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Volumn 12, Issue 4, 2007, Pages 435-445

The HAL3-PPZ1 dependent regulation of nonsense suppression efficiency in yeast and its influence on manifestation of the yeast prion-like determinant [ISP+]

Author keywords

[No Author keywords available]

Indexed keywords

ELONGATION FACTOR; FUNGAL PROTEIN; PHOSPHOPROTEIN PHOSPHATASE; PRION PROTEIN; PROTEIN HAL3; PROTEIN PPZ1; UNCLASSIFIED DRUG;

EID: 33947630362     PISSN: 13569597     EISSN: 13652443     Source Type: Journal    
DOI: 10.1111/j.1365-2443.2007.01064.x     Document Type: Article
Times cited : (12)

References (34)
  • 2
    • 0033638335 scopus 로고    scopus 로고
    • Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A: EEF1Bα
    • Andersen, G.R., Pedersen, L., Valente, L., Chatterjee, I., Kinzy, T.G., Kjeldgaard, M. & Nyborg, J. (2000) Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A: EEF1Bα. Mol. Cell. 6, 1261-1266.
    • (2000) Mol. Cell. , vol.6 , pp. 1261-1266
    • Andersen, G.R.1    Pedersen, L.2    Valente, L.3    Chatterjee, I.4    Kinzy, T.G.5    Kjeldgaard, M.6    Nyborg, J.7
  • 3
    • 0036183665 scopus 로고    scopus 로고
    • Novel protein phosphatases in yeast
    • Arino, J. (2002) Novel protein phosphatases in yeast. Eur. J. Biochem. 269, 1072-1077.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 1072-1077
    • Arino, J.1
  • 4
    • 0033569767 scopus 로고    scopus 로고
    • Mutations in a GTP-binding motif of eukaryotic elongation factor 1A reduce both translational fidelity and the requirement for nucleotide exchange
    • Carr-Schmid, A., Durko, N., Cavallius, J., Merrick, W.C. & Kinzy, T.G. (1999a) Mutations in a GTP-binding motif of eukaryotic elongation factor 1A reduce both translational fidelity and the requirement for nucleotide exchange. J. Biol. Chem. 274, 30297-30302.
    • (1999) J. Biol. Chem. , vol.274 , pp. 30297-30302
    • Carr-Schmid, A.1    Durko, N.2    Cavallius, J.3    Merrick, W.C.4    Kinzy, T.G.5
  • 5
    • 0032788546 scopus 로고    scopus 로고
    • Mutations in elongation factor 1β, a guanine nucleotide exchange factor, enhance translational fidelity
    • Carr-Schmid, A., Valente, L., Loik, V.I., Williams, T., Starita, L.M. & Kinzy, T.G. (1999b) Mutations in elongation factor 1β, a guanine nucleotide exchange factor, enhance translational fidelity. Mol. Cell. Biol. 19, 5257-5266.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5257-5266
    • Carr-Schmid, A.1    Valente, L.2    Loik, V.I.3    Williams, T.4    Starita, L.M.5    Kinzy, T.G.6
  • 7
    • 0033019059 scopus 로고    scopus 로고
    • The yeast ser/thr phosphatases Sit4 and Ppzl play opposite roles in regulation of the cell cycle
    • Clotet, J., Gari, E., Aldea, M. & Arino, J. (1999) The yeast ser/thr phosphatases Sit4 and Ppzl play opposite roles in regulation of the cell cycle. Mol. Cell. Biol. 19, 2408-2415.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 2408-2415
    • Clotet, J.1    Gari, E.2    Aldea, M.3    Arino, J.4
  • 8
    • 0029662221 scopus 로고    scopus 로고
    • The NH2-terminal extension of protein phosphatase PPZ1 has an essential functional role
    • Clotet, J., Posas, F., de Nadal, E. & Arino, J. (1996) The NH2-terminal extension of protein phosphatase PPZ1 has an essential functional role. J. Biol. Chem. 271, 26349-26355.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26349-26355
    • Clotet, J.1    Posas, F.2    de Nadal, E.3    Arino, J.4
  • 9
    • 0029026749 scopus 로고
    • Ribosome mutants with altered accuracy translate with reduced processivity
    • Dong, H. & Kurland, C.G. (1995) Ribosome mutants with altered accuracy translate with reduced processivity. J. Mol. Biol. 248, 551-561.
    • (1995) J. Mol. Biol. , vol.248 , pp. 551-561
    • Dong, H.1    Kurland, C.G.2
  • 10
    • 0029166109 scopus 로고
    • Regulation of cation transport in Saccharomyces cerevisiae by the salt tolerance gene HAL3
    • Ferrando, A., Kron, S.J., Rios, G., Fink, G.R. & Serrano, R. (1995) Regulation of cation transport in Saccharomyces cerevisiae by the salt tolerance gene HAL3. Mol. Cell. Biol. 15, 5470-5481.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5470-5481
    • Ferrando, A.1    Kron, S.J.2    Rios, G.3    Fink, G.R.4    Serrano, R.5
  • 11
