메뉴 건너뛰기




Volumn 33, Issue 10, 2014, Pages 1177-1191

EIF5B employs a novel domain release mechanism to catalyze ribosomal subunit joining

Author keywords

Crystal structure; GTPase; Molecular machines; Ribosome; Subunit joining; Translation initiation

Indexed keywords

GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATE; INITIATION FACTOR; INITIATION FACTOR E1F5B; NUCLEOTIDE; UNCLASSIFIED DRUG; EUKARYOTIC INITIATION FACTOR-5B;

EID: 84900845284     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1002/embj.201387344     Document Type: Article
Times cited : (43)

References (48)
  • 1
    • 0022434014 scopus 로고
    • Direct determination of the association constant between elongation factor Tu X GTP and aminoacyl-tRNA using fluorescence
    • Abrahamson JK, Laue TM, Miller DL, Johnson AE, (1985) Direct determination of the association constant between elongation factor Tu X GTP and aminoacyl-tRNA using fluorescence. Biochemistry 24: 692-700
    • (1985) Biochemistry , vol.24 , pp. 692-700
    • Abrahamson, J.K.1    Laue, T.M.2    Miller, D.L.3    Johnson, A.E.4
  • 4
    • 20444365142 scopus 로고    scopus 로고
    • The cryo-EM structure of a translation initiation complex from Escherichia coli
    • Allen GS, Zavialov A, Gursky R, Ehrenberg M, Frank J, (2005) The cryo-EM structure of a translation initiation complex from Escherichia coli. Cell 121: 703-712
    • (2005) Cell , vol.121 , pp. 703-712
    • Allen, G.S.1    Zavialov, A.2    Gursky, R.3    Ehrenberg, M.4    Frank, J.5
  • 5
    • 0142041880 scopus 로고    scopus 로고
    • The roles of initiation factor 2 and guanosine triphosphate in initiation of protein synthesis
    • Antoun A, Pavlov MY, Andersson K, Tenson T, Ehrenberg M, (2003) The roles of initiation factor 2 and guanosine triphosphate in initiation of protein synthesis. EMBO J 22: 5593-5601
    • (2003) EMBO J , vol.22 , pp. 5593-5601
    • Antoun, A.1    Pavlov, M.Y.2    Andersson, K.3    Tenson, T.4    Ehrenberg, M.5
  • 6
    • 33745763700 scopus 로고    scopus 로고
    • How initiation factors tune the rate of initiation of protein synthesis in bacteria
    • Antoun A, Pavlov MY, Lovmar M, Ehrenberg M, (2006) How initiation factors tune the rate of initiation of protein synthesis in bacteria. EMBO J 25: 2539-2550
    • (2006) EMBO J , vol.25 , pp. 2539-2550
    • Antoun, A.1    Pavlov, M.Y.2    Lovmar, M.3    Ehrenberg, M.4
  • 7
    • 2342547059 scopus 로고    scopus 로고
    • Ribosome formation from subunits studied by stopped-flow and Rayleigh light scattering
    • Antoun A, Pavlov MY, Tenson T, Ehrenberg MM, (2004) Ribosome formation from subunits studied by stopped-flow and Rayleigh light scattering. Biol Proced Online 6: 35-54
    • (2004) Biol Proced Online , vol.6 , pp. 35-54
    • Antoun, A.1    Pavlov, M.Y.2    Tenson, T.3    Ehrenberg, M.M.4
  • 10
    • 0026026818 scopus 로고
    • The GTPase superfamily: Conserved structure and molecular mechanism
    • Bourne HR, Sanders DA, McCormick F, (1991) The GTPase superfamily: conserved structure and molecular mechanism. Nature 349: 117-127
    • (1991) Nature , vol.349 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 11
    • 0025733433 scopus 로고
    • Stabilization of the Escherichia coli elongation factor Tu-GTP-aminoacyl-tRNA complex
    • Delaria K, Guillen M, Louie A, Jurnak F, (1991) Stabilization of the Escherichia coli elongation factor Tu-GTP-aminoacyl-tRNA complex. Arch Biochem Biophys 286: 207-211
