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Volumn 39, Issue 11, 2011, Pages 4587-4597

Translational recoding as a feedback controller: Systems approaches reveal polyamine-specific effects on the antizyme ribosomal frameshift

Author keywords

[No Author keywords available]

Indexed keywords

PLASMID VECTOR; PROTEIN OAZ1; PUTRESCINE; SACCHAROMYCES CEREVISIAE PROTEIN; SPERMIDINE; SPERMINE; UNCLASSIFIED DRUG;

EID: 79959446944     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkq1349     Document Type: Article
Times cited : (34)

References (42)
  • 1
    • 0345688128 scopus 로고    scopus 로고
    • A perspective of polyamine metabolism
    • DOI 10.1042/BJ20031327
    • Wallace, H.M., Fraser, A.V. and Hughes, A. (2003) A perspective of polyamine metabolism. Biochem. J., 376, 1-14. (Pubitemid 37487199)
    • (2003) Biochemical Journal , vol.376 , Issue.1 , pp. 1-14
    • Wallace, H.M.1    Fraser, A.V.2    Hughes, A.3
  • 2
    • 4143049044 scopus 로고    scopus 로고
    • Inhibitors of polyamine metabolism
    • Wallace, H.M. and Fraser, A.V. (2004) Inhibitors of polyamine metabolism. Amino Acids, 26, 353-365.
    • (2004) Amino Acids , vol.26 , pp. 353-365
    • Wallace, H.M.1    Fraser, A.V.2
  • 3
    • 0027462162 scopus 로고
    • Enhancement of the spermidine uptake system and lethal effects of spermidine overaccumulation in ornithine decarboxylase-overproducing L1210 cells under hyposmotic stress
    • Poulin, R., Coward, J.K., Lakanen, J.R. and Pegg, A.E. (1993) Enhancement of the spermidine uptake system and lethal effects of spermidine overaccumulation in ornithine decarboxylaseoverproducing L1210 cells under hyposmotic stress. J. Biol. Chem., 268, 4690-4698. (Pubitemid 23081580)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.7 , pp. 4690-4698
    • Poulin, R.1    Coward, J.K.2    Lakanen, J.R.3    Pegg, A.E.4
  • 4
    • 0028800002 scopus 로고
    • Exposure to ornithine results in excessive accumulation of putrescine and apoptotic cell death in ornithine decarboxylase overproducing mouse myeloma cells
    • Tobias, K.E. and Kahana, C. (1995) Exposure to ornithine results in excessive accumulation of putrescine and apoptotic cell death in ornithine decarboxylase overproducing mouse myeloma cells. Cell Growth Differ., 6, 1279-1285.
    • (1995) Cell Growth Differ. , vol.6 , pp. 1279-1285
    • Tobias, K.E.1    Kahana, C.2
  • 5
    • 34247876224 scopus 로고    scopus 로고
    • Ribosomal frameshifting in decoding antizyme mRNAs from yeast and protists to humans: Close to 300 cases reveal remarkable diversity despite underlying conservation
    • DOI 10.1093/nar/gkm035
    • Ivanov, I.P. and Atkins, J.F. (2007) Ribosomal frameshifting in decoding antizyme mRNAs from yeast and protists to humans: close to 300 cases reveal remarkable diversity despite underlying conservation. Nucleic Acids Res., 35, 1842-1858. (Pubitemid 47064260)
    • (2007) Nucleic Acids Research , vol.35 , Issue.6 , pp. 1842-1858
    • Ivanov, I.P.1    Atkins, J.F.2
  • 6
    • 11244337377 scopus 로고    scopus 로고
    • Polyamines regulate their synthesis by inducing expression and blocking degradation of ODC antizyme
    • DOI 10.1038/sj.emboj.7600473
    • Palanimurugan, R., Scheel, H., Hofmann, K. and Dohmen, R.J. (2004) Polyamines regulate their synthesis by inducing expression and blocking degradation of ODC antizyme. EMBO J., 23, 4857-4867. (Pubitemid 40069715)
    • (2004) EMBO Journal , vol.23 , Issue.24 , pp. 4857-4867
