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Volumn 17, Issue 12, 1997, Pages 7283-7294

Fal1p is an essential DEAD-box protein involved in 40S-ribosomal- subunit biogenesis in Saccharomyces cerevisiae

Author keywords

[No Author keywords available]

Indexed keywords

DEAD BOX PROTEIN; NEOMYCIN; PAROMOMYCIN; RIBOSOME RNA; RNA 18S; RNA HELICASE; RNA HELICASE FAL 1 P; UNCLASSIFIED DRUG;

EID: 0030679565     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.17.12.7283     Document Type: Article
Times cited : (149)

References (85)
  • 1
    • 0029919935 scopus 로고    scopus 로고
    • RNase III cleaves eukaryotic preribosomal RNA at a U3 snoRNP-dependent site
    • Abou Elela, S., H. Igel, and M. Ares, Jr. 1996. RNase III cleaves eukaryotic preribosomal RNA at a U3 snoRNP-dependent site. Cell 85:115-124.
    • (1996) Cell , vol.85 , pp. 115-124
    • Abou Elela, S.1    Igel, H.2    Ares Jr., M.3
  • 2
    • 0022407035 scopus 로고
    • Effect of RP51 gene dosage alterations on ribosome synthesis in Saccharomyces cerevisiae
    • Abovich, N., L. Gritz, L. Tung, and M. Rosbash. 1985. Effect of RP51 gene dosage alterations on ribosome synthesis in Saccharomyces cerevisiae. Mol. Cell. Biol. 5:3429-3435.
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 3429-3435
    • Abovich, N.1    Gritz, L.2    Tung, L.3    Rosbash, M.4
  • 3
    • 0028240897 scopus 로고
    • A new generation of information retrieval tools for biologists: The example of the ExPASy WWW server
    • Appel, R. D., A. Bairoch, and D. F. Hochstrasser. 1994. A new generation of information retrieval tools for biologists: the example of the ExPASy WWW server. Trends Biochem. Sci. 19:258-260.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 258-260
    • Appel, R.D.1    Bairoch, A.2    Hochstrasser, D.F.3
  • 5
    • 0027186303 scopus 로고
    • Yeast prt1 mutations alter heat-shock gene expression through transcript fragmentation
    • Barnes, C. A., R. A. Singer, and G. C. Johnston. 1993. Yeast prt1 mutations alter heat-shock gene expression through transcript fragmentation. EMBO J. 12:3323-3332.
    • (1993) EMBO J. , vol.12 , pp. 3323-3332
    • Barnes, C.A.1    Singer, R.A.2    Johnston, G.C.3
  • 6
    • 77957219751 scopus 로고
    • Mutational analysis of an essential binding site for the U3 snoRNA in the 5′ external transcribed spacer of yeast pre-rRNA
    • Beltrame, M., Y. Henry, and D. Tollervey. 1994. Mutational analysis of an essential binding site for the U3 snoRNA in the 5′ external transcribed spacer of yeast pre-rRNA. Nucleic Acids Res. 22:5139-5147.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 5139-5147
    • Beltrame, M.1    Henry, Y.2    Tollervey, D.3
  • 7
    • 0029093602 scopus 로고
    • Base pairing between U3 and the pre-ribosomal RNA is required for 18S rRNA synthesis
    • Beltrame, M., and D. Tollervey. 1995. Base pairing between U3 and the pre-ribosomal RNA is required for 18S rRNA synthesis. EMBO J. 14:4350-4356.
    • (1995) EMBO J. , vol.14 , pp. 4350-4356
    • Beltrame, M.1    Tollervey, D.2
  • 8
    • 0023484186 scopus 로고
    • 5-Fluoroorotic acid as a selective agent in yeast molecular genetics
    • Boeke, J. D., J. Trueheart, G. Natsoulis, and G. R. Fink. 1987. 5-Fluoroorotic acid as a selective agent in yeast molecular genetics. Methods Enzymol. 154:164-175.
    • (1987) Methods Enzymol. , vol.154 , pp. 164-175
    • Boeke, J.D.1    Trueheart, J.2    Natsoulis, G.3    Fink, G.R.4
  • 9
    • 0028058010 scopus 로고
    • Mutations in eukaryotic 18S ribosomal RNA affect translational fidelity and resistance to aminoglycoside antibiotics
    • Chernoff, Y. O., A. Vincent, and S. W. Liebman. 1994. Mutations in eukaryotic 18S ribosomal RNA affect translational fidelity and resistance to aminoglycoside antibiotics. EMBO J. 13:906-913.
