메뉴 건너뛰기




Volumn 392, Issue 3, 2009, Pages 701-722

Archaeal aIF2B Interacts with Eukaryotic Translation Initiation Factors eIF2α and eIF2Bα: Implications for aIF2B Function and eIF2B Regulation

Author keywords

aIF2B; archaea; eIF2; eIF2B; S. cerevisiae

Indexed keywords

GUANINE NUCLEOTIDE EXCHANGE FACTOR; INITIATION FACTOR; INITIATION FACTOR 2ALPHA; INITIATION FACTOR 2BALPHA; NUCLEOTIDYLTRANSFERASE; RIBOSOME PROTEIN; UNCLASSIFIED DRUG;

EID: 69349100057     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.07.030     Document Type: Article
Times cited : (27)

References (50)
  • 1
    • 34247111608 scopus 로고    scopus 로고
    • eIF2α phosphorylation in cellular stress responses and disease
    • Mathews M., Sonenberg N., and Hershey J.W.B. (Eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Ron D., and Harding H.P. eIF2α phosphorylation in cellular stress responses and disease. In: Mathews M., Sonenberg N., and Hershey J.W.B. (Eds). Translational Control in Biology and Medicine (2007), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY 345-368
    • (2007) Translational Control in Biology and Medicine , pp. 345-368
    • Ron, D.1    Harding, H.P.2
  • 2
    • 36649031282 scopus 로고    scopus 로고
    • The eIF2α kinases
    • Mathews M., Sonenberg N., and Hershey J.W.B. (Eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Dever T.E., Dar A.C., and Sicheri F. The eIF2α kinases. In: Mathews M., Sonenberg N., and Hershey J.W.B. (Eds). Translational Control in Biology and Medicine (2007), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY 319-344
    • (2007) Translational Control in Biology and Medicine , pp. 319-344
    • Dever, T.E.1    Dar, A.C.2    Sicheri, F.3
  • 3
    • 33847416604 scopus 로고    scopus 로고
    • A synthetic protein approach toward accurate mass spectrometric quantification of component stoichiometry of multiprotein complexes
    • Kito K., Ota K., Fujita T., and Ito T. A synthetic protein approach toward accurate mass spectrometric quantification of component stoichiometry of multiprotein complexes. J. Proteome Res. 6 (2007) 792-800
    • (2007) J. Proteome Res. , vol.6 , pp. 792-800
    • Kito, K.1    Ota, K.2    Fujita, T.3    Ito, T.4
  • 4
    • 34249665243 scopus 로고    scopus 로고
    • Mechanism of translation initiation in the yeast Saccharomyces cerevisiae
    • Mathews M., Sonenberg N., and Hershey J.W.B. (Eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Hinnebusch A.G., Dever T.E., and Asano K. Mechanism of translation initiation in the yeast Saccharomyces cerevisiae. In: Mathews M., Sonenberg N., and Hershey J.W.B. (Eds). Translational Control in Biology and Medicine (2007), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY 225-268
    • (2007) Translational Control in Biology and Medicine , pp. 225-268
    • Hinnebusch, A.G.1    Dever, T.E.2    Asano, K.3
  • 5
    • 0036790688 scopus 로고    scopus 로고
    • Characterization of the minimal catalytic domain within eIF2B: the guanine-nucleotide exchange factor for translation initiation
    • Gomez E., Mohammad S.S., and Pavitt G.D. Characterization of the minimal catalytic domain within eIF2B: the guanine-nucleotide exchange factor for translation initiation. EMBO J. 21 (2002) 5292-5301
    • (2002) EMBO J. , vol.21 , pp. 5292-5301
    • Gomez, E.1    Mohammad, S.S.2    Pavitt, G.D.3
  • 6
    • 0032519585 scopus 로고    scopus 로고
    • eIF2 independently binds two distinct eIF2B subcomplexes that catalyze and regulate guanine-nucleotide exchange
    • Pavitt G.D., Ramaiah K.V.A., Kimball S.R., and Hinnebusch A.G. eIF2 independently binds two distinct eIF2B subcomplexes that catalyze and regulate guanine-nucleotide exchange. Genes Dev. 12 (1998) 514-526
    • (1998) Genes Dev. , vol.12 , pp. 514-526