    • Palanimurugan, R.1    Scheel, H.2    Hofmann, K.3    Dohmen, R.J.4
  • 7
    • 0026667106 scopus 로고
    • Regulated degradation of ornithine decarboxylase requires interaction with the polyamine-inducible protein antizyme
    • Li, X. and Coffino, P. (1992) Regulated degradation of ornithine decarboxylase requires interaction with the polyamine-inducible protein antizyme. Mol. Cell. Biol., 12, 3556-3562.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3556-3562
    • Li, X.1    Coffino, P.2
  • 8
    • 0026714435 scopus 로고
    • Ornithine decarboxylase is degraded by the 26S proteasome without ubiquitination
    • DOI 10.1038/360597a0
    • Murakami, Y., Matsufuji, S., Kameji, T., Hayashi, S., Igarashi, K., Tamura, T., Tanaka, K. and Ichihara, A. (1992) Ornithine decarboxylase is degraded by the 26S proteasome without ubiquitination. Nature, 360, 597-599. (Pubitemid 23000711)
    • (1992) Nature , vol.360 , Issue.6404 , pp. 597-599
    • Murakami, Y.1    Matsufuji, S.2    Kameji, T.3    Hayashi, S.4    Igarashi, K.5    Tamura, T.6    Tanaka, K.7    Ichihara, A.8
  • 11
    • 0028073194 scopus 로고
    • Special peptidyl-tRNA molecules can promote translational frameshifting without slippage
    • Vimaladithan, A. and Farabaugh, P.J. (1994) Special peptidyl-tRNA molecules can promote translational frameshifting without slippage. Mol. Cell. Biol., 14, 8107-8116. (Pubitemid 24373559)
    • (1994) Molecular and Cellular Biology , vol.14 , Issue.12 , pp. 8107-8116
    • Vimaladithan, A.1    Farabaugh, P.J.2
  • 12
    • 0033380022 scopus 로고    scopus 로고
    • Near-cognate peptidyl-tRNAs promote +1 programmed translational frameshifting in yeast
    • Sundararajan, A., Michaud, W.A., Qian, Q., Stahl, G. and Farabaugh, P.J. (1999) Near-cognate peptidyl-tRNAs promote+1 programmed translational frameshifting in yeast. Mol. Cell, 4, 1005-1015. (Pubitemid 30054906)
    • (1999) Molecular Cell , vol.4 , Issue.6 , pp. 1005-1015
    • Sundararajan, A.1    Michaud, W.A.2    Qian, Q.3    Stahl, G.4    Farabaugh, P.J.5
  • 14
    • 0029153552 scopus 로고
    • The efficiency of translation termination is determined by a synergistic interplay between upstream and downstream sequences in Saccharomyces cerevisiae
    • Bonetti, B., Fu, L., Moon, J. and Bedwell, D.M. (1995) The efficiency of translation termination is determined by a synergistic interplay between upstream and downstream sequences in Saccharomyces cerevisiae. J. Mol. Biol., 251, 334-345.
    • (1995) J. Mol. Biol. , vol.251 , pp. 334-345
    • Bonetti, B.1    Fu, L.2    Moon, J.3    Bedwell, D.M.4
  • 15
    • 0020651239 scopus 로고
    • Polyamines enhance readthrough of the UGA termination codon in a mammalian messenger RNA
    • Hryniewicz, M.M. and Vonder Haar, R.A. (1983) Polyamines enhance readthrough of the UGA termination codon in a mammalian messenger RNA. Mol. Gen. Genet., 190, 336-343.
    • (1983) Mol. Gen. Genet. , vol.190 , pp. 336-343
    • Hryniewicz, M.M.1    Vonder Haar, R.A.2
  • 16
    • 0037020166 scopus 로고    scopus 로고
    • Polyamines enhance synthesis of the RNA polymerase sigma 38 subunit by suppression of an amber termination codon in the open reading frame
    • Yoshida, M., Kashiwagi, K., Kawai, G., Ishihama, A. and Igarashi, K. (2002) Polyamines enhance synthesis of the RNA polymerase sigma 38 subunit by suppression of an amber termination codon in the open reading frame. J. Biol. Chem., 277, 37139-37146.