    • (1991) Arch Biochem Biophys , vol.286 , pp. 207-211
    • Delaria, K.1    Guillen, M.2    Louie, A.3    Jurnak, F.4
  • 12
    • 0015500970 scopus 로고
    • Studies on the role of guanosine triphosphate in polypeptide chain initiation in Escherichia coli
    • Dubnoff JS, Lockwood AH, Maitra U, (1972) Studies on the role of guanosine triphosphate in polypeptide chain initiation in Escherichia coli. J Biol Chem 247: 2884-2894
    • (1972) J Biol Chem , vol.247 , pp. 2884-2894
    • Dubnoff, J.S.1    Lockwood, A.H.2    Maitra, U.3
  • 13
    • 84884645185 scopus 로고    scopus 로고
    • Initiation factor 2 crystal structure reveals a different domain organization from eukaryotic initiation factor 5B and mechanism among translational GTPases
    • Eiler D, Lin J, Simonetti A, Klaholz BP, Steitz TA, (2013) Initiation factor 2 crystal structure reveals a different domain organization from eukaryotic initiation factor 5B and mechanism among translational GTPases. Proc Natl Acad Sci USA 110: 15662-15667
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 15662-15667
    • Eiler, D.1    Lin, J.2    Simonetti, A.3    Klaholz, B.P.4    Steitz, T.A.5
  • 14
    • 0032573431 scopus 로고    scopus 로고
    • The stability of salt bridges at high temperatures: Implications for hyperthermophilic proteins
    • Elcock AH, (1998) The stability of salt bridges at high temperatures: implications for hyperthermophilic proteins. J Mol Biol 284: 489-502
    • (1998) J Mol Biol , vol.284 , pp. 489-502
    • Elcock, A.H.1
  • 18
    • 0036014793 scopus 로고    scopus 로고
    • Metal-ligand geometry relevant to proteins and in proteins: Sodium and potassium
    • Harding MM, (2002) Metal-ligand geometry relevant to proteins and in proteins: sodium and potassium. Acta Crystallogr D Biol Crystallogr 58: 872-874
    • (2002) Acta Crystallogr D Biol Crystallogr , vol.58 , pp. 872-874
    • Harding, M.M.1
  • 19
    • 50349097986 scopus 로고    scopus 로고
    • Cofactor dependent conformational switching of GTPases
    • Hauryliuk V, Hansson S, Ehrenberg M, (2008) Cofactor dependent conformational switching of GTPases. Biophys J 95: 1704-1715
    • (2008) Biophys J , vol.95 , pp. 1704-1715
    • Hauryliuk, V.1    Hansson, S.2    Ehrenberg, M.3
  • 20
    • 0028204490 scopus 로고
    • Do salt bridges stabilize proteins? A continuum electrostatic analysis
    • Hendsch ZS, Tidor B, (1994) Do salt bridges stabilize proteins? A continuum electrostatic analysis Protein Sci 3: 211-226
    • (1994) Protein Sci , vol.3 , pp. 211-226
    • Hendsch, Z.S.1    Tidor, B.2
  • 21
    • 0002522850 scopus 로고    scopus 로고
    • Garrett R.A. Douthwaite S.R. Liljas A. Matheson A.T. Moore P.B. Noller A.F. (eds), Washington, DC: American Society for Microbiology Press.
    • Hilgenfeld R, Mesters JR, Hogg T, (2000) The Ribosome: Structure, Function, Antibiotics, and Cellular Interactions., Garrett RA, Douthwaite SR, Liljas A, Matheson AT, Moore PB, Noller AF, (eds), Vol. 28, pp. 347-357. Washington, DC: American Society for Microbiology Press.
    • (2000) The Ribosome: Structure, Function, Antibiotics, and Cellular Interactions , vol.28 , pp. 347-357
    • Hilgenfeld, R.1    Mesters, J.R.2    Hogg, T.3
  • 24
    • 0037168583 scopus 로고    scopus 로고
    • Initiation factor eIF5B catalyzes second GTP-dependent step in eukaryotic translation initiation
