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Volumn 17, Issue 8, 1997, Pages 4474-4489

Evidence that GCN1 and GCN20, translational regulators of GCN4, function on elongating ribosomes in activation of eIF2α kinase GCN2

Author keywords

[No Author keywords available]

Indexed keywords

ELONGATION FACTOR 3; INITIATION FACTOR 2; PROTEIN KINASE; REGULATOR PROTEIN; RIBOSOME INACTIVATING PROTEIN;

EID: 1842287951     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/mcb.17.8.4474     Document Type: Article
Times cited : (181)

References (54)
  • 1
    • 0023392267 scopus 로고
    • A method for scne disruption that allows repeated use of URA3 selection in the construction of multiply disrupted yeast strains
    • Alani, E., L. Cao, and N. Kleckner. 1987. A method for scne disruption that allows repeated use of URA3 selection in the construction of multiply disrupted yeast strains. Genetics 116:541-545.
    • (1987) Genetics , vol.116 , pp. 541-545
    • Alani, E.1    Cao, L.2    Kleckner, N.3
  • 3
    • 0027486013 scopus 로고
    • PUB1 is a major nuclear and cytoplasmic polyadenylated RNA-binding protein in Saccharomyces cerevisiae
    • Anderson, J. T., M. R. Paddy, and M. S. Swanson. 1993. PUB1 is a major nuclear and cytoplasmic polyadenylated RNA-binding protein in Saccharomyces cerevisiae. Mol. Cell. Biol. 13:6102-5113.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 6102-15113
    • Anderson, J.T.1    Paddy, M.R.2    Swanson, M.S.3
  • 4
    • 0029049427 scopus 로고
    • Translation elongation factor-3 (EF-3): An evolvine eukaryotic ribosomal protein
    • Belfield, G. P., N. J. Ross-Smith, and M. F. Tuite. 1995. Translation elongation factor-3 (EF-3): an evolvine eukaryotic ribosomal protein. J. Mol. Evol. 41:376-387.
    • (1995) J. Mol. Evol. , vol.41 , pp. 376-387
    • Belfield, G.P.1    Ross-Smith, N.J.2    Tuite, M.F.3
  • 5
    • 0026094617 scopus 로고
    • Mutational analysis of the yeast a-factor transporter STE6, a member of the ATP binding cassette (ABC) protein superfamily
    • Berkower, C., and S. Michaelis. 1991. Mutational analysis of the yeast a-factor transporter STE6, a member of the ATP binding cassette (ABC) protein superfamily. EMBO J. 10:3777-3785.
    • (1991) EMBO J. , vol.10 , pp. 3777-3785
    • Berkower, C.1    Michaelis, S.2
  • 6
    • 0021668558 scopus 로고
    • A positive selection for mutants lacking orotidinc-5′-phosphate decarboxylase activity in yeast: 5-fluoro-orotic acid resistance
    • Boeke, J. D., F. LaCroute, and G. R. Fink. 1984. A positive selection for mutants lacking orotidinc-5′-phosphate decarboxylase activity in yeast: 5-fluoro-orotic acid resistance. Mol. Gen. Genet. 197:345-346.
    • (1984) Mol. Gen. Genet. , vol.197 , pp. 345-346
    • Boeke, J.D.1    LaCroute, F.2    Fink, G.R.3
  • 7
    • 0027732538 scopus 로고
    • Proteins regulating Ras and its relatives
    • Boguski, M. S., and F. McCormick. 1993. Proteins regulating Ras and its relatives. Nature 366:643-654.
    • (1993) Nature , vol.366 , pp. 643-654
    • Boguski, M.S.1    McCormick, F.2
  • 8
    • 0003174053 scopus 로고
    • The stringent response
    • F. C. Neidhardt, J. L. Ingraham, K. B. Low, B. Magasanik, M. Schaechter, and H. E. Umbarger (ed.), American Society for Microbiology, Washington. D.C.
    • Cashel, M., and K. E. Rudd. 1987. The stringent response, p. 1410-1438. In F. C. Neidhardt, J. L. Ingraham, K. B. Low, B. Magasanik, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella typhimurium: cellular and molecular biology. American Society for Microbiology, Washington. D.C.