    • Pavitt, G.D.1    Ramaiah, K.V.A.2    Kimball, S.R.3    Hinnebusch, A.G.4
  • 7
    • 0031020341 scopus 로고    scopus 로고
    • Homologous segments in three subunits of the guanine nucleotide exchange factor eIF2B mediate translational regulation by phosphorylation of eIF2
    • Pavitt G.D., Yang W., and Hinnebusch A.G. Homologous segments in three subunits of the guanine nucleotide exchange factor eIF2B mediate translational regulation by phosphorylation of eIF2. Mol. Cell. Biol. 17 (1997) 1298-1313
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1298-1313
    • Pavitt, G.D.1    Yang, W.2    Hinnebusch, A.G.3
  • 8
    • 0029805459 scopus 로고    scopus 로고
    • Identification of a regulatory subcomplex in the guanine nucleotide exchange factor eIF2B that mediates inhibition by phosphorylated eIF2
    • Yang W., and Hinnebusch A.G. Identification of a regulatory subcomplex in the guanine nucleotide exchange factor eIF2B that mediates inhibition by phosphorylated eIF2. Mol. Cell. Biol. 16 (1996) 6603-6616
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6603-6616
    • Yang, W.1    Hinnebusch, A.G.2
  • 9
    • 0034960171 scopus 로고    scopus 로고
    • Tight binding of the phosphorylated α subunit of initiation factor 2 (eIF2α) to the regulatory subunits of guanine nucleotide exchange factor eIF2B is required for inhibition of translation initiation
    • Krishnamoorthy T., Pavitt G.D., Zhang F., Dever T.E., and Hinnebusch A.G. Tight binding of the phosphorylated α subunit of initiation factor 2 (eIF2α) to the regulatory subunits of guanine nucleotide exchange factor eIF2B is required for inhibition of translation initiation. Mol. Cell. Biol. 21 (2001) 5018-5030
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 5018-5030
    • Krishnamoorthy, T.1    Pavitt, G.D.2    Zhang, F.3    Dever, T.E.4    Hinnebusch, A.G.5
  • 10
    • 20144386673 scopus 로고    scopus 로고
    • PKR and GCN2 kinases and guanine nucleotide exchange factor eukaryotic translation initiation factor 2B (eIF2B) recognize overlapping surfaces on eIF2alpha
    • Dey M., Trieselmann B., Locke E.G., Lu J., Cao C., Dar A.C., et al. PKR and GCN2 kinases and guanine nucleotide exchange factor eukaryotic translation initiation factor 2B (eIF2B) recognize overlapping surfaces on eIF2alpha. Mol. Cell. Biol. 25 (2005) 3063-3075
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 3063-3075
    • Dey, M.1    Trieselmann, B.2    Locke, E.G.3    Lu, J.4    Cao, C.5    Dar, A.C.6
  • 11
    • 0030924304 scopus 로고    scopus 로고
    • Subunit assembly and guanine nucleotide exchange activity of eukaryotic initiation factor-2B expressed in Sf9 cells
    • Fabian J.R., Kimball S.R., Heinzinger N.K., and Jefferson L.S. Subunit assembly and guanine nucleotide exchange activity of eukaryotic initiation factor-2B expressed in Sf9 cells. J. Biol. Chem. 272 (1997) 12359-12365
    • (1997) J. Biol. Chem. , vol.272 , pp. 12359-12365
    • Fabian, J.R.1    Kimball, S.R.2    Heinzinger, N.K.3    Jefferson, L.S.4
  • 12
    • 0032557657 scopus 로고    scopus 로고
    • Regulation of guanine nucleotide exchange through phosphorylation of eukaryotic initiation factor eIF2α
    • Kimball S.R., Fabian J.R., Pavitt G.D., Hinnebusch A.G., and Jefferson L.S. Regulation of guanine nucleotide exchange through phosphorylation of eukaryotic initiation factor eIF2α. J. Biol. Chem. 273 (1998) 12841-12845
    • (1998) J. Biol. Chem. , vol.273 , pp. 12841-12845
    • Kimball, S.R.1    Fabian, J.R.2    Pavitt, G.D.3    Hinnebusch, A.G.4    Jefferson, L.S.5
  • 13
    • 37749042263 scopus 로고    scopus 로고
    • Cavicchioli R. (Ed), ASM Press, Washington, DC
    • In: Cavicchioli R. (Ed). Archaea-Molecular and Cellular Biology (2007), ASM Press, Washington, DC
    • (2007) Archaea-Molecular and Cellular Biology