    • (1994) EMBO J. , vol.13 , pp. 906-913
    • Chernoff, Y.O.1    Vincent, A.2    Liebman, S.W.3
  • 11
    • 0027246625 scopus 로고
    • A new yeast translation initiation factor suppresses a mutation in the eIF-4A RNA helicase
    • Coppolecchia, R., P. Buser, A. Stotz, and P. Linder. 1993. A new yeast translation initiation factor suppresses a mutation in the eIF-4A RNA helicase. EMBO J. 12:4005-4011.
    • (1993) EMBO J. , vol.12 , pp. 4005-4011
    • Coppolecchia, R.1    Buser, P.2    Stotz, A.3    Linder, P.4
  • 12
    • 0031000205 scopus 로고    scopus 로고
    • The p20 and Ded1 proteins have antagonistic roles in eIF4E-dependent translation in Saccharomyces cerevisiae
    • de la Cruz, J., I. Iost, D. Kressler, and P. Linder. 1997. The p20 and Ded1 proteins have antagonistic roles in eIF4E-dependent translation in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 94:5201-5206.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 5201-5206
    • De La Cruz, J.1    Iost, I.2    Kressler, D.3    Linder, P.4
  • 13
    • 0027211846 scopus 로고
    • Yeast ribosomal protein L1 is required for the stability of newly synthesized 5S rRNA and the assembly of 60S ribosomal subunits
    • Deshmukh, M., Y.-F. Tsay, A. G. Paulovich, and J. L. Woolford, Jr. 1993. Yeast ribosomal protein L1 is required for the stability of newly synthesized 5S rRNA and the assembly of 60S ribosomal subunits. Mol. Cell. Biol. 13:2835-2845.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 2835-2845
    • Deshmukh, M.1    Tsay, Y.-F.2    Paulovich, A.G.3    Woolford Jr., J.L.4
  • 14
    • 0024593537 scopus 로고
    • The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis
    • Finley, D., B. Bartel, and A. Varshavsky. 1989. The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis. Nature 338:394-401.
    • (1989) Nature , vol.338 , pp. 394-401
    • Finley, D.1    Bartel, B.2    Varshavsky, A.3
  • 15
    • 0025869164 scopus 로고
    • GCD2, a translational repressor of the GCN4 gene, has a general function in the initiation of protein synthesis in Saccharomyces cerevisiae
    • Foiani, M., A. M. Cigan, C. J. Paddon, S. Harashima, and A. G. Hinnebusch. 1991. GCD2, a translational repressor of the GCN4 gene, has a general function in the initiation of protein synthesis in Saccharomyces cerevisiae. Mol. Cell. Biol. 11:3203-3216.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 3203-3216
    • Foiani, M.1    Cigan, A.M.2    Paddon, C.J.3    Harashima, S.4    Hinnebusch, A.G.5
  • 16
    • 0028340061 scopus 로고
    • Reduced dosage of genes encoding ribosomal protein S18 suppresses a mitochondrial initiation codon mutation in Saccharomyces cerevisiae
    • Folley, L. S., and T. D. Fox. 1994. Reduced dosage of genes encoding ribosomal protein S18 suppresses a mitochondrial initiation codon mutation in Saccharomyces cerevisiae. Genetics 137:369-379.
    • (1994) Genetics , vol.137 , pp. 369-379
    • Folley, L.S.1    Fox, T.D.2
  • 17
    • 0020490603 scopus 로고
    • Molecular cloning and analysis of yeast gene for cycloheximide resistance and ribosomal protein L29
    • Fried, H. M., and J. R. Warner. 1982. Molecular cloning and analysis of yeast gene for cycloheximide resistance and ribosomal protein L29. Nucleic Acids Res. 10:3133-3147.
    • (1982) Nucleic Acids Res. , vol.10 , pp. 3133-3147
    • Fried, H.M.1    Warner, J.R.2
  • 18
    • 0028301073 scopus 로고
    • RNA helicases: Modulators of RNA structure
    • Fuller-Pace, F. V. 1994. RNA helicases: modulators of RNA structure. Trends Cell Biol. 4:271-274.
