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Volumn 423, Issue 3, 2012, Pages 515-519

The binding mechanism of eIF2β with its partner proteins, eIF5 and eIF2Bε

Author keywords

EIF2; EIF2B; EIF5; Intrinsically disordered domain; Translation initiation

Indexed keywords

INITIATION FACTOR 2; INITIATION FACTOR 2BEPSILON; INITIATION FACTOR 2BETA; INITIATION FACTOR 5; UNCLASSIFIED DRUG;

EID: 84863304649     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2012.05.155     Document Type: Article
Times cited : (3)

References (36)
  • 1
    • 75749088029 scopus 로고    scopus 로고
    • Origins and evolution of the mechanisms regulating translation initiation in eukaryotes
    • Hernandez G., Altmann M., Lasko P. Origins and evolution of the mechanisms regulating translation initiation in eukaryotes. Trends Biochem. Sci. 2009, 35:63-73.
    • (2009) Trends Biochem. Sci. , vol.35 , pp. 63-73
    • Hernandez, G.1    Altmann, M.2    Lasko, P.3
  • 2
    • 60149091189 scopus 로고    scopus 로고
    • Regulation of translation initiation in eukaryotes: mechanisms and biological targets
    • Sonenberg N., Hinnebusch A.G. Regulation of translation initiation in eukaryotes: mechanisms and biological targets. Cell 2009, 136:731-745.
    • (2009) Cell , vol.136 , pp. 731-745
    • Sonenberg, N.1    Hinnebusch, A.G.2
  • 4
    • 75149196287 scopus 로고    scopus 로고
    • The mechanism of eukaryotic translation initiation and principles of its regulation
    • Jackson R.J., Hellen C.U.T., Pestova T.V. The mechanism of eukaryotic translation initiation and principles of its regulation. Nat. Rev. Mol. Cell Biol. 2010, 11:113-127.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 113-127
    • Jackson, R.J.1    Hellen, C.U.T.2    Pestova, T.V.3
  • 5
    • 79954437206 scopus 로고    scopus 로고
    • Eukaryotic type translation initiation factor 2: structure-functional aspects
    • Stolboushkina E.A., Garber M.B. Eukaryotic type translation initiation factor 2: structure-functional aspects. Biochemistry (Moscow) 2011, 76:283-294.
    • (2011) Biochemistry (Moscow) , vol.76 , pp. 283-294
    • Stolboushkina, E.A.1    Garber, M.B.2
  • 6
    • 49349090915 scopus 로고    scopus 로고
    • Clues to the mechanism of action of eIF2B, the guanine-nucleotide-exchange factor for translation initiation
    • Mohammad-Qureshi S.S., Jennings M.D., Pavitt G.D. Clues to the mechanism of action of eIF2B, the guanine-nucleotide-exchange factor for translation initiation. Biochem. Soc. Trans. 2008, 36:658-664.
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 658-664
    • Mohammad-Qureshi, S.S.1    Jennings, M.D.2    Pavitt, G.D.3
  • 7
    • 0034307347 scopus 로고    scopus 로고
    • A multifactor complex of eukaryotic initiation factors, eIF1, eIF2, eIF3, eIF5, and initiator tRNA(Met) is an important translation initiation intermediate in vivo
    • Asano K., Clayton J., Shalev A., Hinnebusch A.G. A multifactor complex of eukaryotic initiation factors, eIF1, eIF2, eIF3, eIF5, and initiator tRNA(Met) is an important translation initiation intermediate in vivo. Genes Dev. 2000, 14:2534-2546.
    • (2000) Genes Dev. , vol.14 , pp. 2534-2546
    • Asano, K.1    Clayton, J.2    Shalev, A.3    Hinnebusch, A.G.4
  • 8
    • 0035191271 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factor 5 (elF5) acts as a classical GTPase-activator protein
    • Paulin F.E.M., Campbell L.E., O'Brien K., Loughlin J., Proud C.G. Eukaryotic translation initiation factor 5 (elF5) acts as a classical GTPase-activator protein. Curr. Biol. 2001, 11:55-59.
    • (2001) Curr. Biol. , vol.11 , pp. 55-59
