메뉴 건너뛰기




Volumn 27, Issue 14, 2007, Pages 5225-5234

Critical contacts between the eukaryotic initiation factor 2B (eIF2B) catalytic domain and both eIF2β and -2γ mediate guanine nucleotide exchange

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE EXCHANGE FACTOR; MUTANT PROTEIN;

EID: 34447514386     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.00495-07     Document Type: Article
Times cited : (28)

References (44)
  • 2
    • 33744957161 scopus 로고    scopus 로고
    • Direct binding of translation initiation factor eIF2γ-G domain to its GTPase-activating and GDP-GTP exchange factors eIF5 and eIF2B epsilon
    • Alone, P. V., and T. E. Dever. 2006. Direct binding of translation initiation factor eIF2γ-G domain to its GTPase-activating and GDP-GTP exchange factors eIF5 and eIF2B epsilon. J. Biol. Chem. 281:12636-12644.
    • (2006) J. Biol. Chem , vol.281 , pp. 12636-12644
    • Alone, P.V.1    Dever, T.E.2
  • 3
    • 31344470389 scopus 로고    scopus 로고
    • Diversification of catalytic activities and ligand interactions in the protein fold shared by the sugar isomerases, eIF2B, DeoR transcription factors, acyl-CoA transferases and methenyltetrahydrofolate synthetase
    • Anantharaman, V., and L. Aravind. 2006. Diversification of catalytic activities and ligand interactions in the protein fold shared by the sugar isomerases, eIF2B, DeoR transcription factors, acyl-CoA transferases and methenyltetrahydrofolate synthetase. J. Mol. Biol. 356:823-842.
    • (2006) J. Mol. Biol , vol.356 , pp. 823-842
    • Anantharaman, V.1    Aravind, L.2
  • 4
    • 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., L. Pedersen, L. Valente, I. Chatterjee, T. G. Kinzy, M. Kjeldgaard, and J. Nyborg. 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
  • 6
    • 0033559265 scopus 로고    scopus 로고
    • Conserved bipartite motifs in yeast eIF5 and eIF2Bε, GTPase-activating and GDP-GTP exchange factors in translation initiation, mediate binding to their common substrate eIF2
    • Asano, K., T. Krishnamoorthy, L. Phan, G. D. Pavitt, and A. G. Hinnebusch. 1999. Conserved bipartite motifs in yeast eIF5 and eIF2Bε, GTPase-activating and GDP-GTP exchange factors in translation initiation, mediate binding to their common substrate eIF2. EMBO J. 18:1673-1688.
    • (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
  • 8
    • 33746713880 scopus 로고    scopus 로고
    • The crystal structure of the carboxy-terminal domain of human translation initiation factor eIF5
    • Bieniossek, C., P. Schutz, M. Bumann, A. Limacher, I. Uson, and U. Baumann. 2006. The crystal structure of the carboxy-terminal domain of human translation initiation factor eIF5. J. Mol. Biol. 360:457-465.
    • (2006) J. Mol. Biol , vol.360 , pp. 457-465
    • Bieniossek, C.1    Schutz, P.2    Bumann, M.3    Limacher, A.4    Uson, I.5    Baumann, U.6
  • 9
    • 1542368830 scopus 로고    scopus 로고
    • Structure of the catalytic fragment of translation initiation factor 2B and identification of a critically important catalytic residue
    • Boesen, T., S. S. Mohammad, G. D. Pavitt, and G. R. Andersen. 2004. Structure of the catalytic fragment of translation initiation factor 2B and identification of a critically important catalytic residue. J. Biol. Chem. 279: 10584-10592.
    • (2004) J. Biol. Chem , vol.279 , pp. 10584-10592
    • Boesen, T.1    Mohammad, S.S.2    Pavitt, G.D.3    Andersen, G.R.4
  • 10
    • 0033179296 scopus 로고    scopus 로고
    • GEFs: Structural basis for their activation of small GTP-binding proteins
    • Cherfils, J., and P. Chardin. 1999. GEFs: structural basis for their activation of small GTP-binding proteins. Trends Biochem. Sci. 24:306-311.