  • 14
    • 0025300402 scopus 로고
    • Towards a natural system of organisms: proposal for the domains Archaea, Bacteria, and Eucarya
    • Woese C.R., Kandler O., and Wheelis M.L. Towards a natural system of organisms: proposal for the domains Archaea, Bacteria, and Eucarya. Proc. Natl Acad. Sci. USA 87 (1990) 4576-4579
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 4576-4579
    • Woese, C.R.1    Kandler, O.2    Wheelis, M.L.3
  • 16
    • 15944425052 scopus 로고    scopus 로고
    • The archaeal eIF2 homologue: functional properties of an ancient translation initiation factor
    • Pedulla N., Palermo R., Hasenohrl D., Blasi U., Cammarano P., and Londei P. The archaeal eIF2 homologue: functional properties of an ancient translation initiation factor. Nucleic Acids Res. 33 (2005) 1804-1812
    • (2005) Nucleic Acids Res. , vol.33 , pp. 1804-1812
    • Pedulla, N.1    Palermo, R.2    Hasenohrl, D.3    Blasi, U.4    Cammarano, P.5    Londei, P.6
  • 17
    • 1942437572 scopus 로고    scopus 로고
    • Functional molecular mapping of archaeal translation initiation factor 2
    • Yatime L., Schmitt E., Blanquet S., and Mechulam Y. Functional molecular mapping of archaeal translation initiation factor 2. J. Biol. Chem. 279 (2004) 15984-15993
    • (2004) J. Biol. Chem. , vol.279 , pp. 15984-15993
    • Yatime, L.1    Schmitt, E.2    Blanquet, S.3    Mechulam, Y.4
  • 18
    • 36749037829 scopus 로고    scopus 로고
    • Structure of an archaeal heterotrimeric initiation factor 2 reveals a nucleotide state between the GTP and the GDP states
    • Yatime L., Mechulam Y., Blanquet S., and Schmitt E. Structure of an archaeal heterotrimeric initiation factor 2 reveals a nucleotide state between the GTP and the GDP states. Proc. Natl Acad. Sci. USA 104 (2007) 18445-18450
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 18445-18450
    • Yatime, L.1    Mechulam, Y.2    Blanquet, S.3    Schmitt, E.4
  • 19
    • 34548846390 scopus 로고    scopus 로고
    • New insights into the interactions of the translation initiation factor 2 from archaea with guanine nucleotides and initiator tRNA
    • Nikonov O., Stolboushkina E., Nikulin A., Hasenohrl D., Blasi U., Manstein D.J., et al. New insights into the interactions of the translation initiation factor 2 from archaea with guanine nucleotides and initiator tRNA. J. Mol. Biol. 373 (2007) 328-336
    • (2007) J. Mol. Biol. , vol.373 , pp. 328-336
    • Nikonov, O.1    Stolboushkina, E.2    Nikulin, A.3    Hasenohrl, D.4    Blasi, U.5    Manstein, D.J.6
  • 20
    • 2442714840 scopus 로고    scopus 로고
    • In vitro phosphorylation of initiation factor 2 alpha (aIF2 alpha) from hyperthermophilic archaeon Pyrococcus horikoshii OT3
    • Tahara M., Ohsawa A., Saito S., and Kimura M. In vitro phosphorylation of initiation factor 2 alpha (aIF2 alpha) from hyperthermophilic archaeon Pyrococcus horikoshii OT3. J. Biochem. 135 (2004) 479-485
    • (2004) J. Biochem. , vol.135 , pp. 479-485
    • Tahara, M.1    Ohsawa, A.2    Saito, S.3    Kimura, M.4
  • 21
    • 0033559265 scopus 로고    scopus 로고
    • Conserved bipartite motifs in yeast eIF5 and eIF2Be{open}, GTPase-activating and GDP-GTP exchange factors in translation initiation, mediate binding to their common substrate eIF2
    • Asano K., Krishnamoorthy T., Phan L., Pavitt G.D., and Hinnebusch A.G. Conserved bipartite motifs in yeast eIF5 and eIF2Be{open}, GTPase-activating and GDP-GTP exchange factors in translation initiation, mediate binding to their common substrate eIF2. EMBO J. 18 (1999) 1673-1688
    • (1999) EMBO J. , vol.18 , pp. 1673-1688
    • Asano, K.1    Krishnamoorthy, T.2    Phan, L.3    Pavitt, G.D.4    Hinnebusch, A.G.5
  • 22
    • 33847157932 scopus 로고    scopus 로고
    • Archaeal type III RuBisCOs function in a pathway for AMP metabolism