    • Paulin, F.E.M.1    Campbell, L.E.2    O'Brien, K.3    Loughlin, J.4    Proud, C.G.5
  • 9
    • 0035846821 scopus 로고    scopus 로고
    • Biochemical analysis of the eIF2βγ complex reveals a structural function for eIF2α in catalyzed nucleotide exchange
    • Nika J., Rippel S., Hannig E.M. Biochemical analysis of the eIF2βγ complex reveals a structural function for eIF2α in catalyzed nucleotide exchange. J. Biol. Chem. 2001, 276:1051-1056.
    • (2001) J. Biol. Chem. , vol.276 , pp. 1051-1056
    • Nika, J.1    Rippel, S.2    Hannig, E.M.3
  • 10
    • 26944435515 scopus 로고    scopus 로고
    • Pi release from eIF2, not GTP hydrolysis, is the step controlled by start-site selection during eukaryotic translation initiation
    • Algire M.A., Maag D., Lorsch J.R. Pi release from eIF2, not GTP hydrolysis, is the step controlled by start-site selection during eukaryotic translation initiation. Mol. Cell 2005, 20:251-262.
    • (2005) Mol. Cell , vol.20 , pp. 251-262
    • Algire, M.A.1    Maag, D.2    Lorsch, J.R.3
  • 11
    • 10644249220 scopus 로고    scopus 로고
    • Release of initiation factors from 48S complexes during ribosomal subunit joining and the link between establishment of codon-anticodon base-pairing and hydrolysis of eIF2-bound GTP
    • Unbehaun A., Borukhov S.I., Hellen C.U.T., Pestova T.V. Release of initiation factors from 48S complexes during ribosomal subunit joining and the link between establishment of codon-anticodon base-pairing and hydrolysis of eIF2-bound GTP. Genes Dev. 2004, 18:3078-3093.
    • (2004) Genes Dev. , vol.18 , pp. 3078-3093
    • Unbehaun, A.1    Borukhov, S.I.2    Hellen, C.U.T.3    Pestova, T.V.4
  • 13
    • 34249699125 scopus 로고    scopus 로고
    • Change in nutritional status modulates the abundance of critical pre-initiation intermediate complexes during translation initiation in vivo
    • Singh C.R., Udagawa T., Lee B., Wassink S., He H., Yamamoto Y., Anderson J.T., Pavitt G.D., Asano K. Change in nutritional status modulates the abundance of critical pre-initiation intermediate complexes during translation initiation in vivo. J. Mol. Biol. 2007, 370:315-330.
    • (2007) J. Mol. Biol. , vol.370 , pp. 315-330
    • Singh, C.R.1    Udagawa, T.2    Lee, B.3    Wassink, S.4    He, H.5    Yamamoto, Y.6    Anderson, J.T.7    Pavitt, G.D.8    Asano, K.9
  • 14
    • 33749340583 scopus 로고    scopus 로고
    • An eIF5/eIF2 complex antagonizes guanine nucleotide exchange by eIF2B during translation initiation
    • Singh C.R., Lee B., Udagawa T., Mohammad-Qureshi S.S., Yamamoto Y., Pavitt G.D., Asano K. An eIF5/eIF2 complex antagonizes guanine nucleotide exchange by eIF2B during translation initiation. EMBO J. 2006, 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
  • 15
    • 0034065158 scopus 로고    scopus 로고
    • The structure and function of initiation factors in eukaryotic protein synthesis
    • Pestova T.V., Hellen C.U.T. The structure and function of initiation factors in eukaryotic protein synthesis. Cell. Mol. Life Sci. 2000, 57:651-674.
    • (2000) Cell. Mol. Life Sci. , vol.57 , pp. 651-674
    • Pestova, T.V.1    Hellen, C.U.T.2
  • 16
    • 38149140938 scopus 로고    scopus 로고
    • Eukaryotic initiation factor (eIF) 1 carries two distinct eIF5-binding faces important for multifactor assembly and AUG selection
    • Reibarkh M., Yamamoto Y., Singh C.R., del Rio F., Fahmy A., Lee B., Luna R.E., Ii M., Wagner G., Asano K. Eukaryotic initiation factor (eIF) 1 carries two distinct eIF5-binding faces important for multifactor assembly and AUG selection. J. Biol. Chem. 2008, 283:1094-1103.
