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Volumn 114, Issue 4, 1997, Pages 1293-1305

Acidic phosphoprotein complex of the 60S ribosomal subunit of maize seedling roots. Components and changes in response to flooding

Author keywords

[No Author keywords available]

Indexed keywords

60S RIBOSOMAL SUBUNIT; ACIDIC PHOSPHOPROTEIN COMPLEX; BEHAVIOR THERAPY; COMPLEMENTARY DNA; MAIZE; MESSENGER RNA; PHOSPHORYLATION; PLANT DEVELOPMENT; PLANT GROWTH; PLANT ROOT; RIBOSOME; RNA TRANSLATION; SEEDLING; SEQUENCE ANALYSIS; TRANSFER RNA;

EID: 0031200826     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.114.4.1293     Document Type: Article
Times cited : (69)

References (45)
  • 2
    • 0030265734 scopus 로고    scopus 로고
    • The untranslated regions of maize adhl mRNA enhance translation under low oxygen
    • Bailey-Serres J, Dawe RK (1996) The untranslated regions of maize adhl mRNA enhance translation under low oxygen. Plant Physiol 112: 685-695
    • (1996) Plant Physiol , vol.112 , pp. 685-695
    • Bailey-Serres, J.1    Dawe, R.K.2
  • 3
    • 11944250236 scopus 로고
    • Hypoxie stress-induced changes in ribosomes of maize seedling roots
    • Bailey-Serres J, Freeling M (1990) Hypoxie stress-induced changes in ribosomes of maize seedling roots. Plant Physiol 94: 1237-1243
    • (1990) Plant Physiol , vol.94 , pp. 1237-1243
    • Bailey-Serres, J.1    Freeling, M.2
  • 4
    • 0025321217 scopus 로고
    • A gene family for acidic ribosomal proteins in Schizosaccharomyces pombe: Two essential and two nonessential genes
    • Beltrame M, Bianchi ME (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
  • 5
    • 1842361902 scopus 로고
    • Identification and chemical synthesis of a ribosomal protein antigenic determinant in systemic lupus erythematosus
    • Elkon K, Skelly S, Parnassa A, Moller W, Danho W, Weissbach H, Brot N (1986) Identification and chemical synthesis of a ribosomal protein antigenic determinant in systemic lupus erythematosus. Proc Natl Acad Sci USA 83: 7419-7423
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 7419-7423
    • Elkon, K.1    Skelly, S.2    Parnassa, A.3    Moller, W.4    Danho, W.5    Weissbach, H.6    Brot, N.7
  • 6
    • 0029136453 scopus 로고
    • Post-transcriptional regulation of gene expression in oxygen-deprived roots of maize
    • Fennoy SL, Bailey-Serres J (1995) Post-transcriptional regulation of gene expression in oxygen-deprived roots of maize. Plant J 7: 287-295
    • (1995) Plant J , vol.7 , pp. 287-295
    • Fennoy, S.L.1    Bailey-Serres, J.2
  • 7
    • 0027377836 scopus 로고
    • Synthetic peptides and ribosomal proteins as substrate for 60S ribosomal protein kinase from yeast cells
    • Grankowski N, Gasior E, Issinger O-G (1993) Synthetic peptides and ribosomal proteins as substrate for 60S ribosomal protein kinase from yeast cells. Biochim Biophys Acta 1158: 194-196
    • (1993) Biochim Biophys Acta , vol.1158 , pp. 194-196
    • Grankowski, N.1    Gasior, E.2    Issinger, O.-G.3
  • 8
    • 0025826696 scopus 로고
    • Ribosomal proteins PO, PI and P2 are phosphorylated by casein kinase II at their conserved carboxy termini
    • Hasler P, Brot N, Weissbach H, Parnassa AP, Elkon K (1991) Ribosomal proteins PO, PI and P2 are phosphorylated by casein kinase II at their conserved carboxy termini. J Biol Chem 266: 13815-13820