    • Sato T., Atomi H., and Imanaka T. Archaeal type III RuBisCOs function in a pathway for AMP metabolism. Science 315 (2007) 1003-1006
    • (2007) Science , vol.315 , pp. 1003-1006
    • Sato, T.1    Atomi, H.2    Imanaka, T.3
  • 23
    • 4344584575 scopus 로고    scopus 로고
    • Crystal structure of yeast Ypr118w, a methylthioribose-1-phosphate isomerase related to regulatory eIF2B subunits
    • Bumann M., Djafarzadeh S., Oberholzer A.E., Bigler P., Altmann M., Trachsel H., and Baumann U. Crystal structure of yeast Ypr118w, a methylthioribose-1-phosphate isomerase related to regulatory eIF2B subunits. J. Biol. Chem. 279 (2004) 37087-37094
    • (2004) J. Biol. Chem. , vol.279 , pp. 37087-37094
    • Bumann, M.1    Djafarzadeh, S.2    Oberholzer, A.E.3    Bigler, P.4    Altmann, M.5    Trachsel, H.6    Baumann, U.7
  • 25
    • 2942592401 scopus 로고    scopus 로고
    • Crystal structure of the regulatory subunit of archaeal initiation factor 2B (aIF2B) from hyperthermophilic archaeon Pyrococcus horikoshii OT3: a proposed structure of the regulatory subcomplex of eukaryotic IF2B
    • Kakuta Y., Tahara M., Maetani S., Yao M., Tanaka I., and Kimura M. Crystal structure of the regulatory subunit of archaeal initiation factor 2B (aIF2B) from hyperthermophilic archaeon Pyrococcus horikoshii OT3: a proposed structure of the regulatory subcomplex of eukaryotic IF2B. Biochem. Biophys. Res. Commun. 319 (2004) 725-732
    • (2004) Biochem. Biophys. Res. Commun. , vol.319 , pp. 725-732
    • Kakuta, Y.1    Tahara, M.2    Maetani, S.3    Yao, M.4    Tanaka, I.5    Kimura, M.6
  • 26
    • 0037053309 scopus 로고    scopus 로고
    • Crystal structure of the N-terminal segment of human eukaryotic translation initiation factor 2alpha
    • Nonato M.C., Widom J., and Clardy J. Crystal structure of the N-terminal segment of human eukaryotic translation initiation factor 2alpha. J. Biol. Chem. 277 (2002) 17057-17061
    • (2002) J. Biol. Chem. , vol.277 , pp. 17057-17061
    • Nonato, M.C.1    Widom, J.2    Clardy, J.3
  • 27
    • 25144502820 scopus 로고    scopus 로고
    • Higher-order substrate recognition of eIF2alpha by the RNA-dependent protein kinase PKR
    • Dar A.C., Dever T.E., and Sicheri F. Higher-order substrate recognition of eIF2alpha by the RNA-dependent protein kinase PKR. Cell 122 (2005) 887-900
    • (2005) Cell , vol.122 , pp. 887-900
    • Dar, A.C.1    Dever, T.E.2    Sicheri, F.3
  • 28
    • 27144510561 scopus 로고    scopus 로고
    • Translational regulation of GCN4 and the general amino acid control of yeast
    • Hinnebusch A.G. Translational regulation of GCN4 and the general amino acid control of yeast. Annu. Rev. Microbiol. 59 (2005) 407-450
    • (2005) Annu. Rev. Microbiol. , vol.59 , pp. 407-450
    • Hinnebusch, A.G.1
  • 29
    • 0029144599 scopus 로고
    • Multidomain organization of eukaryotic guanine nucleotide exchange translation initiation factor eIF-2B subunits revealed by analysis of conserved sequence motifs
    • Koonin E.V. Multidomain organization of eukaryotic guanine nucleotide exchange translation initiation factor eIF-2B subunits revealed by analysis of conserved sequence motifs. Protein Sci. 4 (1995) 1608-1617
    • (1995) Protein Sci. , vol.4 , pp. 1608-1617
    • Koonin, E.V.1
  • 30
    • 0027177312 scopus 로고
    • A protein complex of translational regulators of GCN4 is the guanine nucleotide exchange factor for eIF-2 in yeast
    • Cigan A.M., Bushman J.L., Boal T.R., and Hinnebusch A.G. A protein complex of translational regulators of GCN4 is the guanine nucleotide exchange factor for eIF-2 in yeast. Proc. Natl Acad. Sci. USA 90 (1993) 5350-5354
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 5350-5354
    • Cigan, A.M.1    Bushman, J.L.2    Boal, T.R.3    Hinnebusch, A.G.4