    • (1994) Trends Cell Biol. , vol.4 , pp. 271-274
    • Fuller-Pace, F.V.1
  • 19
    • 0027301893 scopus 로고
    • DbpA: A DEAD box protein specifically activated by 23S rRNA
    • Fuller-Pace, F. V., S. M. Nicol, A. D. Reid, and D. P. Lane. 1993. DbpA: a DEAD box protein specifically activated by 23S rRNA. EMBO J. 12:3619-3626.
    • (1993) EMBO J. , vol.12 , pp. 3619-3626
    • Fuller-Pace, F.V.1    Nicol, S.M.2    Reid, A.D.3    Lane, D.P.4
  • 20
    • 0026562884 scopus 로고
    • Improved method for high efficiency transformation of intact yeast cells
    • Gietz, D., A. St. Jean, R. A. Woods, and R. H. Schiestl. 1992. Improved method for high efficiency transformation of intact yeast cells. Nucleic Acids Res. 20:1425.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 1425
    • Gietz, D.1    St. Jean, A.2    Woods, R.A.3    Schiestl, R.H.4
  • 22
    • 0024344173 scopus 로고
    • Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes
    • Gorbalenya, A. E., E. V. Koonin, A. P. Donchenko, and V. M. Blinov. 1989. Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes. Nucleic Acids Res. 17:4713-4730.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 4713-4730
    • Gorbalenya, A.E.1    Koonin, E.V.2    Donchenko, A.P.3    Blinov, V.M.4
  • 24
    • 0024393487 scopus 로고
    • RNA helicase activity associated with the human p68 protein
    • Hirling, H., M. Scheffner, T. Restle, and H. Stahl. 1989. RNA helicase activity associated with the human p68 protein. Nature 339:562-564.
    • (1989) Nature , vol.339 , pp. 562-564
    • Hirling, H.1    Scheffner, M.2    Restle, T.3    Stahl, H.4
  • 25
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S. N., H. D. Hunt, R. M. Horton, J. K. Pullen, and L. R. Pease. 1989. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77:51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 26
    • 0025932166 scopus 로고
    • Depletion of U3 small nucleolar RNA inhibits cleavage in the 5′ external transcribed spacer of yeast preribosomal RNA and impairs formation of 18S ribosomal RNA
    • Hughes, J. M. X., and M. Ares, Jr. 1991. Depletion of U3 small nucleolar RNA inhibits cleavage in the 5′ external transcribed spacer of yeast preribosomal RNA and impairs formation of 18S ribosomal RNA. EMBO J. 10:4231-4239.
    • (1991) EMBO J. , vol.10 , pp. 4231-4239
    • Hughes, J.M.X.1    Ares Jr., M.2
  • 27
    • 0006895405 scopus 로고    scopus 로고
    • RNA turnover: The helicase story unwinds
    • Jacobs Anderson, J. S., and R. Parker. 1996. RNA turnover: the helicase story unwinds. Curr. Biol. 6:780-782.
    • (1996) Curr. Biol. , vol.6 , pp. 780-782
    • Jacobs Anderson, J.S.1    Parker, R.2
  • 28
    • 0027153326 scopus 로고
    • A U3 snoRNP protein with homology to splicing factor PRP4 and Gβ domains is required for ribosomal RNA processing
    • Jansen, R., D. Tollervey, and E. C. Hurt. 1993. A U3 snoRNP protein with homology to splicing factor PRP4 and Gβ domains is required for ribosomal RNA processing. EMBO J. 12:2549-2558.
    • (1993) EMBO J. , vol.12 , pp. 2549-2558
    • Jansen, R.1    Tollervey, D.2    Hurt, E.C.3
  • 31
    • 0026535919 scopus 로고
    • The purified yeast pre-mRNA splicing factor PRP2 is an RNA-dependent NTPase
    • Kim, S.-H., J. Smith, A. Claude, and R.-J. Lin. 1992. The purified yeast pre-mRNA splicing factor PRP2 is an RNA-dependent NTPase. EMBO J. 11:2319-2326.
    • (1992) EMBO J. , vol.11 , pp. 2319-2326
    • Kim, S.-H.1    Smith, J.2    Claude, A.3    Lin, R.-J.4
  • 32
    • 0024787601 scopus 로고
    • Isolation and characterization of yeast ribosomal RNA precursors and preribosomes
    • Klootwijk, J., and R. J. Planta. 1989. Isolation and characterization of yeast ribosomal RNA precursors and preribosomes. Methods Enzymol. 180:96-109.