    • (1987) Escherichia Coli and Salmonella Typhimurium: Cellular and Molecular Biology , pp. 1410-1438
    • Cashel, M.1    Rudd, K.E.2
  • 9
    • 0025310336 scopus 로고
    • A cluster of cystic fibrosis mutations in the first nucleotide-binding fold of the cystic fibrosis conductance regulator protein
    • Cutting, G. R., L. M. Kasch, B. J. Rosentein, J. Zielenski, L.-C. Tsui, S. E. Antonarakis, and H. Kazazian. 1990. A cluster of cystic fibrosis mutations in the first nucleotide-binding fold of the cystic fibrosis conductance regulator protein. Nature 346:366-369.
    • (1990) Nature , vol.346 , pp. 366-369
    • Cutting, G.R.1    Kasch, L.M.2    Rosentein, B.J.3    Zielenski, J.4    Tsui, L.-C.5    Antonarakis, S.E.6    Kazazian, H.7
  • 10
    • 0019843254 scopus 로고
    • Protein synthesis in yeast. I. Purification and properties of elongation factor 3 from Saccharomyces cerevisiae
    • Dasmahapatra, B., and K. Chakraburttry. 1981. Protein synthesis in yeast. I. Purification and properties of elongation factor 3 from Saccharomyces cerevisiae. J. Biol. Chem. 256:9999-10004.
    • (1981) J. Biol. Chem. , vol.256 , pp. 9999-10004
    • Dasmahapatra, B.1    Chakraburttry, K.2
  • 11
    • 0026556814 scopus 로고
    • Phosphorylation of initiation factor 2α by protein kinase GCN2 mediates gene-specific translational control of GCN4 in yeast
    • Dever, T. E., L. Feng, R. C. Wek, A. M. Cigan, T. D. Donahue, and A. G. Hinnebusch. 1992. Phosphorylation of initiation factor 2α by protein kinase GCN2 mediates gene-specific translational control of GCN4 in yeast. Cell 68:585-596.
    • (1992) Cell , vol.68 , pp. 585-596
    • Dever, T.E.1    Feng, L.2    Wek, R.C.3    Cigan, A.M.4    Donahue, T.D.5    Hinnebusch, A.G.6
  • 12
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux, J., P. Haeberli, and O. Smithies. 1984. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 12:387-395.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 13
    • 0020693541 scopus 로고
    • A short nucleotide sequence required for regulation of HIS4 by the general control system of yeast
    • Dunahue, T. F., R. S. Daves, G. Lucchini, and G. R. Fink. 1983. A short nucleotide sequence required for regulation of HIS4 by the general control system of yeast. Cell 32:89-98.
    • (1983) Cell , vol.32 , pp. 89-98
    • Dunahue, T.F.1    Daves, R.S.2    Lucchini, G.3    Fink, G.R.4
  • 15
    • 0027132575 scopus 로고
    • ABC transporters: Bacterial exporters
    • Fath, M. J., and R. Kolter. 1993. ABC transporters: bacterial exporters. Microbiol. Rev. 57:995-1017.
    • (1993) Microbiol. Rev. , vol.57 , pp. 995-1017
    • Fath, M.J.1    Kolter, R.2
  • 16
    • 0028263738 scopus 로고
    • Construction of an improved host strain for two hybrid screening
    • Feilotter, H. E., G. J. Hannon, C. J. Ruddell, and D. Beach. 1994. Construction of an improved host strain for two hybrid screening. Nucleic Acids Res. 22:15102-1503.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 15102-21503
    • Feilotter, H.E.1    Hannon, G.J.2    Ruddell, C.J.3    Beach, D.4
  • 17
    • 0020413063 scopus 로고
    • Analysis of temperature-sensitive mutant ts187 of Succharomyces cerevisiae altered in a component required for the initiation of protein synthesis
    • Feinberg, B., C. S. McLaughlin, and K. Moldave. 1982. Analysis of temperature-sensitive mutant ts187 of Succharomyces cerevisiae altered in a component required for the initiation of protein synthesis. J. Biol. Chem. 257: 1084-10851.