    • 0024266139 scopus 로고
    • New yeast- Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites
    • Gietz, R.D. & Sugino, A. (1988) New yeast- Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites. Gene 74, 527-534.
    • (1988) Gene , vol.74 , pp. 527-534
    • Gietz, R.D.1    Sugino, A.2
  • 12
    • 0032873415 scopus 로고    scopus 로고
    • Three new dominant drug resistance cassettes for gene disruption in Saccharomyces cerevisiae
    • Goldstein, A.L. & McCusker, J.H. (1999) Three new dominant drug resistance cassettes for gene disruption in Saccharomyces cerevisiae. Yeast 15, 1541-1553.
    • (1999) Yeast , vol.15 , pp. 1541-1553
    • Goldstein, A.L.1    McCusker, J.H.2
  • 13
    • 0038576863 scopus 로고    scopus 로고
    • A method to assess compositional bias in biological sequences and its application to prion-like glutamine/asparagine-rich domains in eukaryotic proteomes
    • Harrison, P.M. & Gerstein, M. (2003) A method to assess compositional bias in biological sequences and its application to prion-like glutamine/asparagine-rich domains in eukaryotic proteomes. Genome Biol. 4, R40.
    • (2003) Genome Biol. , vol.4
    • Harrison, P.M.1    Gerstein, M.2
  • 14
    • 0027390846 scopus 로고
    • Cloning and characterization of the elongation factor EF-1β homologue of Saccharomyces cerevisiae. EF-1β is essential for growth
    • Hiraga, K., Suzuki, K., Tsuchiya, E. & Miyakawa, T. (1993) Cloning and characterization of the elongation factor EF-1β homologue of Saccharomyces cerevisiae. EF-1β is essential for growth. FEBS Lett. 316, 165-169.
    • (1993) FEBS Lett. , vol.316 , pp. 165-169
    • Hiraga, K.1    Suzuki, K.2    Tsuchiya, E.3    Miyakawa, T.4
  • 17
    • 0028217902 scopus 로고
    • Multiple genes encode the translation elongation factor EF-1γ in Saccharomyces cerevisiae
    • Kinzy, T.G., Ripmaster, T.L. & Woolford, J.L. Jr (1994) Multiple genes encode the translation elongation factor EF-1γ in Saccharomyces cerevisiae. Nucleic Acids Res. 22, 2703-2707.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 2703-2707
    • Kinzy, T.G.1    Ripmaster, T.L.2    Woolford, J.L.3
  • 18
    • 0037439231 scopus 로고    scopus 로고
    • Termination of translation: Interplay of mRNA, rRNAs and release factors?
    • Kisselev, L., Ehrenberg, M. & Frolova, L. (2003) Termination of translation: Interplay of mRNA, rRNAs and release factors? EMBO J. 22, 175-182.
    • (2003) EMBO J. , vol.22 , pp. 175-182
    • Kisselev, L.1    Ehrenberg, M.2    Frolova, L.3
  • 19
    • 0027219432 scopus 로고
    • A pair of functionally redundant yeast genes (PPZ1 and PPZ2) encoding type 1-related protein phosphatases function within the PKC1-mediated pathway
    • Lee, K.S., Hines, L.K. & Levin, D.E. (1993) A pair of functionally redundant yeast genes (PPZ1 and PPZ2) encoding type 1-related protein phosphatases function within the PKC1-mediated pathway. Mol. Cell. Biol. 13, 5843-5853.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 5843-5853
    • Lee, K.S.1    Hines, L.K.2    Levin, D.E.3
  • 21
    • 0034710897 scopus 로고    scopus 로고
    • A census of glutamine/asparagine-rich regions: Implications for their conserved function and the prediction of novel prions
    • Michelitsch, M.D. & Weissman, J.S. (2000) A census of glutamine/ asparagine-rich regions: Implications for their conserved function and the prediction of novel prions. Proc. Natl. Acad. Sci. USA 97, 11910-11915.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 11910-11915
    • Michelitsch, M.D.1    Weissman, J.S.2
  • 22
    • 5644250569 scopus 로고    scopus 로고
    • Functional characterization of the yeast Ppz1 phosphatase inhibitory subunit Hal3: A mutagenesis study
    • Munoz, I., Ruiz, A., Marquina, M., Barcelo, A., Albert, A. & Arino, J. (2004) Functional characterization of the yeast Ppz1 phosphatase inhibitory subunit Hal3: A mutagenesis study. J. Biol. Chem. 279, 42619-42627.
    • (2004) J. Biol. Chem. , vol.279 , pp. 42619-42627
    • Munoz, I.1    Ruiz, A.2    Marquina, M.3    Barcelo, A.4    Albert, A.5    Arino, J.6
  • 23
    • 0032560472 scopus 로고    scopus 로고
    • The yeast halotolerance determinant Hal3p is an inhibitory subunit of the Ppz1p Ser/Thr protein phosphatase