  • 31
    • 0023797126 scopus 로고
    • Molecular analysis of GCN3, a translational activator of GCN4: evidence for posttranslational control of GCN3 regulatory function
    • Hannig E.M., and Hinnebusch A.G. Molecular analysis of GCN3, a translational activator of GCN4: evidence for posttranslational control of GCN3 regulatory function. Mol. Cell. Biol. 8 (1988) 4808-4820
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 4808-4820
    • Hannig, E.M.1    Hinnebusch, A.G.2
  • 32
    • 33847118046 scopus 로고    scopus 로고
    • TFB1 or TFB2 is sufficient for Thermococcus kodakaraensis viability and for basal transcription in vitro
    • Santangelo T.J., Cubonova L., James C.L., and Reeve J.N. TFB1 or TFB2 is sufficient for Thermococcus kodakaraensis viability and for basal transcription in vitro. J. Mol. Biol. 367 (2007) 344-357
    • (2007) J. Mol. Biol. , vol.367 , pp. 344-357
    • Santangelo, T.J.1    Cubonova, L.2    James, C.L.3    Reeve, J.N.4
  • 33
    • 0000889541 scopus 로고
    • Mutations in the GCD7 subunit of yeast guanine nucleotide exchange factor eIF-2B overcome the inhibitory effects of phosphorylated eIF-2 on translation initiation
    • Vazquez de Aldana C.R., and Hinnebusch A.G. Mutations in the GCD7 subunit of yeast guanine nucleotide exchange factor eIF-2B overcome the inhibitory effects of phosphorylated eIF-2 on translation initiation. Mol. Cell. Biol. 14 (1994) 3208-3222
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 3208-3222
    • Vazquez de Aldana, C.R.1    Hinnebusch, A.G.2
  • 34
    • 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 cerevisiae
    • Hannig E.H., Williams N.P., Wek R.C., and Hinnebusch A.G. The translational activator GCN3 functions downstream from GCN1 and GCN2 in the regulatory pathway that couples GCN4 expression to amino acid availability in Saccharomyces cerevisiae. Genetics 126 (1990) 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
  • 35
    • 0022817680 scopus 로고
    • Multiple GCD genes required for repression of GCN4, a transcriptional activator of amino acid biosynthetic genes in Saccharomyces cerevisiae
    • Harashima S., and Hinnebusch A.G. Multiple GCD genes required for repression of GCN4, a transcriptional activator of amino acid biosynthetic genes in Saccharomyces cerevisiae. Mol. Cell. Biol. 6 (1986) 3990-3998
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 3990-3998
    • Harashima, S.1    Hinnebusch, A.G.2
  • 36
    • 0021799425 scopus 로고
    • The 60S ribosomal subunit as a carrier of eukaryotic initiation factor 2 and the site of reversing factor activity during protein synthesis
    • Shaun N., Thomas B., Matts R.L., Levin D.H., and London I.M. The 60S ribosomal subunit as a carrier of eukaryotic initiation factor 2 and the site of reversing factor activity during protein synthesis. J. Biol. Chem. 260 (1985) 9860-9866
    • (1985) J. Biol. Chem. , vol.260 , pp. 9860-9866
    • Shaun, N.1    Thomas, B.2    Matts, R.L.3    Levin, D.H.4    London, I.M.5
  • 37
    • 25644436944 scopus 로고    scopus 로고
    • Translation initiation: structures, mechanisms and evolution
    • Marintchev A., and Wagner G. Translation initiation: structures, mechanisms and evolution. Q. Rev. Biophys. 37 (2004) 197-284
    • (2004) Q. Rev. Biophys. , vol.37 , pp. 197-284
    • Marintchev, A.1    Wagner, G.2
  • 38
    • 4444333127 scopus 로고    scopus 로고
    • Solution structure of human initiation factor eIF2alpha reveals homology to the elongation factor eEF1B
    • Ito T., Marintchev A., and Wagner G. Solution structure of human initiation factor eIF2alpha reveals homology to the elongation factor eEF1B. Structure 12 (2004) 1693-1704
    • (2004) Structure , vol.12 , pp. 1693-1704
    • Ito, T.1    Marintchev, A.2    Wagner, G.3
