메뉴 건너뛰기




Volumn 319, Issue 3, 2004, Pages 725-732

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

Author keywords

Archaea; Crystal structure; Eukaryotic initiation factor 2B; Guanine nucleotide exchange factor; Pyrococcus horikoshii

Indexed keywords

ARCHAEAL INITIATION FACTOR 2B; ARCHAEAL PROTEIN; GUANINE NUCLEOTIDE EXCHANGE FACTOR; INITIATION FACTOR; ISOMERASE; RIBOSE 5 PHOSPHATE; UNCLASSIFIED DRUG;

EID: 2942592401     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.05.045     Document Type: Article
Times cited : (20)

References (33)
  • 1
    • 0030803256 scopus 로고    scopus 로고
    • Translational regulation of yeast GCN4. A window on factors that control initiator TRNA binding to the ribosome
    • Hinnebusch A.G. Translational regulation of yeast GCN4. A window on factors that control initiator TRNA binding to the ribosome. J. Biol. Chem. 272:1997;21661-21664
    • (1997) J. Biol. Chem. , vol.272 , pp. 21661-21664
    • Hinnebusch, A.G.1
  • 3
    • 0002352428 scopus 로고    scopus 로고
    • Protein kinases that phosphorylate eIF2 and eIF2B, their role in eukaryotic cell translational control
    • J.W.B. Hershey, M.B. Mathews, & N. Sonenberg. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Clemens M.J. Protein kinases that phosphorylate eIF2 and eIF2B, their role in eukaryotic cell translational control. Hershey J.W.B., Mathews M.B., Sonenberg N. Translational Control. 1996;139-172 Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • (1996) Translational Control , pp. 139-172
    • Clemens, M.J.1
  • 4
    • 0026718508 scopus 로고
    • Mechanism and regulation of eukaryotic protein synthesis
    • Merrick W.C. Mechanism and regulation of eukaryotic protein synthesis. Microbiol. Rev. 56:1992;291-315
    • (1992) Microbiol. Rev. , vol.56 , pp. 291-315
    • Merrick, W.C.1
  • 5
    • 0029968705 scopus 로고    scopus 로고
    • Initiation of protein synthesis in eukaryotic cells
    • Pain V.M. Initiation of protein synthesis in eukaryotic cells. Eur. J. Biochem. 236:1996;747-771
    • (1996) Eur. J. Biochem. , vol.236 , pp. 747-771
    • Pain, V.M.1
  • 6
    • 0027407751 scopus 로고
    • Regulation of eukaryotic protein synthesis by initiation factors
    • Rhoads R.E. Regulation of eukaryotic protein synthesis by initiation factors. J. Biol. Chem. 268:1993;3017-3029
    • (1993) J. Biol. Chem. , vol.268 , pp. 3017-3029
    • Rhoads, R.E.1
  • 7
    • 0033061571 scopus 로고    scopus 로고
    • Initiation of translation in prokaryotes and eukaryotes
    • Kozak M. Initiation of translation in prokaryotes and eukaryotes. Gene. 234:1999;187-208
    • (1999) Gene , vol.234 , pp. 187-208
    • Kozak, M.1
  • 8
    • 0028582139 scopus 로고
    • The guanine nucleotide exchange factor, eIF-2B
    • Price N., Proud C. The guanine nucleotide exchange factor, eIF-2B. Biochimie. 76:1994;748-760
    • (1994) Biochimie , vol.76 , pp. 748-760
    • Price, N.1    Proud, C.2
  • 9
    • 0027177312 scopus 로고
    • A protein complex of translational regulators of GCN4 mRNA is the guanine nucleotide-exchange factor for translation initiation factor 2 in yeast
    • Cigan A.M., Bushman J.L., Boal T.R., Hinnebusch A.G. A protein complex of translational regulators of GCN4 mRNA is the guanine nucleotide-exchange factor for translation initiation factor 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
  • 10
    • 0002470681 scopus 로고    scopus 로고
    • Mechanism and regulation of initiator methionyl-tRNA binding to ribosomes
    • N. Sonenberg, J.W.B. Hershey, & M.B. Mathews. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Hinnebusch A.G. Mechanism and regulation of initiator methionyl-tRNA binding to ribosomes. Sonenberg N., Hershey J.W.B., Mathews M.B. Translational Control of Gene Expression. 2000;185-243 Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • (2000) Translational Control of Gene Expression , pp. 185-243
    • Hinnebusch, A.G.1
  • 11
    • 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., 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
  • 12
    • 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., Yang W., 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.1    Yang, W.2    Hinnebusch, A.G.3
  • 13
    • 0034024628 scopus 로고    scopus 로고