    • (1999) Trends Biochem. Sci , vol.24 , pp. 306-311
    • Cherfils, J.1    Chardin, P.2
  • 11
    • 0025853453 scopus 로고
    • Complex formation by positive and negative translational regulators of GCN4
    • Cigan, A. M., M. Foiani, E. M. Hannig, and A. G. Hinnebusch. 1991. Complex formation by positive and negative translational regulators of GCN4. Mol. Cell. Biol. 11:3217-3228.
    • (1991) Mol. Cell. Biol , vol.11 , pp. 3217-3228
    • Cigan, A.M.1    Foiani, M.2    Hannig, E.M.3    Hinnebusch, A.G.4
  • 12
    • 0030907057 scopus 로고    scopus 로고
    • Using GCN4 as a reporter of eIF2α phosphorylation and translational regulation in yeast
    • Dever, T. E. 1997. Using GCN4 as a reporter of eIF2α phosphorylation and translational regulation in yeast. Methods 11:403-417.
    • (1997) Methods , vol.11 , pp. 403-417
    • Dever, T.E.1
  • 15
    • 0029022224 scopus 로고
    • Mutations in GCD11, the structural gene for eIF-2 gamma in yeast, alter translational regulation of GCN4 and the selection of the start site for protein synthesis
    • Dorris, D. R., F. L. Erickson, and E. M. Hannig. 1995. Mutations in GCD11, the structural gene for eIF-2 gamma in yeast, alter translational regulation of GCN4 and the selection of the start site for protein synthesis. EMBO J. 14:2239-2249.
    • (1995) EMBO J , vol.14 , pp. 2239-2249
    • Dorris, D.R.1    Erickson, F.L.2    Hannig, E.M.3
  • 16
    • 0029858531 scopus 로고    scopus 로고
    • Ligand interactions with eukaryotic translation initiation factor 2: Role of the γ-subunit
    • Erickson, F. L., and E. M. Hannig. 1996. Ligand interactions with eukaryotic translation initiation factor 2: role of the γ-subunit. EMBO J. 15:6311-6320.
    • (1996) EMBO J , vol.15 , pp. 6311-6320
    • Erickson, F.L.1    Hannig, E.M.2
  • 17
    • 0035004387 scopus 로고    scopus 로고
    • Minimum requirements for the function of eukaryotic translation initiation factor 2
    • Erickson, F. L., J. Nika, S. Rippel, and E. M. Hannig. 2001. Minimum requirements for the function of eukaryotic translation initiation factor 2. Genetics 158:123-132.
    • (2001) Genetics , vol.158 , pp. 123-132
    • Erickson, F.L.1    Nika, J.2    Rippel, S.3    Hannig, E.M.4
  • 18
    • 32544438040 scopus 로고    scopus 로고
    • The large spectrum of eIF2B-related diseases
    • Fogli, A., and O. Boespflug-Tanguy. 2006. The large spectrum of eIF2B-related diseases. Biochem. Soc. Trans. 34:22-29.
    • (2006) Biochem. Soc. Trans , vol.34 , pp. 22-29
    • Fogli, A.1    Boespflug-Tanguy, O.2
  • 20
    • 5044229348 scopus 로고    scopus 로고
    • Molecular mechanisms of translational control
    • Gebauer, F., and M. W. Hentze. 2004. Molecular mechanisms of translational control. Nat. Rev. Mol. Cell Biol. 5:827-835.
    • (2004) Nat. Rev. Mol. Cell Biol , vol.5 , pp. 827-835
    • Gebauer, F.1    Hentze, M.W.2
  • 21
    • 0036790688 scopus 로고    scopus 로고
    • Characterization of the minimal catalytic domain within eIF2B: The guanine-nucleotide exchange factor for translation initiation
    • Gomez, E., S. S. Mohammad, and G. D. Pavitt. 2002. Characterization of the minimal catalytic domain within eIF2B: the guanine-nucleotide exchange factor for translation initiation. EMBO J. 21:5292-5301.