  • 39
    • 0021099673 scopus 로고
    • A GDP/GTP exchange factor essential for eukaryotic initiation factor 2 cycling in Ehrlich ascites tumor cells and its regulation by eukaryotic initiation factor 2 phosphorylation
    • Panniers R., and Henshaw E.C. A GDP/GTP exchange factor essential for eukaryotic initiation factor 2 cycling in Ehrlich ascites tumor cells and its regulation by eukaryotic initiation factor 2 phosphorylation. J. Biol. Chem. 258 (1983) 7928-7934
    • (1983) J. Biol. Chem. , vol.258 , pp. 7928-7934
    • Panniers, R.1    Henshaw, E.C.2
  • 40
    • 0021099278 scopus 로고
    • Purification of the eukaryotic initiation factor 2-eukaryotic initiation factor 2B complex and characterization of its guanine nucleotide exchange activity during protein synthesis initiation
    • Konieczny A., and Safer B. Purification of the eukaryotic initiation factor 2-eukaryotic initiation factor 2B complex and characterization of its guanine nucleotide exchange activity during protein synthesis initiation. J. Biol. Chem. 258 (1983) 3402-3408
    • (1983) J. Biol. Chem. , vol.258 , pp. 3402-3408
    • Konieczny, A.1    Safer, B.2
  • 41
    • 0021722443 scopus 로고
    • Regulation of protein synthesis in eukaryotes. Mode of action of eRF, an eIF-2-recycling factor from rabbit reticulocytes in GDP/GTP exchange
    • Salimans M., Goumans H., Amesz H., Beene R., and Voorma H.O. Regulation of protein synthesis in eukaryotes. Mode of action of eRF, an eIF-2-recycling factor from rabbit reticulocytes in GDP/GTP exchange. Eur. J. Biochem. 145 (1984) 91-98
    • (1984) Eur. J. Biochem. , vol.145 , pp. 91-98
    • Salimans, M.1    Goumans, H.2    Amesz, H.3    Beene, R.4    Voorma, H.O.5
  • 42
    • 0025853453 scopus 로고
    • Complex formation by positive and negative translational regulators of GCN4
    • Cigan A.M., Foiani M., Hannig E.M., and Hinnebusch A.G. Complex formation by positive and negative translational regulators of GCN4. Mol. Cell. Biol. 11 (1991) 3217-3228
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 3217-3228
    • Cigan, A.M.1    Foiani, M.2    Hannig, E.M.3    Hinnebusch, A.G.4
  • 43
    • 0028954118 scopus 로고
    • Studies on the transformation of intact yeast cells by the LiAc/SS-DNA/PEG procedure
    • Gietz R.D., Willems A.R., and Woods R.A. Studies on the transformation of intact yeast cells by the LiAc/SS-DNA/PEG procedure. Yeast 11 (1995) 355-560
    • (1995) Yeast , vol.11 , pp. 355-560
    • Gietz, R.D.1    Willems, A.R.2    Woods, R.A.3
  • 44
    • 0028971194 scopus 로고
    • Modulation of tRNAiMet, eIF-2 and eIF-2B expression shows that GCN4 translation is inversely coupled to the level of eIF-2.GTP.Met-tRNAiMet ternary complexes
    • Dever T.E., Yang W., Åström S., Byström A.S., and Hinnebusch A.G. Modulation of tRNAiMet, eIF-2 and eIF-2B expression shows that GCN4 translation is inversely coupled to the level of eIF-2.GTP.Met-tRNAiMet ternary complexes. Mol. Cell. Biol. 15 (1995) 6351-6363
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6351-6363
    • Dever, T.E.1    Yang, W.2    Åström, S.3    Byström, A.S.4    Hinnebusch, A.G.5
  • 46
    • 41949115912 scopus 로고    scopus 로고
    • Double-stranded RNA-activated protein kinase PKR of fishes and amphibians: varying the number of double-stranded RNA binding domains and lineage-specific duplications
    • Rothenburg S., Deigendesch N., Dey M., Dever T.E., and Tazi L. Double-stranded RNA-activated protein kinase PKR of fishes and amphibians: varying the number of double-stranded RNA binding domains and lineage-specific duplications. BMC Biol. 6 (2008) 12
    • (2008) BMC Biol. , vol.6 , pp. 12
    • Rothenburg, S.1    Deigendesch, N.2    Dey, M.3    Dever, T.E.4    Tazi, L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.