    • Identification of domains and residues within three 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., Pavitt G.D. Identification of domains and residues within three subunit of eukaryotic translation initiation factor 2B (eIF2B. ε) required for guanine nucleotide exchange reveals a novel activation function promoted by eIF2B complex formation Mol. Cell. Biol. 20:2000;3965-3976
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 3965-3976
    • Gomez, E.1    Pavitt, G.D.2
  • 14
    • 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., 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
  • 16
  • 17
    • 0001271789 scopus 로고
    • Phylogenetic structure of the prokaryotic domain: The primary kingdoms
    • Woese C.R., Fox G.E. Phylogenetic structure of the prokaryotic domain: the primary kingdoms. Proc. Natl. Acad. Sci. USA. 74:1977;5088-5090
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 5088-5090
    • Woese, C.R.1    Fox, G.E.2
  • 19
    • 0031915895 scopus 로고    scopus 로고
    • Universally conserved translation initiation actors
    • Kyrpides N.C., Woese C.R. Universally conserved translation initiation actors. Proc. Natl. Acad. Sci. USA. 95:1998;224-228
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 224-228
    • Kyrpides, N.C.1    Woese, C.R.2
  • 20
    • 0032584201 scopus 로고    scopus 로고
    • Archaeal translation initiation revisited: The initiation factor 2 and eukaryotic initiation factor 2B α-β-δ subunit families
    • Kyrpides N.C., Woese C.R. Archaeal translation initiation revisited: the initiation factor 2 and eukaryotic initiation factor 2B. α-β-δ subunit families Proc. Natl. Acad. Sci. USA. 95:1998;3726-3730
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3726-3730
    • Kyrpides, N.C.1    Woese, C.R.2
  • 21
    • 0037007203 scopus 로고    scopus 로고
    • The large subunit of initiation factor aIF2 is a close structural homologue of elongation factors
    • Schmitt E., Blanquet S., Mechulam Y. The large subunit of initiation factor aIF2 is a close structural homologue of elongation factors. EMBO J. 21:2002;1821-1832
    • (2002) EMBO J. , vol.21 , pp. 1821-1832
    • Schmitt, E.1    Blanquet, S.2    Mechulam, Y.3
  • 22
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • C.W. Jr. Carter, & R.M. Sweet. New York: Academic Press
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Carter C.W. Jr., Sweet R.M. Methods in Enzymology 276: Macromolecular Crystallography, part A. 1997;307-326 Academic Press, New York
    • (1997) Methods in Enzymology 276: Macromolecular Crystallography, Part a , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 24
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis A., Morris R., Lamzin V.S. Automated protein model building combined with iterative structure refinement. Nat. Struct. Biol. 6:1999;458-463
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 25
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A. 47:1991;489-501
    • (1991) Acta Crystallogr. a , vol.47 , pp. 489-501
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 26
    • 0014432781 scopus 로고
    • Solvent contents of protein crystals
    • Matthews B.W. Solvent contents of protein crystals. J. Mol. Biol. 33:1968;491-497
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 28
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W., Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers. 22:1983;2577-2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 30
    • 0036278183 scopus 로고    scopus 로고
    • A hyperthermostable D-ribose-5-phosphate isomerase from Pyrococcus horikoshii. Characterization and three-dimensional structure
    • Ishikawa K., Matsui I., Payan F., Cambillau C., Ishida H., Kawarabayashi Y., Kikuchi H., Roussel A. A hyperthermostable D-ribose-5-phosphate isomerase from Pyrococcus horikoshii. Characterization and three-dimensional structure. Structure. 10:2002;877-886
    • (2002) Structure , vol.10 , pp. 877-886
    • Ishikawa, K.1    Matsui, I.2    Payan, F.3    Cambillau, C.4    Ishida, H.5    Kawarabayashi, Y.6    Kikuchi, H.7    Roussel, A.8
  • 32
    • 2442714840 scopus 로고    scopus 로고
    • In vitro phosphorylation of initiation factor 2α (aIF2α) from hyperthermophilic archaeon Pyrococcus horikoshii OT3
    • Tahara M., Ohsawa A., Saito S., Kimura M. In vitro phosphorylation of initiation factor 2α (aIF2. α) 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
  • 33
    • 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., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:1994;4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.