    • Lee JH, Pestova TV, Shin BS, Cao C, Choi SK, Dever TE, (2002) Initiation factor eIF5B catalyzes second GTP-dependent step in eukaryotic translation initiation. Proc Natl Acad Sci USA 99: 16689-16694
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 16689-16694
    • Lee, J.H.1    Pestova, T.V.2    Shin, B.S.3    Cao, C.4    Choi, S.K.5    Dever, T.E.6
  • 25
    • 0022412615 scopus 로고
    • Kinetic studies of Escherichia coli elongation factor Tu-guanosine 5'-triphosphate-aminoacyl-tRNA complexes
    • Louie A, Jurnak F, (1985) Kinetic studies of Escherichia coli elongation factor Tu-guanosine 5'-triphosphate-aminoacyl-tRNA complexes. Biochemistry 24: 6433-6439
    • (1985) Biochemistry , vol.24 , pp. 6433-6439
    • Louie, A.1    Jurnak, F.2
  • 26
    • 25644436944 scopus 로고    scopus 로고
    • Translation initiation: Structures, mechanisms and evolution
    • Marintchev A, Wagner G, (2004) Translation initiation: structures, mechanisms and evolution. Q Rev Biophys 37: 197-284
    • (2004) Q Rev Biophys , vol.37 , pp. 197-284
    • Marintchev, A.1    Wagner, G.2
  • 28
    • 33748572261 scopus 로고    scopus 로고
    • Termination of translation in eukaryotes is mediated by the quaternary eRF1*eRF3*GTP*Mg2+ complex. The biological roles of eRF3 and prokaryotic RF3 are profoundly distinct
    • Mitkevich VA, Kononenko AV, Petrushanko IY, Yanvarev DV, Makarov AA, Kisselev LL, (2006) Termination of translation in eukaryotes is mediated by the quaternary eRF1*eRF3*GTP*Mg2+ complex. The biological roles of eRF3 and prokaryotic RF3 are profoundly distinct. Nucleic Acids Res 34: 3947-3954
    • (2006) Nucleic Acids Res , vol.34 , pp. 3947-3954
    • Mitkevich, V.A.1    Kononenko, A.V.2    Petrushanko, I.Y.3    Yanvarev, D.V.4    Makarov, A.A.5    Kisselev, L.L.6
  • 31
    • 78751632668 scopus 로고    scopus 로고
    • Activation of initiation factor 2 by ligands and mutations for rapid docking of ribosomal subunits
    • Pavlov MY, Zorzet A, Andersson DI, Ehrenberg M, (2011) Activation of initiation factor 2 by ligands and mutations for rapid docking of ribosomal subunits. EMBO J 30: 289-301
    • (2011) EMBO J , vol.30 , pp. 289-301
    • Pavlov, M.Y.1    Zorzet, A.2    Andersson, D.I.3    Ehrenberg, M.4
  • 32
    • 3543005385 scopus 로고    scopus 로고
    • Thermodynamics of protein-ligand interactions: History, presence, and future aspects
    • Perozzo R, Folkers G, Scapozza L, (2004) Thermodynamics of protein-ligand interactions: history, presence, and future aspects. J Recept Signal Transduct Res 24: 1-52
    • (2004) J Recept Signal Transduct Res , vol.24 , pp. 1-52
    • Perozzo, R.1    Folkers, G.2    Scapozza, L.3
  • 35
    • 0034703718 scopus 로고    scopus 로고
    • X-Ray structures of the universal translation initiation factor IF2/eIF5B: Conformational changes on GDP and GTP binding
    • Roll-Mecak A, Cao C, Dever TE, Burley SK, (2000) X-Ray structures of the universal translation initiation factor IF2/eIF5B: conformational changes on GDP and GTP binding. Cell 103: 781-792
    • (2000) Cell , vol.103 , pp. 781-792
    • Roll-Mecak, A.1    Cao, C.2    Dever, T.E.3    Burley, S.K.4
  • 37
    • 0021821218 scopus 로고
    • Kinetics and thermodynamics of the interaction of elongation factor Tu with elongation factor Ts, guanine nucleotides, and aminoacyl-tRNA
    • Romero G, Chau V, Biltonen RL, (1985) Kinetics and thermodynamics of the interaction of elongation factor Tu with elongation factor Ts, guanine nucleotides, and aminoacyl-tRNA. J Biol Chem 260: 6167-6174