    • (2002) EMBO J , vol.21 , pp. 5292-5301
    • Gomez, E.1    Mohammad, S.S.2    Pavitt, G.D.3
  • 22
    • 0034024628 scopus 로고    scopus 로고
    • Identification of domains and residues within the ε subunit of eukaryotic translation initiation factor 2B (eIF2Bε) required for guanine nucleotide exchange reveals a novel activation function promoted by eIF2B complex formation
    • Gomez, E., and G. D. Pavitt. 2000. Identification of domains and residues within the ε subunit of eukaryotic translation initiation factor 2B (eIF2Bε) required for guanine nucleotide exchange reveals a novel activation function promoted by eIF2B complex formation. Mol. Cell. Biol. 20:3965-3976.
    • (2000) Mol. Cell. Biol , vol.20 , pp. 3965-3976
    • Gomez, E.1    Pavitt, G.D.2
  • 23
    • 27144510561 scopus 로고    scopus 로고
    • Translational regulation of GCN4 and the general amino acid control of yeast
    • Hinnebusch, A. G. 2005. Translational regulation of GCN4 and the general amino acid control of yeast. Annu. Rev. Microbiol. 59:407-450.
    • (2005) Annu. Rev. Microbiol , vol.59 , pp. 407-450
    • Hinnebusch, A.G.1
  • 24
    • 0030886675 scopus 로고    scopus 로고
    • GTP hydrolysis controls stringent selection of the AUG start codon during translation initiation in Saccharomyces cerevisiae
    • Huang, H. K., H. Yoon, E. M. Hannig, and T. F. Donahue. 1997. GTP hydrolysis controls stringent selection of the AUG start codon during translation initiation in Saccharomyces cerevisiae. Genes Dev. 11:2396-2413.
    • (1997) Genes Dev , vol.11 , pp. 2396-2413
    • Huang, H.K.1    Yoon, H.2    Hannig, E.M.3    Donahue, T.F.4
  • 25
    • 33646068185 scopus 로고    scopus 로고
    • Heightened stress response in primary fibroblasts expressing mutant eIF2B genes from CACH/VWM leukodystrophy patients
    • Kantor, L., H. P. Harding, D. Ron, R. Schiffmann, C. R. Kaneski, S. R. Kimball, and O. Elroy-Stein. 2005. Heightened stress response in primary fibroblasts expressing mutant eIF2B genes from CACH/VWM leukodystrophy patients. Hum. Genet. 118:99-106.
    • (2005) Hum. Genet , vol.118 , pp. 99-106
    • Kantor, L.1    Harding, H.P.2    Ron, D.3    Schiffmann, R.4    Kaneski, C.R.5    Kimball, S.R.6    Elroy-Stein, O.7
  • 26
    • 0030025671 scopus 로고    scopus 로고
    • The structure of the Escherichia coli EF-Tu EF-Ts complex at 2.5A resolution
    • Kawashima, T., C. Berthet-Colominas, M. Wulff, S. Cusack, and R. Leberman. 1996. The structure of the Escherichia coli EF-Tu EF-Ts complex at 2.5A resolution. Nature 379:511-518.
    • (1996) Nature , vol.379 , pp. 511-518
    • Kawashima, T.1    Berthet-Colominas, C.2    Wulff, M.3    Cusack, S.4    Leberman, R.5
  • 27
    • 34447515801 scopus 로고    scopus 로고
    • Purification of FLAG-tagged eukaryotic initiation factor 2B complexes, sub-complexes and fragments from Saccharomyces cerevisiae
    • in press
    • Mohammad-Qureshi, S. S., R. Haddad, K. S. Palmer, J. P. Richardson, E. Gomez, and G. D. Pavitt. Purification of FLAG-tagged eukaryotic initiation factor 2B complexes, sub-complexes and fragments from Saccharomyces cerevisiae. Methods Enzymol., in press.