    • (1989) Methods Enzymol. , vol.180 , pp. 96-109
    • Klootwijk, J.1    Planta, R.J.2
  • 33
    • 0025886782 scopus 로고
    • Similarities in RNA helicases
    • Koonin, E. V. 1991. Similarities in RNA helicases. Nature 352:290.
    • (1991) Nature , vol.352 , pp. 290
    • Koonin, E.V.1
  • 34
    • 0024546509 scopus 로고
    • The scanning model for translation: An update
    • Kozak, M. 1989. The scanning model for translation: an update. J. Cell Biol. 108:229-241.
    • (1989) J. Cell Biol. , vol.108 , pp. 229-241
    • Kozak, M.1
  • 35
    • 0028866774 scopus 로고
    • The 18S rRNA dimethylase Dim1p is required for pre-ribosomal RNA processing in yeast
    • Lafontaine, D., J. Vandenhaute, and D. Tollervey. 1995. The 18S rRNA dimethylase Dim1p is required for pre-ribosomal RNA processing in yeast. Genes Dev. 9:2470-2481.
    • (1995) Genes Dev. , vol.9 , pp. 2470-2481
    • Lafontaine, D.1    Vandenhaute, J.2    Tollervey, D.3
  • 36
    • 0026776083 scopus 로고
    • NSR1 is required for prerRNA processing and for the proper maintenance of steady-state levels of ribosomal subunits
    • Lee, W.-C., D. Zabetakis, and T. Mélèse. 1992. NSR1 is required for prerRNA processing and for the proper maintenance of steady-state levels of ribosomal subunits. Mol. Cell. Biol. 12:3865-3871.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3865-3871
    • Lee, W.-C.1    Zabetakis, D.2    Mélèse, T.3
  • 37
    • 0025166298 scopus 로고
    • Depletion of U14 small nuclear RNA (snR128) disrupts production of 18S rRNA in Saccharomyces cerevisiae
    • Li, H. V., J. Zagorski, and M. J. Fournier. 1990. Depletion of U14 small nuclear RNA (snR128) disrupts production of 18S rRNA in Saccharomyces cerevisiae. Mol. Cell. Biol. 10:1145-1152.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 1145-1152
    • Li, H.V.1    Zagorski, J.2    Fournier, M.J.3
  • 38
    • 0028222187 scopus 로고
    • Localization of vasa protein to the Drosophila pole plasm is independent of its RNA-binding and helicase activities
    • Liang, L., W. Diehl-Jones, and P. Lasko. 1994. Localization of vasa protein to the Drosophila pole plasm is independent of its RNA-binding and helicase activities Development 120:1201-1211.
    • (1994) Development , vol.120 , pp. 1201-1211
    • Liang, L.1    Diehl-Jones, W.2    Lasko, P.3
  • 39
    • 0030929129 scopus 로고    scopus 로고
    • The rRNA-processing function of the yeast U14 small nucleolar RNA can be rescued by a conserved RNA helicase-like protein
    • Liang, W.-Q., J. A. Clark, and M. J. Fournier. 1997. The rRNA-processing function of the yeast U14 small nucleolar RNA can be rescued by a conserved RNA helicase-like protein. Mol. Cell. Biol. 17:4124-4132.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4124-4132
    • Liang, W.-Q.1    Clark, J.A.2    Fournier, M.J.3
  • 40
    • 0028818298 scopus 로고
    • U14 base-pairs with 18S rRNA: A novel snoRNA interaction required for rRNA processing
    • Liang, W.-Q., and M. J. Fournier. 1995. U14 base-pairs with 18S rRNA: a novel snoRNA interaction required for rRNA processing. Genes Dev. 9: 2433-2443.