    • de Nadal, E., Clotet, J., Posas, F., Serrano, R., Gomez, N. & Arino, J. (1998) The yeast halotolerance determinant Hal3p is an inhibitory subunit of the Ppz1p Ser/Thr protein phosphatase. Proc. Natl. Acad. Sci. USA 95, 7357-7362.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7357-7362
    • de Nadal, E.1    Clotet, J.2    Posas, F.3    Serrano, R.4    Gomez, N.5    Arino, J.6
  • 24
    • 0035805492 scopus 로고    scopus 로고
    • A role for the PpZ Ser/Thr protein phosphatases in the regulation of translation elongation factor 1Bα
    • de Nadal, E., Fadden, R.P., Ruiz, A., Haystead, T. & Arino, J. (2001) A role for the PpZ Ser/Thr protein phosphatases in the regulation of translation elongation factor 1Bα. J. Biol. Chem. 276, 14829-14834.
    • (2001) J. Biol. Chem. , vol.276 , pp. 14829-14834
    • de Nadal, E.1    Fadden, R.P.2    Ruiz, A.3    Haystead, T.4    Arino, J.5
  • 25
    • 0029019792 scopus 로고
    • The PPZ protein phosphatases are important determinants of salt tolerance in yeast cells
    • Posas, F., Camps, M. & Arino, J. (1995) The PPZ protein phosphatases are important determinants of salt tolerance in yeast cells. J. Biol. Chem. 270, 13036-13041.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13036-13041
    • Posas, F.1    Camps, M.2    Arino, J.3
  • 26
    • 0027339732 scopus 로고
    • The PPZ protein phosphatases are involved in the maintenance of osmotic stability of yeast cells
    • Posas, F., Casamayor, A. & Arino, J. (1993) The PPZ protein phosphatases are involved in the maintenance of osmotic stability of yeast cells. FEBS Lett. 318, 282-286.
    • (1993) FEBS Lett. , vol.318 , pp. 282-286
    • Posas, F.1    Casamayor, A.2    Arino, J.3
  • 27
    • 0026753631 scopus 로고
    • Molecular cloning and analysis of a yeast protein phosphatase with an unusual amino-terminal region
    • Posas, F., Casamayor, A., Morral, N. & Arino, J. (1992) Molecular cloning and analysis of a yeast protein phosphatase with an unusual amino-terminal region. J. Biol. Chem. 267, 11734-11740.
    • (1992) J. Biol. Chem. , vol.267 , pp. 11734-11740
    • Posas, F.1    Casamayor, A.2    Morral, N.3    Arino, J.4
  • 28
    • 0023545322 scopus 로고
    • A Saccharomyces cerevisiae genomic plasmid bank based on a centromere-containing shuttle vector
    • Rose, M.D., Novick, P., Thomas, J.H., Botstein, D. & Fink, G.R. (1987) A Saccharomyces cerevisiae genomic plasmid bank based on a centromere-containing shuttle vector. Gene 60, 237-243.
    • (1987) Gene , vol.60 , pp. 237-243
    • Rose, M.D.1    Novick, P.2    Thomas, J.H.3    Botstein, D.4    Fink, G.R.5
  • 29
  • 30
    • 0034903337 scopus 로고    scopus 로고
    • In vivo site-directed mutagenesis using oligonucleotides
    • Storici, F., Lewis, L.K. & Resnick, M.A. (2001) In vivo site-directed mutagenesis using oligonucleotides. Nat. Biotechnol. 19, 773-776.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 773-776
    • Storici, F.1    Lewis, L.K.2    Resnick, M.A.3
  • 31
    • 0242320516 scopus 로고    scopus 로고
    • Yeast as a sensor of factors affecting the accuracy of protein synthesis
    • Valente, L. & Kinzy, T.G. (2003) Yeast as a sensor of factors affecting the accuracy of protein synthesis. Cell. Mol. Life Sci. 60, 2115-2130.
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 2115-2130
    • Valente, L.1    Kinzy, T.G.2
  • 33
    • 0028676232 scopus 로고
    • New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae
    • Wach, A., Brachat, A., Pohlmann, R. & Philippsen, P. (1994) New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae. Yeast 10, 1793-1808.
    • (1994) Yeast , vol.10 , pp. 1793-1808
    • Wach, A.1    Brachat, A.2    Pohlmann, R.3    Philippsen, P.4
  • 34
    • 0036500159 scopus 로고    scopus 로고
    • The PpZ protein phosphatases are key regulators of K+ and pH homeostasis: Implications for salt tolerance, cell wall integrity and cell cycle progression
    • Yenush, L., Mulet, J.M., Arino, J. & Serrano, R. (2002) The PpZ protein phosphatases are key regulators of K+ and pH homeostasis: implications for salt tolerance, cell wall integrity and cell cycle progression. EMBO J. 21, 920-929.
    • (2002) EMBO J. , vol.21 , pp. 920-929
    • Yenush, L.1    Mulet, J.M.2    Arino, J.3    Serrano, R.4


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