 37-48
    • Uchiumi, T.1    Kikuchi, M.2    Terao, K.3    Iwasaki, K.4    Ogata, K.5
  • 59
    • 0023393132 scopus 로고
    • Topography and stoichiometry of acidic proteins in large ribosomal subunits from Artemia salina as determined by crosslinking
    • Uchiumi, T., Wahba, A.J., and Traut, R.R. (1987) Topography and stoichiometry of acidic proteins in large ribosomal subunits from Artemia salina as determined by crosslinking. Proc Natl Acad Sci USA 84: 5580-5584.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 5580-5584
    • Uchiumi, T.1    Wahba, A.J.2    Traut, R.R.3
  • 60
    • 0034628508 scopus 로고    scopus 로고
    • A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae
    • Uetz, P., Giot, L., Cagney, G., Mansfield, T.A., Judson, R.S., Knight, J.R., et al. (2000) A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae. Nature 403: 623-627.
    • (2000) Nature , vol.403 , pp. 623-627
    • Uetz, P.1    Giot, L.2    Cagney, G.3    Mansfield, T.A.4    Judson, R.S.5    Knight, J.R.6
  • 61
    • 0026035948 scopus 로고
    • Characterization of the yeast acidic ribosomal phosphoproteins using monoclonal antibodies. Proteins L44/L45 and L44′ have different functional roles
    • Vilella, M.D., Remacha, M., Ortiz, B.L., Mendez, E., and Ballesta, J.P.G. (1991) Characterization of the yeast acidic ribosomal phosphoproteins using monoclonal antibodies. Proteins L44/L45 and L44′ have different functional roles. Eur J Biochem 196: 407-414.
    • (1991) Eur J Biochem , vol.196 , pp. 407-414
    • Vilella, M.D.1    Remacha, M.2    Ortiz, B.L.3    Mendez, E.4    Ballesta, J.P.G.5
  • 62
    • 0025988131 scopus 로고
    • Characterization of the yeast acidic ribosomal phosphoproteins using monoclonal antibodies. Proteins L44/L45 and L44′ have different functional roles
    • Wool, I.G., Chan, Y.L., Glück, A., and Suzuki, K. (1991) Characterization of the yeast acidic ribosomal phosphoproteins using monoclonal antibodies. Proteins L44/L45 and L44′ have different functional roles. Biochimie 73: 861-870.
    • (1991) Biochimie , vol.73 , pp. 861-870
    • Wool, I.G.1    Chan, Y.L.2    Glück, A.3    Suzuki, K.4
  • 63
    • 0030711636 scopus 로고    scopus 로고
    • Phosphorylation of the acidic ribosomal P proteins inSaccharomyces cerevisiae. A reappraisal
    • Zambrano, R., Briones, E., Remacha, M., and Ballesta, J.P.G. (1997) Phosphorylation of the acidic ribosomal P proteins inSaccharomyces cerevisiae. A reappraisal. Biochemistry 36: 14439-14446.
    • (1997) Biochemistry , vol.36 , pp. 14439-14446
    • Zambrano, R.1    Briones, E.2    Remacha, M.3    Ballesta, J.P.G.4
  • 64
    • 0017256641 scopus 로고
    • The ribosomal proteins of Saccharomyces cerevisiae. Phosphorylated and exchangeable proteins
    • Zinker, S., and Warner, J.R. (1976) The ribosomal proteins of Saccharomyces cerevisiae. Phosphorylated and exchangeable proteins. J Biol Chem 251: 1799-1807.
    • (1976) J Biol Chem , vol.251 , pp. 1799-1807
    • Zinker, S.1    Warner, J.R.2
  • 65
    • 0030739177 scopus 로고    scopus 로고
    • The exchangeable yeast ribosomal acidic protein YP2βeta shows characteristics of a partly folded state under physiological conditions
    • Zurdo, J., Sanz, J.M., Gonzalez, C., Rico, M., and Ballesta, J.P.G. (1997) The exchangeable yeast ribosomal acidic protein YP2βeta shows characteristics of a partly folded state under physiological conditions. Biochemistry 36: 9625-9635.
    • (1997) Biochemistry , vol.36 , pp. 9625-9635
    • Zurdo, J.1    Sanz, J.M.2    Gonzalez, C.3    Rico, M.4    Ballesta, J.P.G.5
  • 66
    • 0034254519 scopus 로고    scopus 로고
    • Structural differences between Saccharomyces cerevisiae ribosomal stalk proteins P1 and P2 support their functional diversity
    • Zurdo, J., Gonzalez, C., Sanz, J.M., Rico, M., Remacha, M., and Ballesta, J.P.G. (2000a) Structural differences between Saccharomyces cerevisiae ribosomal stalk proteins P1 and P2 support their functional diversity. Biochemistry 39: 8935-8943.
    • (2000) Biochemistry , vol.39 , pp. 8935-8943
    • Zurdo, J.1    Gonzalez, C.2    Sanz, J.M.3    Rico, M.4    Remacha, M.5    Ballesta, J.P.G.6
  • 67
    • 0034254658 scopus 로고    scopus 로고
    • Assembly of Saccharomyces cerevisiae ribosomal stalk: Binding of P1 proteins is required for the interaccion of P2 proteins
    • Zurdo, J., van den Berg, A., Parada, P., Nusspaumer, G., Jimenez-Diaz, A., Remacha, M., and Ballesta, J.P.G. (2000b) Assembly of Saccharomyces cerevisiae ribosomal stalk: Binding of P1 proteins is required for the interaccion of P2 proteins. Biochemistry 39: 8929-8934.
    • (2000) Biochemistry , vol.39 , pp. 8929-8934
    • Zurdo, J.1    Van den Berg, A.2    Parada, P.3    Nusspaumer, G.4    Jimenez-Diaz, A.5    Remacha, M.6    Ballesta, J.P.G.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.