    • (1982) J. Biol. Chem. , vol.257 , pp. 1084-10851
    • Feinberg, B.1    McLaughlin, C.S.2    Moldave, K.3
  • 18
    • 0026482012 scopus 로고
    • Bacterial periplasmic permeases as model systems for the superfamily of traffic ATPases, including the multidrug resistance protein and the cystic fibrosis transmembrane conductance regulator
    • Ferro-Luzzi Ames, G. 1992. Bacterial periplasmic permeases as model systems for the superfamily of traffic ATPases, including the multidrug resistance protein and the cystic fibrosis transmembrane conductance regulator. Int. Rev. Cytol. 137A: 1-35.
    • (1992) Int. Rev. Cytol. , vol.137 A , pp. 1-35
    • Ferro-Luzzi Ames, G.1
  • 19
    • 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
  • 20
    • 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., and A. Sugino. 1988. New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites. Gene 74:527-34.
    • (1988) Gene , vol.74 , pp. 527-534
    • Gietz, R.D.1    Sugino, A.2
  • 21
    • 0025147469 scopus 로고
    • The translational activator GCN3 functions downstream from GCN1 and GCN2 in the regulatory pathway that couples GCN4 expression to amino acid availability in Saccharomyces-fs cerevisiae
    • Hannig, E. H., N. P. Williams, R. C. Wek, and A. G. Hinnebusch. 1990. The translational activator GCN3 functions downstream from GCN1 and GCN2 in the regulatory pathway that couples GCN4 expression to amino acid availability in Saccharomyces-fs cerevisiae. Genetics 126:549-562.
    • (1990) Genetics , vol.126 , pp. 549-562
    • Hannig, E.H.1    Williams, N.P.2    Wek, R.C.3    Hinnebusch, A.G.4
  • 22
    • 0025832056 scopus 로고
    • Translational control in mammalian cells
    • Hershey, J. W. B. 1991. Translational control in mammalian cells. Annu. Rev. Biochem. 60:717-755.
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 717-755
    • Hershey, J.W.B.1
  • 23
    • 0026621245 scopus 로고
    • ABC transporters: From microorganisms to man
    • Higgins, C. F. 1992. ABC transporters: from microorganisms to man. Annu. Rev. Cell Biol. 8:67-113.
    • (1992) Annu. Rev. Cell Biol. , vol.8 , pp. 67-113
    • Higgins, C.F.1
  • 24
    • 0000729653 scopus 로고    scopus 로고
    • Translational control of GCN4: Gene-specific regulation by phosphorylation of eIF2
    • J. W. B. Hershey, M. B. Malhews, and N. Sonenberg (ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Hinnebusch, A. G. 1996. Translational control of GCN4: gene-specific regulation by phosphorylation of eIF2, p. 199-244. In J. W. B. Hershey, M. B. Malhews, and N. Sonenberg (ed.), Translational control. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1996) Translational Control , pp. 199-244
    • Hinnebusch, A.G.1
  • 25
    • 0024437753 scopus 로고
    • Role of yeast elongation factor 3 in the elongation cycle
    • Kamath, A., and K. Chakraburtty. 1989. Role of yeast elongation factor 3 in the elongation cycle. J. Biol. Chem. 264:15423-15428.
    • (1989) J. Biol. Chem. , vol.264 , pp. 15423-15428
    • Kamath, A.1    Chakraburtty, K.2
  • 27
    • 0025170681 scopus 로고
    • The fungal vacuole: Composition, function, and biogenesis
    • Klionsky, D. J., P. Herman, and S. D. Emr. 1990. The fungal vacuole: composition, function, and biogenesis. Microbiol. Rev. 54:266-292.
    • (1990) Microbiol. Rev. , vol.54 , pp. 266-292
    • Klionsky, D.J.1    Herman, P.2    Emr, S.D.3
  • 28
    • 0026073302 scopus 로고
    • Highexpression vectors with multiple cloning sites for construction of trpE fusion genes: pATH vectors
    • Koerner, T. J., J. E. Hill, A. M. Myers, and A. Tzagoloff, 1991. Highexpression vectors with multiple cloning sites for construction of trpE fusion genes: pATH vectors. Methods Enzymol. 194:477-490.