    • (1991) J Biol Chem , vol.266 , pp. 13815-13820
    • Hasler, P.1    Brot, N.2    Weissbach, H.3    Parnassa, A.P.4    Elkon, K.5
  • 9
    • 0028453745 scopus 로고
    • Nucleotide sequence of a rice acidic ribosomal phosphoprotein PO cDNA
    • Hihara Y, Umeda M, Hara C, Toriyama K, Uchimiya H (1994) Nucleotide sequence of a rice acidic ribosomal phosphoprotein PO cDNA. Plant Physiol 105: 753-754
    • (1994) Plant Physiol , vol.105 , pp. 753-754
    • Hihara, Y.1    Umeda, M.2    Hara, C.3    Toriyama, K.4    Uchimiya, H.5
  • 10
    • 0014949207 scopus 로고
    • Cleavage of structral proteins during the assembly of the head of bateriophage T4
    • Laemmli UK (1970) Cleavage of structral proteins during the assembly of the head of bateriophage T4. Nature 227: 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 11
    • 0023741528 scopus 로고
    • Reconstitution of the active rat liver 60S ribosomal subunit from different preparations of core particles and split proteins
    • Lavergne J-P, Marzouki A, Reboud J-P, Reboud A-M (1988) Reconstitution of the active rat liver 60S ribosomal subunit from different preparations of core particles and split proteins. FEBS Lett 236: 345-351
    • (1988) FEBS Lett , vol.236 , pp. 345-351
    • Lavergne, J.-P.1    Marzouki, A.2    Reboud, J.-P.3    Reboud, A.-M.4
  • 12
    • 0026326231 scopus 로고
    • Comparative biochemistry and biophysics of ribosomal proteins
    • Liljas A (1991) Comparative biochemistry and biophysics of ribosomal proteins. Int Rev Cytol 124: 103-135
    • (1991) Int Rev Cytol , vol.124 , pp. 103-135
    • Liljas, A.1
  • 13
    • 0024202789 scopus 로고
    • On the size and the role of a free cytosolic pool of acidic ribosomal proteins in yeast Saccharomyces cerevisiae
    • Mitsui K, Nakagawa T, Tsurugi K (1988) On the size and the role of a free cytosolic pool of acidic ribosomal proteins in yeast Saccharomyces cerevisiae. J Biochem 104: 908-911
    • (1988) J Biochem , vol.104 , pp. 908-911
    • Mitsui, K.1    Nakagawa, T.2    Tsurugi, K.3
  • 14
    • 0000747514 scopus 로고
    • Hypothesis: Ribosomal protein L12 drives movement of tRNA
    • WE Hill, A Dahlberg, RA Garrett, PB Moore, D Schlessinger, JD Warner, eds. American Society of Microbiologists, Washington, DC
    • Möller W (1990) Hypothesis: ribosomal protein L12 drives movement of tRNA. In WE Hill, A Dahlberg, RA Garrett, PB Moore, D Schlessinger, JD Warner, eds. The Ribosome: Structure, Function and Evolution. American Society of Microbiologists, Washington, DC, pp 380-389
    • (1990) The Ribosome: Structure, Function and Evolution , pp. 380-389
    • Möller, W.1
  • 15
    • 0025719209 scopus 로고
    • Phosphorylation controls binding of acidic proteins to the ribosome
    • Naranda T, Ballesta JPG (1991) Phosphorylation controls binding of acidic proteins to the ribosome. Proc Natl Acad Sci USA 88- 10563-10567
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 10563-10567
    • Naranda, T.1    Ballesta, J.P.G.2
  • 16
    • 0027466272 scopus 로고
    • The activity controlling phosphorylation site is not the same in the four acidic ribosomal proteins from Saccharomyces cerevisiae
    • Naranda T, Remacha M, Ballesta JPG (1993) The activity controlling phosphorylation site is not the same in the four acidic ribosomal proteins from Saccharomyces cerevisiae. J Biol Chem 268: 2451-2457