    • (2008) J. Biol. Chem. , vol.283 , pp. 1094-1103
    • Reibarkh, M.1    Yamamoto, Y.2    Singh, C.R.3    del Rio, F.4    Fahmy, A.5    Lee, B.6    Luna, R.E.7    Ii, M.8    Wagner, G.9    Asano, K.10
  • 17
    • 0036846237 scopus 로고    scopus 로고
    • Direct eIF2-eIF3 contact in the multifactor complex is important for translation initiation in vivo
    • Valasek L., Nielsen K.H., Hinnebusch A.G. Direct eIF2-eIF3 contact in the multifactor complex is important for translation initiation in vivo. EMBO 2002, 21:5886-5898.
    • (2002) EMBO , vol.21 , pp. 5886-5898
    • Valasek, L.1    Nielsen, K.H.2    Hinnebusch, A.G.3
  • 18
    • 0033559265 scopus 로고    scopus 로고
    • Conserved bipartite motifs in yeast eIF5 and eIF2Be, 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., Hinnebusch A.G. Conserved bipartite motifs in yeast eIF5 and eIF2Be, GTPase-activating and GDP-GTP exchange factors in translation initiation, mediate binding to their common substrate eIF2. EMBO J. 1999, 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
  • 19
    • 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., Yao M., Sakai N., Toya S., Tanaka I. Structure of archaeal translational initiation factor 2βγ-GDP reveals significant conformational change of the β-subunit and switch 1 region. Proc. Natl. Acad. Sci. U. S. A. 2006, 103:13016-13021.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 13016-13021
    • Sokabe, M.1    Yao, M.2    Sakai, N.3    Toya, S.4    Tanaka, I.5
  • 20
    • 1342331856 scopus 로고    scopus 로고
    • Structure of the archaeal translation initiation factor aIF2β from methanobacterium thermoautotrophicum: implications for translation initiation
    • Gutierrez P., Osborne M.J., Siddiqui N., Trempe J.F., Arrowsmith C., Gehring K. Structure of the archaeal translation initiation factor aIF2β from methanobacterium thermoautotrophicum: implications for translation initiation. Protein Sci. 2004, 13:659-667.
    • (2004) Protein Sci. , vol.13 , pp. 659-667
    • Gutierrez, P.1    Osborne, M.J.2    Siddiqui, N.3    Trempe, J.F.4    Arrowsmith, C.5    Gehring, K.6
  • 21
    • 0032931764 scopus 로고    scopus 로고
    • The β subunit of eukaryotic translation initiation factor 2 binds mRNA through the lysine repeats and a region comprising the C-2-C-2 motif
    • Laurino J.P., Thompson G.M., Pacheco E., Castilho B.A. The β subunit of eukaryotic translation initiation factor 2 binds mRNA through the lysine repeats and a region comprising the C-2-C-2 motif. Mol. Cell. Biol. 1999, 19:173-181.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 173-181
    • Laurino, J.P.1    Thompson, G.M.2    Pacheco, E.3    Castilho, B.A.4
  • 22
    • 0031282976 scopus 로고    scopus 로고
    • Specific interaction of eukaryotic translation initiation factor 5 (eIF5) with the b subunit of eIF2
    • Das S., Maiti T., Das K., Maitra U. Specific interaction of eukaryotic translation initiation factor 5 (eIF5) with the b subunit of eIF2. J. Biol. Chem. 1997, 272:31712-31718.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31712-31718
    • Das, S.1    Maiti, T.2    Das, K.3    Maitra, U.4
  • 23
    • 33645677012 scopus 로고    scopus 로고
    • Structure of the eukaryotic initiation factor (eIF) 5 reveals a fold common to several translation factors
    • Conte M.R., Kelly G., Babon J., Sanfelice D., Youell J., Smerdon S.J., Proud C.G. Structure of the eukaryotic initiation factor (eIF) 5 reveals a fold common to several translation factors. Biochemistry 2006, 45:4550-4558.
    • (2006) Biochemistry , vol.45 , pp. 4550-4558