    • (1991) Methods Enzymol. , vol.194 , pp. 477-490
    • Koerner, T.J.1    Hill, J.E.2    Myers, A.M.3    Tzagoloff, A.4
  • 29
    • 0026726804 scopus 로고
    • Autoregulation of the yeast lysyl-tRNA synthetase gene GCD5/KRS1 by translational and tianscriptional control mechanisms
    • Lanker, S., J. L. Bushman, A. G. Hinnebusch, H. Trachsel, and P. P. Mueller. 1992. Autoregulation of the yeast lysyl-tRNA synthetase gene GCD5/KRS1 by translational and tianscriptional control mechanisms. Cell 70:647-657.
    • (1992) Cell , vol.70 , pp. 647-657
    • Lanker, S.1    Bushman, J.L.2    Hinnebusch, A.G.3    Trachsel, H.4    Mueller, P.P.5
  • 30
    • 0030005755 scopus 로고    scopus 로고
    • The I.M.A.G.E. consortium: An integrated molecular analysis of genomes and their expression
    • Lennon, G., C. Auffray, M. Pnlymeropoulns, and M. B. Soares. 1996. The I.M.A.G.E. consortium: an integrated molecular analysis of genomes and their expression. Genomics 33:151-152.
    • (1996) Genomics , vol.33 , pp. 151-152
    • Lennon, G.1    Auffray, C.2    Pnlymeropoulns, M.3    Soares, M.B.4
  • 31
    • 0027175499 scopus 로고
    • GCN1, a translational activator of GCN4 in Saccharomyces cerevisiae, required for phosphorylalion of eukaryotic translation initiation factor 2 by protein kinase GCN2
    • Marton, M. J., D. Crouch, and A. G. Hinnebusch. 1993. GCN1, a translational activator of GCN4 in Saccharomyces cerevisiae, required for phosphorylalion of eukaryotic translation initiation factor 2 by protein kinase GCN2. Mol. Cell. Biol. 13:3541-3556.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 3541-3556
    • Marton, M.J.1    Crouch, D.2    Hinnebusch, A.G.3
  • 33
    • 0028568642 scopus 로고
    • Purified yeast translational initiation factor eIF-3 is an RNA-binding protein complex that contains the PRT1 protein
    • Naranda, T., S. E. MacMillan, and J. W. B. Hershey. 1994. Purified yeast translational initiation factor eIF-3 is an RNA-binding protein complex that contains the PRT1 protein. J. Biol. Chem. 269:32286-32292.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32286-32292
    • Naranda, T.1    MacMillan, S.E.2    Hershey, J.W.B.3
  • 35
    • 0029143936 scopus 로고
    • The duplicated Saccharomyces cerevisiae gene SSM1 encodes a eucaryotic homolog of the eubacterial and archaebacterial L1 ribosomal proteins
    • Petitjean, A., N. Bonneuaud, and F. Lacroute. 1995. The duplicated Saccharomyces cerevisiae gene SSM1 encodes a eucaryotic homolog of the eubacterial and archaebacterial L1 ribosomal proteins. Mol. Cell. Biol. 15:5071-5081.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5071-5081
    • Petitjean, A.1    Bonneuaud, N.2    Lacroute, F.3
  • 36
    • 0025801817 scopus 로고
    • Ribosome-association of GCN2 protein kinase, a translational activator of the GCN4 gene of Saccharomyces cerevisiae
    • Ramirez, M., R. C. Wek, and A. G. Hinnebusch. 1991. Ribosome-association of GCN2 protein kinase, a translational activator of the GCN4 gene of Saccharomyces cerevisiae. Mol. Cell. Biol. 11:3027-3036.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 3027-3036
    • Ramirez, M.1    Wek, R.C.2    Hinnebusch, A.G.3
  • 37
    • 0017263835 scopus 로고
    • Stringent factor from Escherichia culi directs ribosomal binding and release of uncharged tRNA
    • Richter, D. 1976. Stringent factor from Escherichia culi directs ribosomal binding and release of uncharged tRNA. Proc. Natl. Acad. Sci. USA 73:707-711.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 707-711
    • Richter, D.1
  • 39
    • 0031001762 scopus 로고    scopus 로고
    • The transcriptional activators BAS1, BAS2, and ABF1 bind positive regulatory sites as the critical elements for adenine regulation of ADE5,7
    • Rolfes, R. J., F. Zhang, and A. G. Hinnebusch. 1997. The transcriptional activators BAS1, BAS2, and ABF1 bind positive regulatory sites as the critical elements for adenine regulation of ADE5,7. J. Biol. Chem. 272: 13343-13354.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13343-13354
    • Rolfes, R.J.1    Zhang, F.2    Hinnebusch, A.G.3
  • 40
    • 0025140815 scopus 로고
    • Isolation and characterization of the structural gene encoding elongation factor 3
    • Sandbaken, M., J. A. Lupisella, B. DiDomenico, and K. Chakraburtty. 1990. Isolation and characterization of the structural gene encoding elongation factor 3. Biochim. Biophys. Acta 1050:230-234.