    • (1993) J Biol Chem , vol.268 , pp. 2451-2457
    • Naranda, T.1    Remacha, M.2    Ballesta, J.P.G.3
  • 17
    • 0025014843 scopus 로고
    • A family of genes encode the multiple forms of the Saccharomyces cerevisiae ribosomal proteins equivalent to the Escherichia coll L12 proteiri and a single form of the Ll0-equivalent ribosomal protein
    • Newton CH, Shimmin LC, Yee J, Dennis PP (1990) A family of genes encode the multiple forms of the Saccharomyces cerevisiae ribosomal proteins equivalent to the Escherichia coll L12 proteiri and a single form of the Ll0-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
  • 18
    • 0027530457 scopus 로고
    • Structural and functional domains of Escherichia coli ribosomal protein L7/L12: The hinge region is required for activity
    • Oleinikov AV, Perroud B, Wang B, Traut RR (1993) Structural and functional domains of Escherichia coli ribosomal protein L7/L12: the hinge region is required for activity. J Biol Chem 268: 917-922
    • (1993) J Biol Chem , vol.268 , pp. 917-922
    • Oleinikov, A.V.1    Perroud, B.2    Wang, B.3    Traut, R.R.4
  • 19
    • 0025742662 scopus 로고
    • Phosphorylation of casein kinase II
    • Palen E, Traugh JA (1991) Phosphorylation of casein kinase II. Biochemistry 30: 5586-5590 :
    • (1991) Biochemistry , vol.30 , pp. 5586-5590
    • Palen, E.1    Traugh, J.A.2
  • 20
    • 0027133833 scopus 로고
    • Characterization of ribosomal protein phosphorylation in maize axes during germination
    • Pérez-Méndez A, Aguilar R, Briones E, Sanchez de Jiménez E (1993) Characterization of ribosomal protein phosphorylation in maize axes during germination. Plant Sci 94: 71-79
    • (1993) Plant Sci , vol.94 , pp. 71-79
    • Pérez-Méndez, A.1    Aguilar, R.2    Briones, E.3    Sanchez De Jiménez, E.4
  • 21
    • 0026560274 scopus 로고
    • Specific protein kinase from Saccharomyces cerevisiae cells phosphorylating 60S ribosomal proteins
    • Pilecki M, Grankowski N, Jacobs J, Gasior E (1992) Specific protein kinase from Saccharomyces cerevisiae cells phosphorylating 60S ribosomal proteins. Eur J Biochem 206: 259-267
    • (1992) Eur J Biochem , vol.206 , pp. 259-267
    • Pilecki, M.1    Grankowski, N.2    Jacobs, J.3    Gasior, E.4
  • 22
    • 0029141228 scopus 로고
    • Purification, N-terminal sequencing and properties of wheat embryo acidic ribosomal A proteins with sequence similarity to calmodulin
    • Polya GM, Stapleton D, Morrice N (1995) Purification, N-terminal sequencing and properties of wheat embryo acidic ribosomal A proteins with sequence similarity to calmodulin. Plant Sci 105: 177-188
    • (1995) Plant Sci , vol.105 , pp. 177-188
    • Polya, G.M.1    Stapleton, D.2    Morrice, N.3
  • 23
    • 0028981381 scopus 로고
    • Ribosomal acidic phosphoproteins PI and P2 are not required for cell viability but regulate the pattern of protein expression in Saccharomyces cerevisiae
    • Remacha M, Jimenez-Diaz A, Bermejo B, Rodriguez-Gabriel MA, Guarinos E, Ballesta JPG (1995) Ribosomal acidic phosphoproteins PI and P2 are not required for cell viability but regulate the pattern of protein expression in Saccharomyces 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
  • 24
    • 0025266702 scopus 로고