    • (1995) Genes Dev. , vol.9 , pp. 2433-2443
    • Liang, W.-Q.1    Fournier, M.J.2
  • 42
    • 1842398952 scopus 로고
    • An essential yeast protein, encoded by duplicated genes TIF1 and TIF2 and homologous to the mammalian translation initiation factor eIF-4A, can suppress a mitochondrial missense mutation
    • Linder, P., and P. P. Slonimski. 1989. An essential yeast protein, encoded by duplicated genes TIF1 and TIF2 and homologous to the mammalian translation initiation factor eIF-4A, can suppress a mitochondrial missense mutation. Proc. Natl. Acad. Sci. USA 86:2286-2290.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 2286-2290
    • Linder, P.1    Slonimski, P.P.2
  • 43
    • 0030034498 scopus 로고    scopus 로고
    • The DExH box protein Suv3p is a component of a yeast mitochondrial 3′-to-5′ exoribonuclease that suppresses group I intron toxicity
    • Margossian, S. P., H. Li, H. P. Zassenhaus, and R. A. Butow. 1996. The DExH box protein Suv3p is a component of a yeast mitochondrial 3′-to-5′ exoribonuclease that suppresses group I intron toxicity. Cell 84:199-209.
    • (1996) Cell , vol.84 , pp. 199-209
    • Margossian, S.P.1    Li, H.2    Zassenhaus, H.P.3    Butow, R.A.4
  • 44
    • 0029055194 scopus 로고
    • The nucleolus: An organelle formed by the act of building a ribosome
    • Mélèse, T., and Z. Xue. 1995. The nucleolus: an organelle formed by the act of building a ribosome. Curr. Opin. Cell Biol. 7:319-324.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 319-324
    • Mélèse, T.1    Xue, Z.2
  • 45
    • 0028331455 scopus 로고
    • The translation initiation factor eIF-4B contains an RNA-binding region that is distinct and independent from its ribonucleoprotein consensus sequence
    • Méthot, N., A. Pause, J. W. B. Hershey, and N. Sonenberg. 1994. The translation initiation factor eIF-4B contains an RNA-binding region that is distinct and independent from its ribonucleoprotein consensus sequence. Mol. Cell. Biol. 14:2307-2316.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2307-2316
    • Méthot, N.1    Pause, A.2    Hershey, J.W.B.3    Sonenberg, N.4
  • 46
    • 0026091767 scopus 로고
    • Assembly of 60S ribosomal subunits is perturbed in temperature-sensitive yeast mutants defective in ribosomal protein L16
    • Moritz, M., B. A. Pulaski, and J. L. Woolford, Jr. 1991. Assembly of 60S ribosomal subunits is perturbed in temperature-sensitive yeast mutants defective in ribosomal protein L16. Mol. Cell. Biol. 11:5681-5692.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 5681-5692
    • Moritz, M.1    Pulaski, B.A.2    Woolford Jr., J.L.3
  • 47
    • 0027447757 scopus 로고
    • Yeast snR30 is a small nucleolar RNA required for 18S rRNA synthesis
    • Morrissey, J. P., and D. Tollervey. 1993. Yeast snR30 is a small nucleolar RNA required for 18S rRNA synthesis. Mol. Cell. Biol. 13:2469-2477.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 2469-2477
    • Morrissey, J.P.1    Tollervey, D.2
  • 48
    • 0026501752 scopus 로고
    • A rapid method for localized mutagenesis of yeast genes
    • Muhlrad, D., R. Hunter, and R. Parker. 1992. A rapid method for localized mutagenesis of yeast genes. Yeast 8:79-82.
    • (1992) Yeast , vol.8 , pp. 79-82
    • Muhlrad, D.1    Hunter, R.2    Parker, R.3
  • 49
    • 0029736818 scopus 로고    scopus 로고
    • 18S rRNA processing requires the RNA helicase-like protein Rrp3
    • O'Day, C. L., F. Chavanikamannil, and J. Abelson. 1996. 18S rRNA processing requires the RNA helicase-like protein Rrp3. Nucleic Acids Res. 24:3201-3207.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 3201-3207
    • O'Day, C.L.1    Chavanikamannil, F.2    Abelson, J.3
  • 50
    • 0027494565 scopus 로고
    • The HRIGRXXR region of the DEAD box RNA helicase eukaryotic translation initiation factor 4A is required for RNA binding and ATP hydrolysis
    • Pause, A., N. Méthot, and N. Sonenberg. 1993. The HRIGRXXR region of the DEAD box RNA helicase eukaryotic translation initiation factor 4A is required for RNA binding and ATP hydrolysis. Mol. Cell. Biol. 13:6789-6798.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 6789-6798
    • Pause, A.1    Méthot, N.2    Sonenberg, N.3
  • 51
    • 0027137838 scopus 로고
    • Helicases and RNA unwinding in translation
    • Pause, A., and N. Sonenberg. 1993. Helicases and RNA unwinding in translation. Curr. Opin. Struct. Biol. 3:953-959.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 953-959
    • Pause, A.1    Sonenberg, N.2
  • 52
    • 0026680746 scopus 로고
    • Mutational analysis of a DEAD box RNA helicase: The mammalian translation initiation factor eIF-4A
    • Pause, A., and N. Sonenberg. 1992. Mutational analysis of a DEAD box RNA helicase: the mammalian translation initiation factor eIF-4A. EMBO J. 11:2643-2654.