    • (1990) Biochim. Biophys. Acta , vol.1050 , pp. 230-234
    • Sandbaken, M.1    Lupisella, J.A.2    DiDomenico, B.3    Chakraburtty, K.4
  • 41
    • 0021163053 scopus 로고
    • An arginine/histidine exchange transport system in vacuolar-membrane vesicles of Saccharomyces cerevisiae
    • Sato, T., Y. Ohsumi, and Y. Anraku. 1984. An arginine/histidine exchange transport system in vacuolar-membrane vesicles of Saccharomyces cerevisiae. J. Biol. Chem. 259:11509-11511.
    • (1984) J. Biol. Chem. , vol.259 , pp. 11509-11511
    • Sato, T.1    Ohsumi, Y.2    Anraku, Y.3
  • 42
    • 0021128729 scopus 로고
    • Substrate specificities of active transport systems for amino acids in vacuolar-membrane vesicles of Saccharomyces cerevisiae
    • Sato, T., Y. Ohsumi, and Y. Anraku. 1984. Substrate specificities of active transport systems for amino acids in vacuolar-membrane vesicles of Saccharomyces cerevisiae. J. Biol. Chem. 259:11505-11508.
    • (1984) J. Biol. Chem. , vol.259 , pp. 11505-11508
    • Sato, T.1    Ohsumi, Y.2    Anraku, Y.3
  • 43
    • 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. Mieter. 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    Mieter, P.2
  • 44
    • 0344135964 scopus 로고
    • A ribosome-dependent GTPase from yeast distinct from elongation factor 2
    • Skogerson, L., and E. Wakatama. 1976. A ribosome-dependent GTPase from yeast distinct from elongation factor 2. Proc. Natl. Acad. Sci. USA 73:73-76.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 73-76
    • Skogerson, L.1    Wakatama, E.2
  • 45
    • 0028064872 scopus 로고
    • A yeast metal resistance protein similar to human cystic fibrosis transmembrane conductance regulator (CFTR) and multidrug resistance-associated protein
    • Szczypka, M. S., J. A. Wemmie, W. S. Moye-Rowley, and D. J. Thiele. 1994. A yeast metal resistance protein similar to human cystic fibrosis transmembrane conductance regulator (CFTR) and multidrug resistance-associated protein. J. Biol. Chem. 269:22853-22857.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22853-22857
    • Szczypka, M.S.1    Wemmie, J.A.2    Moye-Rowley, W.S.3    Thiele, D.J.4
  • 46
    • 0029154909 scopus 로고
    • The elongation factor unique in higher fungi and essential for protein biosynthesis is an E site factor
    • Triana-Alonso, F. J., K. Chakraburtty, and K. H. Nierhaus. 1995. The elongation factor unique in higher fungi and essential for protein biosynthesis is an E site factor. J. Biol. Chem. 270:20473-20478.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20473-20478
    • Triana-Alonso, F.J.1    Chakraburtty, K.2    Nierhaus, K.H.3
  • 47
    • 0023733679 scopus 로고
    • Role of yeast elongation factor 3 (EF-3) at the AA-tRNA binding step
    • Uritani, M., and M. Miyazaki. 1988. Role of yeast elongation factor 3 (EF-3) at the AA-tRNA binding step. J. Biochem. 104:118-126.