    • (2002) J. Biol. Chem. , vol.277 , pp. 37139-37146
    • Yoshida, M.1    Kashiwagi, K.2    Kawai, G.3    Ishihama, A.4    Igarashi, K.5
  • 18
    • 0032873415 scopus 로고    scopus 로고
    • Three new dominant drug resistance cassettes for gene disruption in Saccharomyces cerevisiae
    • DOI 10.1002/(SICI)1097-0061(199910)15:14<1541::AID-YEA476>3.0.CO;2- K
    • Goldstein, A.L. and McCusker, J.H. (1999) Three new dominant drug resistance cassettes for gene disruption in Saccharomyces cerevisiae. Yeast, 15, 1541-1553. (Pubitemid 29472165)
    • (1999) Yeast , vol.15 , Issue.14 , pp. 1541-1553
    • Goldstein, A.L.1    McCusker, J.H.2
  • 19
    • 0025978949 scopus 로고
    • Getting started with yeast
    • Sherman, F. (1991) Getting started with yeast. Methods Enzymol., 194, 3-21.
    • (1991) Methods Enzymol. , vol.194 , pp. 3-21
    • Sherman, F.1
  • 20
    • 0035876480 scopus 로고    scopus 로고
    • Improvement of the analysis of dansylated derivatives of polyamines and their conjugates by high-performance liquid chromatography
    • DOI 10.1016/S0021-9673(01)00841-X, PII S002196730100841X
    • Fontaniella, B., Mateos, J.L., Vicente, C. and Legaz, M.E. (2001) Improvement of the analysis of dansylated derivatives of polyamines and their conjugates by high-performance liquid chromatography. J. Chromatogr. A, 919, 283-288. (Pubitemid 32568188)
    • (2001) Journal of Chromatography A , vol.919 , Issue.2 , pp. 283-288
    • Fontaniella, B.1    Mateos, J.L.2    Vicente, C.3    Legaz, M.-E.4
  • 23
    • 0029070954 scopus 로고
    • Versatile vectors to study recoding: Conservation of rules between yeast and mammalian cells
    • Stahl, G., Bidou, L., Rousset, J.P. and Cassan, M. (1995) Versatile vectors to study recoding: conservation of rules between yeast and mammalian cells. Nucleic Acids Res., 23, 1557-1560.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 1557-1560
    • Stahl, G.1    Bidou, L.2    Rousset, J.P.3    Cassan, M.4
  • 25
    • 0036270543 scopus 로고    scopus 로고
    • Transformation of yeast by lithium acetate/single-stranded carrier DNA/polyethylene glycol method
    • DOI 10.1016/S0076-6879(02)50957-5
    • Gietz, R.D. and Woods, R.A. (2002) Transformation of yeast by lithium acetate/single-stranded carrier DNA/polyethylene glycol method. Methods Enzymol., 350, 87-96. (Pubitemid 34619485)
    • (2002) Methods in Enzymology , vol.350 , pp. 87-96
    • Gietz, R.D.1    Woods, R.A.2
  • 26
    • 13544262685 scopus 로고    scopus 로고
    • Genome-wide prediction of stop codon readthrough during translation in the yeast Saccharomyces cerevisiae
    • DOI 10.1093/nar/gkh1004
    • Williams, I., Richardson, J., Starkey, A. and Stansfield, I. (2004) Genome-wide prediction of stop codon readthrough during translation in the yeast Saccharomyces cerevisiae. Nucleic Acids Res., 32, 6605-6616. (Pubitemid 40220372)
    • (2004) Nucleic Acids Research , vol.32 , Issue.22 , pp. 6605-6616
    • Williams, I.1    Richardson, J.2    Starkey, A.3    Stansfield, I.4
  • 27
    • 0019119792 scopus 로고
    • Regulatory mutations affecting ornithine decarboxylase activity in Saccharomyces cerevisiae
    • Cohn, M.S., Tabor, C.W. and Tabor, H. (1980) Regulatory mutations affecting ornithine decarboxylase activity in Saccharomyces cerevisiae. J. Bacteriol., 142, 791-799. (Pubitemid 11230329)
    • (1980) Journal of Bacteriology , vol.142 , Issue.3 , pp. 791-799
    • Cohn, M.S.1    Tabor, C.W.2    Tabor, H.3
  • 28
    • 0018096894 scopus 로고
    • Polyamine auxotrophs of Saccharomyces cerevisiae