    • (1992) EMBO J. , vol.11 , pp. 2643-2654
    • Pause, A.1    Sonenberg, N.2
  • 54
    • 0029922992 scopus 로고    scopus 로고
    • A DEAD-box RNA helicase in the Escherichia coli RNA degradosome
    • Py, B., C. F. Higgins, H. M. Krisch, and A. J. Carpousis. 1996. A DEAD-box RNA helicase in the Escherichia coli RNA degradosome. Nature 381:169-172.
    • (1996) Nature , vol.381 , pp. 169-172
    • Py, B.1    Higgins, C.F.2    Krisch, H.M.3    Carpousis, A.J.4
  • 55
    • 0026470789 scopus 로고
    • A putative ATP-dependent RNA helicase involved in Saccharomyces cerevisiae ribosome assembly
    • Ripmaster, T. L., G. P. Vaughn, and J. L. Woolford, Jr. 1992. A putative ATP-dependent RNA helicase involved in Saccharomyces cerevisiae ribosome assembly. Proc. Natl. Acad. Sci. USA 89:11131-11135.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11131-11135
    • Ripmaster, T.L.1    Vaughn, G.P.2    Woolford Jr., J.L.3
  • 56
    • 0020645054 scopus 로고
    • One-step gene disruption in yeast
    • Rothstein, R. J. 1983. One-step gene disruption in yeast. Methods Enzymol. 101:202-211.
    • (1983) Methods Enzymol. , vol.101 , pp. 202-211
    • Rothstein, R.J.1
  • 57
    • 0025176473 scopus 로고
    • Bidirectional RNA helicase activity of eucaryotic translation initiation factors 4A and 4F
    • Rozen, F., I. Edery, K. Meerovitch, T. E. Dever, W. C. Merrick, and N. Sonenberg. 1990. Bidirectional RNA helicase activity of eucaryotic translation initiation factors 4A and 4F. Mol. Cell. Biol. 10:1134-1144.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 1134-1144
    • Rozen, F.1    Edery, I.2    Meerovitch, K.3    Dever, T.E.4    Merrick, W.C.5    Sonenberg, N.6
  • 58
    • 0026478895 scopus 로고
    • NOP3 is an essential yeast protein which is required for pre-rRNA processing
    • Russell, I. D., and D. Tollervey. 1992. NOP3 is an essential yeast protein which is required for pre-rRNA processing. J. Cell Biol. 119:737-747.
    • (1992) J. Cell Biol. , vol.119 , pp. 737-747
    • Russell, I.D.1    Tollervey, D.2
  • 59
    • 0025271804 scopus 로고
    • Translation initiation and ribosomal biogenesis: Involvement of a putative rRNA helicase and RPL46
    • Sachs, A. B., and R. W. Davis. 1990. Translation initiation and ribosomal biogenesis: involvement of a putative rRNA helicase and RPL46. Science 247:1077-1079.
    • (1990) Science , vol.247 , pp. 1077-1079
    • Sachs, A.B.1    Davis, R.W.2
  • 61
    • 0026569419 scopus 로고
    • D-E-A-D protein family of putative RNA helicases
    • Schmid, S. R., and P. Linder. 1992. D-E-A-D protein family of putative RNA helicases. Mol. Microbiol. 6:283-292.
    • (1992) Mol. Microbiol. , vol.6 , pp. 283-292
    • Schmid, S.R.1    Linder, P.2
  • 62
    • 0025898593 scopus 로고
    • Translation initiation factor 4A from Saccharomyces cerevisiae: Analysis of residues conserved in the D-E-A-D family of RNA helicases
    • Schmid, S. R., and P. Linder. 1991. Translation initiation factor 4A from Saccharomyces cerevisiae: analysis of residues conserved in the D-E-A-D family of RNA helicases. Mol. Cell. Biol. 11:3463-3471.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 3463-3471
    • Schmid, S.R.1    Linder, P.2
  • 63
    • 0030906569 scopus 로고    scopus 로고
    • The yeast phosphatidylinositol kinase homolog TOR2 activates RHO1 and RHO2 via the exchange factor ROM2
    • Schmidt, A., M. Bickle, T. Beck, and M. N. Hall. 1997. The yeast phosphatidylinositol kinase homolog TOR2 activates RHO1 and RHO2 via the exchange factor ROM2. Cell 88:531-542.