    • Methods Enzymol
    • Mohammad-Qureshi, S.S.1    Haddad, R.2    Palmer, K.S.3    Richardson, J.P.4    Gomez, E.5    Pavitt, G.D.6
  • 28
    • 28844478867 scopus 로고    scopus 로고
    • eIF2B, a mediator of general and gene-specific translational control
    • Pavitt, G. D. 2005. eIF2B, a mediator of general and gene-specific translational control. Biochem. Soc. Trans. 33:1487-1492.
    • (2005) Biochem. Soc. Trans , vol.33 , pp. 1487-1492
    • Pavitt, G.D.1
  • 29
    • 0028926048 scopus 로고
    • Protein-protein interactions: Methods for detection and analysis
    • Phizicky, E. M., and S. Fields. 1995. Protein-protein interactions: methods for detection and analysis. Microbiol. Rev. 59:94-123.
    • (1995) Microbiol. Rev , vol.59 , pp. 94-123
    • Phizicky, E.M.1    Fields, S.2
  • 30
    • 0346243924 scopus 로고    scopus 로고
    • Structural snapshots of the mechanism and inhibition of a guanine nucleotide exchange factor
    • Renault, L., B. Guibert, and J. Cherfils. 2003. Structural snapshots of the mechanism and inhibition of a guanine nucleotide exchange factor. Nature 426:525-530.
    • (2003) Nature , vol.426 , pp. 525-530
    • Renault, L.1    Guibert, B.2    Cherfils, J.3
  • 31
    • 1542344340 scopus 로고    scopus 로고
    • Mutations causing childhood ataxia with central nervous system hypomyelination reduce eukaryotic initiation factor 2B complex formation and activity
    • Richardson, J. P., S. S. Mohammad, and G. D. Pavitt. 2004. Mutations causing childhood ataxia with central nervous system hypomyelination reduce eukaryotic initiation factor 2B complex formation and activity. Mol. Cell. Biol. 24:2352-2363.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 2352-2363
    • Richardson, J.P.1    Mohammad, S.S.2    Pavitt, G.D.3
  • 32
    • 1642304746 scopus 로고    scopus 로고
    • X-ray structure of translation initiation factor eIF2γ: Implications for tRNA and eIF2α binding
    • Roll-Mecak, A., P. Alone, C. Cao, T. E. Dever, and S. K. Burley. 2004. X-ray structure of translation initiation factor eIF2γ: implications for tRNA and eIF2α binding. J. Biol. Chem. 279:10634-10642.
    • (2004) J. Biol. Chem , vol.279 , pp. 10634-10642
    • Roll-Mecak, A.1    Alone, P.2    Cao, C.3    Dever, T.E.4    Burley, S.K.5
  • 33
    • 33749340583 scopus 로고    scopus 로고
    • An eIF5/eIF2 complex antagonizes guanine nucleotide exchange by eIF2B during translation initiation
    • Singh, C. R., B. Lee, T. Udagawa, S. S. Mohammad-Qureshi, Y. Yamamoto, G. D. Pavitt, and K. Asano. 2006. An eIF5/eIF2 complex antagonizes guanine nucleotide exchange by eIF2B during translation initiation. EMBO J. 25:4537-4546.
    • (2006) EMBO J , vol.25 , pp. 4537-4546
    • Singh, C.R.1    Lee, B.2    Udagawa, T.3    Mohammad-Qureshi, S.S.4    Yamamoto, Y.5    Pavitt, G.D.6    Asano, K.7
  • 34
    • 33748350921 scopus 로고    scopus 로고
    • Structure of archaeal translational initiation factor 2βγ-GDP reveals significant conformational change of the β-subunit and switch 1 region
    • Sokabe, M., M. Yao, N. Sakai, S. Toya, and I. Tanaka. 2006. Structure of archaeal translational initiation factor 2βγ-GDP reveals significant conformational change of the β-subunit and switch 1 region. Proc. Natl. Acad. Sci. USA 103:13016-13021.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 13016-13021
    • Sokabe, M.1    Yao, M.2    Sakai, N.3    Toya, S.4    Tanaka, I.5
  • 35
    • 0032538347 scopus 로고    scopus 로고
    • Invasion of the nucleotide snatchers: Structural insights into the mechanism of G protein GEFs
    • Sprang, S. R., and D. E. Coleman. 1998. Invasion of the nucleotide snatchers: structural insights into the mechanism of G protein GEFs. Cell 95:155-158.