    • Whitney, P.A. and Morris, D.R. (1978) Polyamine auxotrophs of Saccharomyces cerevisiae. J. Bacteriol., 134, 214-220. (Pubitemid 8334706)
    • (1978) Journal of Bacteriology , vol.134 , Issue.1 , pp. 214-220
    • Whitney, P.A.1    Morris, D.R.2
  • 29
    • 0017847685 scopus 로고
    • Isolation and characterization of Saccharomyces cerevisiae mutants deficient in S-adenosylmethionine decarboxylase, spermidine, and spermine
    • Cohn, M.S., Tabor, C.W. and Tabor, H. (1978) Isolation and characterization of Saccharomyces cerevisiae mutants deficient in S-adenosylmethionine decarboxylase, spermidine, and spermine. J. Bacteriol., 134, 208-213. (Pubitemid 8334705)
    • (1978) Journal of Bacteriology , vol.134 , Issue.1 , pp. 208-213
    • Cohn, M.S.1    Tabor, C.W.2    Tabor, H.3
  • 30
    • 0022001625 scopus 로고
    • Polyamines in microorganisms
    • Tabor, C.W. and Tabor, H. (1985) Polyamines in microorganisms. Microbiol. Rev., 49, 81-99. (Pubitemid 15134122)
    • (1985) Microbiological Reviews , vol.49 , Issue.1 , pp. 81-99
    • Tabor, C.W.1    Tabor, H.2
  • 31
    • 0029658939 scopus 로고    scopus 로고
    • Characterization of the Caccharomyces cerevisiae FMS1 gene related to Candida albicans corticosteroid-binding protein 1
    • DOI 10.1007/s002940050109
    • Joets, J., Pousset, D., Marcireau, C. and Karst, F. (1996) Characterization of the Saccharomyces cerevisiae FMS1 gene related to Candida albicans corticosteroid-binding protein 1. Curr. Genet., 30, 115-120. (Pubitemid 26261675)
    • (1996) Current Genetics , vol.30 , Issue.2 , pp. 115-120
    • Joets, J.1    Pousset, D.2    Marcireau, C.3    Karst, F.4
  • 32
    • 0035815728 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Is Capable of de Novo Pantothenic Acid Biosynthesis Involving a Novel Pathway of β-Alanine Production from Spermine
    • DOI 10.1074/jbc.M009804200
    • White, W.H., Gunyuzlu, P.L. and Toyn, J.H. (2001) Saccharomyces cerevisiae is capable of de novo pantothenic acid biosynthesis involving a novel pathway of beta-alanine production from spermine. J. Biol. Chem., 276, 10794-10800. (Pubitemid 38089254)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.14 , pp. 10794-10800
    • White, W.H.1    Gunyuzlu, P.L.2    Toyn, J.H.3
  • 33
    • 0345133303 scopus 로고    scopus 로고
    • Spermidine but not spermine is essential for hypusine biosynthesis and growth in Saccharomyces cerevisiae: Spermine is converted to spermidine in vivo by the FMS1-amine oxidase
    • DOI 10.1073/pnas.1835918100
    • Chattopadhyay, M.K., Tabor, C.W. and Tabor, H. (2003) Spermidine but not spermine is essential for hypusine biosynthesis and growth in Saccharomyces cerevisiae: spermine is converted to spermidine in vivo by the FMS1-amine oxidase. Proc. Natl Acad. Sci. USA, 100, 13869-13874. (Pubitemid 37499158)
    • (2003) Proceedings of the National Academy of Sciences of the United States of America , vol.100 , Issue.SUPPL. 2 , pp. 13869-13874
    • Chattopadhyay, M.K.1    Tabor, C.W.2    Tabor, H.3
  • 34
    • 20444451644 scopus 로고    scopus 로고
    • A yeast polyamine acetyltransferase
    • DOI 10.1074/jbc.M414008200
    • Liu, B., Sutton, A. and Sternglanz, R. (2005) A yeast polyamine acetyltransferase. J. Biol. Chem., 280, 16659-16664. (Pubitemid 41389123)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.17 , pp. 16659-16664
    • Liu, B.1    Sutton, A.2    Sternglanz, R.3
  • 35
    • 0027997081 scopus 로고
    • SPE1 and SPE2: Two essential genes in the biosynthesis of polyamines that modulate +1 ribosomal frameshifting in Saccharomyces cerevisiae