    • (1985) J Biol Chem , vol.260 , pp. 6167-6174
    • Romero, G.1    Chau, V.2    Biltonen, R.L.3
  • 38
    • 33847224854 scopus 로고    scopus 로고
    • Intragenic suppressor mutations restore GTPase and translation functions of a eukaryotic initiation factor 5B switch II mutant
    • Shin BS, Acker MG, Maag D, Kim JR, Lorsch JR, Dever TE, (2007) Intragenic suppressor mutations restore GTPase and translation functions of a eukaryotic initiation factor 5B switch II mutant. Mol Cell Biol 27: 1677-1685
    • (2007) Mol Cell Biol , vol.27 , pp. 1677-1685
    • Shin, B.S.1    Acker, M.G.2    Maag, D.3    Kim, J.R.4    Lorsch, J.R.5    Dever, T.E.6
  • 39
    • 38449087681 scopus 로고    scopus 로고
    • Molecular genetic structure-function analysis of translation initiation factor eIF5B
    • Shin BS, Dever TE, (2007) Molecular genetic structure-function analysis of translation initiation factor eIF5B. Methods Enzymol 429: 185-201
    • (2007) Methods Enzymol , vol.429 , pp. 185-201
    • Shin, B.S.1    Dever, T.E.2
  • 40
    • 0037184985 scopus 로고    scopus 로고
    • Uncoupling of initiation factor eIF5B/IF2 GTPase and translational activities by mutations that lower ribosome affinity
    • Shin BS, Maag D, Roll-Mecak A, Arefin MS, Burley SK, Lorsch JR, Dever TE, (2002) Uncoupling of initiation factor eIF5B/IF2 GTPase and translational activities by mutations that lower ribosome affinity. Cell 111: 1015-1025
    • (2002) Cell , vol.111 , pp. 1015-1025
    • Shin, B.S.1    Maag, D.2    Roll-Mecak, A.3    Arefin, M.S.4    Burley, S.K.5    Lorsch, J.R.6    Dever, T.E.7
  • 44
    • 84879663355 scopus 로고    scopus 로고
    • Elongation factor G bound to the ribosome in an intermediate state of translocation
    • Tourigny DS, Fernandez IS, Kelley AC, Ramakrishnan V, (2013) Elongation factor G bound to the ribosome in an intermediate state of translocation. Science 340: 1235490
    • (2013) Science , vol.340 , pp. 1235490
    • Tourigny, D.S.1    Fernandez, I.S.2    Kelley, A.C.3    Ramakrishnan, V.4
  • 45
    • 34447302886 scopus 로고    scopus 로고
    • Position of eukaryotic initiation factor eIF5B on the 80S ribosome mapped by directed hydroxyl radical probing
    • Unbehaun A, Marintchev A, Lomakin IB, Didenko T, Wagner G, Hellen CU, Pestova TV, (2007) Position of eukaryotic initiation factor eIF5B on the 80S ribosome mapped by directed hydroxyl radical probing. EMBO J 26: 3109-3123
    • (2007) EMBO J , vol.26 , pp. 3109-3123
    • Unbehaun, A.1    Marintchev, A.2    Lomakin, I.B.3    Didenko, T.4    Wagner, G.5    Hellen, C.U.6    Pestova, T.V.7
  • 46
    • 0035834388 scopus 로고    scopus 로고
    • The guanine nucleotide-binding switch in three dimensions
    • Vetter IR, Wittinghofer A, (2001) The guanine nucleotide-binding switch in three dimensions. Science 294: 1299-1304
    • (2001) Science , vol.294 , pp. 1299-1304
    • Vetter, I.R.1    Wittinghofer, A.2
  • 47
    • 78149302861 scopus 로고    scopus 로고
    • The mechanism for activation of GTP hydrolysis on the ribosome
    • Voorhees RM, Schmeing TM, Kelley AC, Ramakrishnan V, (2010) The mechanism for activation of GTP hydrolysis on the ribosome. Science 330: 835-838
    • (2010) Science , vol.330 , pp. 835-838
    • Voorhees, R.M.1    Schmeing, T.M.2    Kelley, A.C.3    Ramakrishnan, V.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.