    • (1998) Cell , vol.95 , pp. 155-158
    • Sprang, S.R.1    Coleman, D.E.2
  • 36
    • 33846027894 scopus 로고    scopus 로고
    • Structural evidence for a common intermediate in small G protein-GEF reactions
    • Thomas, C., I. Fricke, A. Scrima, A. Berken, and A. Wittinghofer. 2007. Structural evidence for a common intermediate in small G protein-GEF reactions. Mol. Cell 25:141-149.
    • (2007) Mol. Cell , vol.25 , pp. 141-149
    • Thomas, C.1    Fricke, I.2    Scrima, A.3    Berken, A.4    Wittinghofer, A.5
  • 37
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson, J. D., T. J. Gibson, F. Plewniak, F. Jeanmougin, and D. G. Higgins. 1997. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25:4876-4882.
    • (1997) Nucleic Acids Res , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 40
    • 33646173651 scopus 로고    scopus 로고
    • Crystal structure of the C-terminal domain of S. cerevisiae eIF5
    • Wei, Z., Y. Xue, H. Xu, and W. Gong. 2006. Crystal structure of the C-terminal domain of S. cerevisiae eIF5. J. Mol. Biol. 359:1-9.
    • (2006) J. Mol. Biol , vol.359 , pp. 1-9
    • Wei, Z.1    Xue, Y.2    Xu, H.3    Gong, W.4
  • 41
    • 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 86:4579-4583.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 4579-4583
    • Wek, R.C.1    Jackson, B.M.2    Hinnebusch, A.G.3
  • 42
    • 0025330827 scopus 로고
    • Identification of positive-acting domains in GCN2 protein kinase required for translational activation of GCN4 expression
    • Wek, R. C., M. Ramirez, B. M. Jackson, and A. G. Hinnebusch. 1990. Identification of positive-acting domains in GCN2 protein kinase required for translational activation of GCN4 expression. Mol. Cell. Biol. 10:2820-2831.
    • (1990) Mol. Cell. Biol , vol.10 , pp. 2820-2831
    • Wek, R.C.1    Ramirez, M.2    Jackson, B.M.3    Hinnebusch, A.G.4
  • 43
    • 28044445673 scopus 로고    scopus 로고
    • The eukaryotic initiation factor (eIF) 5 HEAT domain mediates multifactor assembly and scanning with distinct interfaces to eIF1, eIF2, eIF3, and eIF4G
    • Yamamoto, Y., C. R. Singh, A. Marintchev, N. S. Hall, E. M. Hannig, G. Wagner, and K. Asano. 2005. The eukaryotic initiation factor (eIF) 5 HEAT domain mediates multifactor assembly and scanning with distinct interfaces to eIF1, eIF2, eIF3, and eIF4G. Proc. Natl. Acad. Sci. USA 102:16164-16169.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 16164-16169
    • Yamamoto, Y.1    Singh, C.R.2    Marintchev, A.3    Hall, N.S.4    Hannig, E.M.5    Wagner, G.6    Asano, K.7
  • 44
    • 33644790001 scopus 로고    scopus 로고
    • Structural switch of the γ subunit in an archaeal aIF2 αγ heterodimer
    • Yatime, L., Y. Mechulam, S. Blanquet, and E. Schmitt. 2006. Structural switch of the γ subunit in an archaeal aIF2 αγ heterodimer. Structure 14:119-128.
    • (2006) Structure , vol.14 , pp. 119-128
    • Yatime, L.1    Mechulam, Y.2    Blanquet, S.3    Schmitt, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.