    • Balasundaram, D., Dinman, J.D., Tabor, C.W. and Tabor, H. (1994) SPE1 and SPE2: Two essential genes in the biosynthesis of polyamines that modulate+1 ribosomal frameshifting in Saccharomyces cerevisiae. J. Bacteriol., 176, 7126-7128. (Pubitemid 24349463)
    • (1994) Journal of Bacteriology , vol.176 , Issue.22 , pp. 7126-7128
    • Balasundaram, D.1    Dinman, J.D.2    Tabor, C.W.3    Tabor, H.4
  • 37
    • 0036640347 scopus 로고    scopus 로고
    • The identification of spermine binding sites in 16S rRNA allows interpretation of the spermine effect on ribosomal 30S subunit functions
    • Amarantos, I., Zarkadis, I.K. and Kalpaxis, D.L. (2002) The identification of spermine binding sites in 16S rRNA allows interpretation of the spermine effect on ribosomal 30S subunit functions. Nucleic Acids Res., 30, 2832-2843. (Pubitemid 34778143)
    • (2002) Nucleic Acids Research , vol.30 , Issue.13 , pp. 2832-2843
    • Amarantos, I.1    Zarkadis, I.K.2    Kalpaxis, D.L.3
  • 38
    • 19144368005 scopus 로고    scopus 로고
    • Localization of spermine binding sites in 23S rRNA by photoaffinity labeling: Parsing the spermine contribution to ribosomal 50S subunit functions
    • DOI 10.1093/nar/gki557
    • Xaplanteri, M.A., Petropoulos, A.D., Dinos, G.P. and Kalpaxis, D.L. (2005) Localization of spermine binding sites in 23S rRNA by photoaffinity labeling: parsing the spermine contribution to ribosomal 50S subunit functions. Nucleic Acids Res., 33, 2792-2805. (Pubitemid 41511219)
    • (2005) Nucleic Acids Research , vol.33 , Issue.9 , pp. 2792-2805
    • Xaplanteri, M.A.1    Petropoulos, A.D.2    Dinos, G.P.3    Kalpaxis, D.L.4
  • 39
    • 0034307464 scopus 로고    scopus 로고
    • Photoaffinity polyamines: Interactions with AcPhe-tRNA free in solution or bound at the P-site of Escherichia coli ribosomes
    • Amarantos, I. and Kalpaxis, D.L. (2000) Photoaffinity polyamines: Interactions with AcPhe-tRNA free in solution or bound at the P-site of Escherichia coli ribosomes. Nucleic Acids Res., 28, 3733-3742.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 3733-3742
    • Amarantos, I.1    Kalpaxis, D.L.2
  • 40
    • 0035179156 scopus 로고    scopus 로고
    • Cell culture analysis of the regulatory frameshift event required for the expression of mammalian antizymes
    • DOI 10.1046/j.1365-2443.2001.00477.x
    • Howard, M.T., Shirts, B.H., Zhou, J., Carlson, C.L., Matsufuji, S., Gesteland, R.F., Weeks, R.S. and Atkins, J.F. (2001) Cell culture analysis of the regulatory frameshift event required for the expression of mammalian antizymes. Genes Cells, 6, 931-941. (Pubitemid 33100028)
    • (2001) Genes to Cells , vol.6 , Issue.11 , pp. 931-941
    • Howard, M.T.1    Shirts, B.H.2    Zhou, J.3    Carlson, C.L.4    Matsufuji, S.5    Gesteland, R.F.6    Weeks, R.S.7    Atkins, J.F.8
  • 42
    • 0028230446 scopus 로고
    • A segment of mRNA encoding the leader peptide of the CPA1 gene confers repression by arginine on a heterologous yeast gene transcript
    • Delbecq, P., Werner, M., Feller, A., Filipkowski, R.K., Messenguy, F. and Pierard, A. (1994) A segment of mRNA encoding the leader peptide of the CPA1 gene confers repression by arginine on a heterologous yeast gene transcript. Mol. Cell. Biol., 14, 2378-2390. (Pubitemid 24108220)
    • (1994) Molecular and Cellular Biology , vol.14 , Issue.4 , pp. 2378-2390
    • Delbecq, P.1    Werner, M.2    Feller, A.3    Filipkowski, R.K.4    Messenguy, F.5    Pierard, A.6


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