    • (1988) J. Biochem. , vol.104 , pp. 118-126
    • Uritani, M.1    Miyazaki, M.2
  • 48
    • 0029001571 scopus 로고
    • GCN20, a novel ATP binding cassette protein, and GCN1 reside in a complex that mediates activation of the eIF-2u kinase GCN2 in amino acidstarved cells
    • Vazquez de Aldana, C. R., M. J. Marton, and A. G. Hinnebusch. 1995. GCN20, a novel ATP binding cassette protein, and GCN1 reside in a complex that mediates activation of the eIF-2u kinase GCN2 in amino acidstarved cells. EMBO J. 14:3184-3199.
    • (1995) EMBO J. , vol.14 , pp. 3184-3199
    • Vazquez De Aldana, C.R.1    Marton, M.J.2    Hinnebusch, A.G.3
  • 49
    • 0024381444 scopus 로고
    • Juxtaposition of domains homologous to protein kinases and histidyl-tRNA synthetases in GCN2 protein suggests a mechanism for coupling GCN4 expression to amino acid availability
    • Wek, R. C., B. M. Jackson, and A. G. Hinnebusch. 1989 Juxtaposition of domains homologous to protein kinases and histidyl-tRNA synthetases in GCN2 protein suggests a mechanism for coupling GCN4 expression to amino acid availability. Proc. Natl. Acad. Sci. USA 86:4579-1583.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 4579-11583
    • Wek, R.C.1    Jackson, B.M.2    Hinnebusch, A.G.3
  • 50
    • 0029006391 scopus 로고
    • The histidyl-tRNA synthetaserelated sequence in the eIF-2α protein kinase GCN2 interacts with tRNA and is required for activation in response to starvation for different amino acids
    • Wek, S. A., S. Zhu, and R. C. Wek. 1995. The histidyl-tRNA synthetaserelated sequence in the eIF-2α protein kinase GCN2 interacts with tRNA and is required for activation in response to starvation for different amino acids. Mol. Cell. Biol. 15:4497-4506.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4497-4506
    • Wek, S.A.1    Zhu, S.2    Wek, R.C.3
  • 51
    • 0028575444 scopus 로고
    • Cadmium tolerance mediated by the yeast AP-1 protein requires the presence of an ATP-binding cassette transporter-encoding gene. YCF1
    • Wemmie, J. A., M. S. Szczypka, D. J. Thiele, and W. S. Moye-Rowley. 1994. Cadmium tolerance mediated by the yeast AP-1 protein requires the presence of an ATP-binding cassette transporter-encoding gene. YCF1. J. Biol. Chem. 269:32592-32597.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32592-32597
    • Wemmie, J.A.1    Szczypka, M.S.2    Thiele, D.J.3    Moye-Rowley, W.S.4
  • 52
    • 0018668142 scopus 로고
    • Vacuoles: The sole compartments of digestive enzymes in yeast Saccharomyces cerevisiae?
    • Wiemkin, A., M. Schellenberg, and K. Urech. 1979. Vacuoles: the sole compartments of digestive enzymes in yeast Saccharomyces cerevisiae? Arch. Microbiol. 123:23-35.
    • (1979) Arch. Microbiol. , vol.123 , pp. 23-35
    • Wiemkin, A.1    Schellenberg, M.2    Urech, K.3
  • 53
    • 0025362525 scopus 로고
    • Role of vacuolar acidification in protein sorting and zymogen activation: A genetic analysis of the yeast vacuolar proton-translocating ATPase
    • Yamashiro, C. T., P. M. Kane, D. F. Wolczyk, R. A. Preston, and T. H. Stevens. 1990. Role of vacuolar acidification in protein sorting and zymogen activation: a genetic analysis of the yeast vacuolar proton-translocating ATPase. Mol. Cell. Biol. 10:3737-3749.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 3737-3749
    • Yamashiro, C.T.1    Kane, P.M.2    Wolczyk, D.F.3    Preston, R.A.4    Stevens, T.H.5
  • 54
    • 0024368864 scopus 로고
    • Precise gene fusion by PCR
    • Yon, J., and M. Fried. 1988. Precise gene fusion by PCR. Nucleic Acids Res. 17:4895.
    • (1988) Nucleic Acids Res. , vol.17 , pp. 4895
    • Yon, J.1    Fried, M.2


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