    • (1997) Cell , vol.88 , pp. 531-542
    • Schmidt, A.1    Bickle, M.2    Beck, T.3    Hall, M.N.4
  • 64
    • 0026019713 scopus 로고
    • PRP16 is an RNA-dependent ATPase that interacts transiently with the spliceosome
    • Schwer, B., and C. Guthrie. 1991. PRP16 is an RNA-dependent ATPase that interacts transiently with the spliceosome. Nature 349:494-499.
    • (1991) Nature , vol.349 , pp. 494-499
    • Schwer, B.1    Guthrie, C.2
  • 65
    • 0023762645 scopus 로고
    • Codon usage patterns in Escherichia coli, Bacillus subtilis, Saccharomyces cerevisiae, Schizosaccharomyces pombe, Drosophila melano-gaster and Homo sapiens: A review of the considerable within-species diversity
    • Sharp, P. M., E. Cowe, D. G. Higgins, D. C. Shields, K. H. Wolfe, and F. Wright. 1988. Codon usage patterns in Escherichia coli, Bacillus subtilis, Saccharomyces cerevisiae, Schizosaccharomyces pombe, Drosophila melano-gaster and Homo sapiens: a review of the considerable within-species diversity. Nucleic Acids Res. 16:8207-8211.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 8207-8211
    • Sharp, P.M.1    Cowe, E.2    Higgins, D.G.3    Shields, D.C.4    Wolfe, K.H.5    Wright, F.6
  • 66
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R. S., and P. Hieter. 1989. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122:19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 67
    • 0024977417 scopus 로고
    • Elevated recombination rates in transcriptionally active DNA
    • Thomas, B. J., and R. Rothstein. 1989. Elevated recombination rates in transcriptionally active DNA. Cell 56:619-630.
    • (1989) Cell , vol.56 , pp. 619-630
    • Thomas, B.J.1    Rothstein, R.2
  • 68
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 69
    • 0030589668 scopus 로고    scopus 로고
    • Trans-acting factors in ribosome synthesis
    • Tollervey, D. 1996. trans-acting factors in ribosome synthesis. Exp. Cell Res. 229:226-232.
    • (1996) Exp. Cell Res. , vol.229 , pp. 226-232
    • Tollervey, D.1
  • 70
    • 0023661309 scopus 로고
    • A yeast small nuclear RNA is required for normal processing of pre-ribosomal RNA
    • Tollervey, D. 1987. A yeast small nuclear RNA is required for normal processing of pre-ribosomal RNA. EMBO J. 6:4169-4175.
    • (1987) EMBO J. , vol.6 , pp. 4169-4175
    • Tollervey, D.1
  • 71
    • 0025963863 scopus 로고
    • The small nucleolar RNP protein NOP1 (fibrillarin) is required for pre-rRNA processing in yeast
    • Tollervey, D., H. Lehtonen, M. Carmo-Fonseca, and E. C. Hurt. 1991. The small nucleolar RNP protein NOP1 (fibrillarin) is required for pre-rRNA processing in yeast. EMBO J. 10:573-583.
    • (1991) EMBO J. , vol.10 , pp. 573-583
    • Tollervey, D.1    Lehtonen, H.2    Carmo-Fonseca, M.3    Hurt, E.C.4
  • 72
    • 0015935199 scopus 로고
    • The cytoplasmic maturation of a ribosomal precursor ribonucleic acid in yeast
    • Udem, S. A., and J. R. Warner. 1973. The cytoplasmic maturation of a ribosomal precursor ribonucleic acid in yeast. J. Biol. Chem. 248:1412-1416.
    • (1973) J. Biol. Chem. , vol.248 , pp. 1412-1416
    • Udem, S.A.1    Warner, J.R.2
  • 74
    • 0029118645 scopus 로고
    • Two distinct recognition signals define the site of endonucleolytic cleavage at the 5′-end of yeast 18S rRNA
    • Venema, J., Y. Henry, and D. Tollervey. 1995. Two distinct recognition signals define the site of endonucleolytic cleavage at the 5′-end of yeast 18S rRNA. EMBO J. 14:4883-4892.