    • Disruption of single copy genes encoding acidic ribosomal proteins in Saccharomyces cerevisiae
    • Remacha M, Santos C, Ballesta JPG (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
  • 25
    • 0026651735 scopus 로고
    • Stable binding of the eukaryotic acidic phosphoproteins to the ribosome is not an absolute requirement for in vivo protein synthesis
    • Remacha M, Santos C, Bermejo B, Naranda T, Ballesta JPG (1992) Stable binding of the eukaryotic acidic phosphoproteins to the ribosome is not an absolute requirement for in 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
  • 28
    • 0019428163 scopus 로고
    • Effect of phosphorylation on the affinity of acidic proteins from Saccharomyces cerevisiae for the ribosomes
    • Sanchez-Madrid F, Vidales FJ, Ballesta JPG (1981) Effect of phosphorylation on the affinity of acidic proteins from Saccharomyces cerevisiae for the ribosomes. Eur J Biochem 114: 609-613
    • (1981) Eur J Biochem , vol.114 , pp. 609-613
    • Sanchez-Madrid, F.1    Vidales, F.J.2    Ballesta, J.P.G.3
  • 29
    • 0028232189 scopus 로고
    • Ribosomal protein PO, contrary to phosphoproteins PI and P2, is required for ribosome activity and Saccharomyces cerevisiae viability
    • Santos C, Ballesta JPG (1994) Ribosomal protein PO, contrary to phosphoproteins PI and P2, is required for ribosome activity and Saccharomyces cerevisiae viability. J Biol Chem 269: 15689- 15696
    • (1994) J Biol Chem , vol.269 , pp. 15689-15696
    • Santos, C.1    Ballesta, J.P.G.2
  • 31
    • 0002623943 scopus 로고
    • Control of ribosome biosynthesis in plant cell cultures under heat shock conditions. II. Ribosomal proteins
    • Scharf K-D, 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
  • 33
    • 0027637654 scopus 로고
    • Identification and molecular characterization of ZAG1, the maize homolog of the Arabidopsis floral homeotic gene Agamous
    • Schmidt RJ, Veit B, Mandel MA, Mena M, Hake S, Yanofsky M (1993) Identification and molecular characterization of ZAG1, the maize homolog of the Arabidopsis floral homeotic gene Agamous. Plant Cell 5: 729-737
    • (1993) Plant Cell , vol.5 , pp. 729-737
    • Schmidt, R.J.1    Veit, B.2    Mandel, M.A.3    Mena, M.4    Hake, S.5    Yanofsky, M.6
  • 34
    • 0028836318 scopus 로고
    • Purification and partial characterization of an acidic ribosomal protein kinase from maize
    • Sepúlveda G, Aguilar R, Sánchez de Jiménez E (1995) Purification and partial characterization of an acidic ribosomal protein kinase from maize. Physiol Plant 94: 715-721
    • (1995) Physiol Plant , vol.94 , pp. 715-721
    • Sepúlveda, G.1    Aguilar, R.2    Sánchez De Jiménez, E.3
  • 35
    • 0027480627 scopus 로고
    • Replacement of the Lll 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, Musters W, Cundiffe E, Dahlberg AE (1993) Replacement of the Lll 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    Musters, W.2    Cundiffe, E.3    Dahlberg, A.E.4
  • 37
    • 0002989329 scopus 로고
    • Structure and function of Escherichia coli ribosomal protein L7/L12: Effect of cross-links and deletions
    • KH Nierhaus, ed, Plenum Press, New York
    • Traut RR, Oleinikov AV, Makarov E, Jokhadze G, Perroud B, Wang B (1993) Structure and function of Escherichia coli ribosomal protein L7/L12: effect of cross-links and deletions. In KH Nierhaus, ed, The Translational Apparatus, Plenum Press, New York, pp 521-532