    • Conte, M.R.1    Kelly, G.2    Babon, J.3    Sanfelice, D.4    Youell, J.5    Smerdon, S.J.6    Proud, C.G.7
  • 24
    • 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 eIF2Bε
    • Alone P.V., Dever T.E. Direct binding of translation initiation factor eIF2γ-G domain to its GTPase- activating and GDP-GTP exchange factors eIF5 and eIF2Bε. J. Biol. Chem. 2006, 281:12636-12644.
    • (2006) J. Biol. Chem. , vol.281 , pp. 12636-12644
    • Alone, P.V.1    Dever, T.E.2
  • 25
    • 0029144599 scopus 로고
    • Multidomain organization of eukaryotic guanine nucleotide exchange translation initiation factor eIF2B subunits revealed by analysis of conserved sequence motifs
    • Koonin E.V. Multidomain organization of eukaryotic guanine nucleotide exchange translation initiation factor eIF2B subunits revealed by analysis of conserved sequence motifs. Protein Sci. 1995, 4:1608-1617.
    • (1995) Protein Sci. , vol.4 , pp. 1608-1617
    • Koonin, E.V.1
  • 26
    • 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., Mohammad S.S., Pavitt G.D., Andersen G.R. Structure of the catalytic fragment of translation initiation factor 2B and identification of a critically important catalytic residue. J. Biol. Chem. 2004, 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
  • 27
    • 33646173651 scopus 로고    scopus 로고
    • Crystal structure of the C-terminal domain of Scerevisiae eIF5
    • Wei Z., Xue Y., Xu H., Gong W. Crystal structure of the C-terminal domain of Scerevisiae eIF5. J. Mol. Biol. 2006, 359:1-9.
    • (2006) J. Mol. Biol. , vol.359 , pp. 1-9
    • Wei, Z.1    Xue, Y.2    Xu, H.3    Gong, W.4
  • 28
    • 44349189806 scopus 로고    scopus 로고
    • K2D2: estimation of protein secondary structure from circular dichroism spectra
    • Perez-Iratxeta C., Andrade-Navarro M.A. K2D2: estimation of protein secondary structure from circular dichroism spectra. BMC. Struct. Biol. 2008, 8:25.
    • (2008) BMC. Struct. Biol. , vol.8 , pp. 25
    • Perez-Iratxeta, C.1    Andrade-Navarro, M.A.2
  • 32
    • 0029185933 scopus 로고
    • CRYSOL - a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun D., Barberato C., Koch M.H.J. CRYSOL - a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Crystallogr. 1995, 28:768-773.
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.J.3
  • 33
    • 0029032691 scopus 로고
    • Structural characterization of the molten globule and native states of apomyoglobin by solution X-ray scattering
    • Kataoka M., Nishii I., Fujisawa T., Ueki T., Tokunaga F., Goto Y. Structural characterization of the molten globule and native states of apomyoglobin by solution X-ray scattering. J. Mol. Biol. 1995, 249:215-228.
    • (1995) J. Mol. Biol. , vol.249 , pp. 215-228
    • Kataoka, M.1    Nishii, I.2    Fujisawa, T.3    Ueki, T.4    Tokunaga, F.5    Goto, Y.6
  • 35
    • 77952734403 scopus 로고
    • EIF5 has GDI activity necessary for translational control by eIF2 phosphorylation
    • Jennings M.D., Pavitt G.D. EIF5 has GDI activity necessary for translational control by eIF2 phosphorylation. Nature 1982, 465:378-381.
    • (1982) Nature , vol.465 , pp. 378-381
    • Jennings, M.D.1    Pavitt, G.D.2
  • 36
    • 79952049228 scopus 로고    scopus 로고
    • EIF5 is a dual function GAP and GDI for eukaryotic translational control
    • Jennings M.D., Pavitt G.D. eIF5 is a dual function GAP and GDI for eukaryotic translational control. Small Gtpases 2011, 1:118-123.
    • (2011) Small Gtpases , vol.1 , pp. 118-123
    • Jennings, M.D.1    Pavitt, G.D.2


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