    • (1995) EMBO J. , vol.14 , pp. 4883-4892
    • Venema, J.1    Henry, Y.2    Tollervey, D.3
  • 75
    • 0344700502 scopus 로고    scopus 로고
    • In vivo mutational analysis of ribosomal RNA in Saccharomyces cerevisiae
    • R. Martin (ed.). in press. Humana Press, Totowa, N.J.
    • Venema, J., R. J. Planta, and H. A. Raué. In vivo mutational analysis of ribosomal RNA in Saccharomyces cerevisiae. In R. Martin (ed.). Protein synthesis: methods and protocols, in press. Humana Press, Totowa, N.J.
    • Protein Synthesis: Methods and Protocols
    • Venema, J.1    Planta, R.J.2    Raué, H.A.3
  • 76
    • 0029618257 scopus 로고
    • Processing of pre-ribosomal RNA in Saccharomyces cerevisiae
    • Venema, J., and D. Tollervey. 1995. Processing of pre-ribosomal RNA in Saccharomyces cerevisiae. Yeast 11:1629-1650.
    • (1995) Yeast , vol.11 , pp. 1629-1650
    • Venema, J.1    Tollervey, D.2
  • 77
    • 0029853905 scopus 로고    scopus 로고
    • RRP5 is required for formation of both 18S and 5.8S rRNA in yeast
    • Venema, J., and D. Tollervey. 1996. RRP5 is required for formation of both 18S and 5.8S rRNA in yeast. EMBO J. 15:5701-5714.
    • (1996) EMBO J. , vol.15 , pp. 5701-5714
    • Venema, J.1    Tollervey, D.2
  • 78
    • 0029871347 scopus 로고    scopus 로고
    • PCR-synthesis of marker cassettes with long flanking homology regions for gene disruptions in S. cerevisiae
    • Wach, A. 1996. PCR-synthesis of marker cassettes with long flanking homology regions for gene disruptions in S. cerevisiae. Yeast 12:259-265.
    • (1996) Yeast , vol.12 , pp. 259-265
    • Wach, A.1
  • 79
    • 0030840519 scopus 로고    scopus 로고
    • Heterologous H1S3 marker and GFP reporter modules for PCR-targeting in Saccharomyces cerevisiae
    • Wach, A., A. Brachat, C. Alberti-Segui, C. Rebischung, and P. Philippsen. 1997. Heterologous H1S3 marker and GFP reporter modules for PCR-targeting in Saccharomyces cerevisiae. Yeast 13:1065-1075.
    • (1997) Yeast , vol.13 , pp. 1065-1075
    • Wach, A.1    Brachat, A.2    Alberti-Segui, C.3    Rebischung, C.4    Philippsen, P.5
  • 80
    • 0028676232 scopus 로고
    • New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae
    • Wach, A., A. Brachat, R. Pöhlmann, and P. Philippsen. 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    Pöhlmann, R.3    Philippsen, P.4
  • 81
    • 0024999340 scopus 로고
    • Single-step purification of shuttle vectors from yeast for high frequency back-transformation into E. coli
    • Ward, A. 1990. Single-step purification of shuttle vectors from yeast for high frequency back-transformation into E. coli. Nucleic Acids Res. 18:5319.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 5319
    • Ward, A.1
  • 82
    • 0026418629 scopus 로고
    • Alive with DEAD proteins
    • Wassarman, D. A., and J. A. Steitz. 1991. Alive with DEAD proteins. Nature 349:463-464.
    • (1991) Nature , vol.349 , pp. 463-464
    • Wassarman, D.A.1    Steitz, J.A.2
  • 84
    • 0028794516 scopus 로고
    • Construction of a set of convenient Saccharomyces cerevisiae strains that are isogenic to S288C
    • Winston, F., C. Dollard, and S. L. Ricupero-Hovasse. 1995. Construction of a set of convenient Saccharomyces cerevisiae strains that are isogenic to S288C. Yeast 11:53-55.
    • (1995) Yeast , vol.11 , pp. 53-55
    • Winston, F.1    Dollard, C.2    Ricupero-Hovasse, S.L.3


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