    • (1993) The Translational Apparatus , pp. 521-532
    • Traut, R.R.1    Oleinikov, A.V.2    Makarov, E.3    Jokhadze, G.4    Perroud, B.5    Wang, B.6
  • 38
    • 0017842196 scopus 로고
    • Isolation of eukaryotic ribosomal proteins: Purification and characterization of the 60S ribosomal subunit proteins La, Lb, Lf, PI, P2, L13', L14, L18', L20 and L38
    • Tsurugi K, Collatz E, Todokoro K, Ulbrich N, Lightfoot HN, Wool IG (1978) Isolation of eukaryotic ribosomal proteins: purification and characterization of the 60S ribosomal subunit proteins La, Lb, Lf, PI, P2, L13', L14, L18', L20 and L38. J Biol Chem 253: 946-955
    • (1978) J Biol Chem , vol.253 , pp. 946-955
    • Tsurugi, K.1    Collatz, E.2    Todokoro, K.3    Ulbrich, N.4    Lightfoot, H.N.5    Wool, I.G.6
  • 39
    • 3543003676 scopus 로고
    • Nucleotide sequence of a maize (Zea mays L.) cDNA (accession no. U29383) coding for a P2-type acidic ribosomal protein (PGR 95-064)
    • Vangala S, Bailey-Serres J (1995) Nucleotide sequence of a maize (Zea mays L.) cDNA (accession no. U29383) coding for a P2-type acidic ribosomal protein (PGR 95-064). Plant Physiol 109: 721
    • (1995) Plant Physiol , vol.109 , pp. 721
    • Vangala, S.1    Bailey-Serres, J.2
  • 40
    • 0029982589 scopus 로고    scopus 로고
    • Native 3D structure of eukaryotic 80S ribosome: Morphological homology with the E. coli 70S ribosome
    • Verschoor A, Srivastava S, Grassucci R, Frank J (1996) Native 3D structure of eukaryotic 80S ribosome: morphological homology with the E. coli 70S ribosome. J Cell Biol 133: 495-505
    • (1996) J Cell Biol , vol.133 , pp. 495-505
    • Verschoor, A.1    Srivastava, S.2    Grassucci, R.3    Frank, J.4
  • 41
    • 0001095375 scopus 로고
    • Elongation and termination reactions of protein synthesis on maize root tip polyribosomes studied in a homologous cell-free system
    • Webster C, Kim C-Y, Roberts JKM (1991) Elongation and termination reactions of protein synthesis on maize root tip polyribosomes studied in a homologous cell-free system. Plant Physiol 96:418-425
    • (1991) Plant Physiol , vol.96 , pp. 418-425
    • Webster, C.1    Kim, C.-Y.2    Roberts, J.K.M.3
  • 42
    • 0025988131 scopus 로고
    • The primary structure of rat ribosomal proteins PO, PI and P2 and a proposal for a uniform nomenclature for mammalian and yeast ribosomal proteins
    • Wool IG, Chan YL, Gluck A, Suzuki K (1991) The primary structure of rat ribosomal proteins PO, PI and P2 and a proposal for a uniform nomenclature for mammalian and yeast ribosomal proteins. Biochimie 73: 861-870
    • (1991) Biochimie , vol.73 , pp. 861-870
    • Wool, I.G.1    Chan, Y.L.2    Gluck, A.3    Suzuki, K.4
  • 44
    • 0018844581 scopus 로고
    • P5/P5', the acidic ribosomal phosphoproteins from Saccharomyces cerevisiae
    • Zinker S (1980) P5/P5', the acidic ribosomal phosphoproteins from Saccharomyces cerevisiae. Biochim Biophys Acta 606: 76-82
    • (1980) Biochim Biophys Acta , vol.606 , pp. 76-82
    • Zinker, S.1
  • 45
    • 0017256641 scopus 로고
    • The ribosomal proteins of Saccharomyces cerevisiae; phosphorylated and exchangeable proteins
    • Zinker S, Warner JR (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


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