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Volumn 47, Issue 20, 2008, Pages 5590-5598

Solution structure of C-terminal Escherichia coli translation initiation factor IF2 by small-angle X-ray scattering

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; COMPUTER SOFTWARE; CRYSTAL STRUCTURE; PROTEINS; X RAY SCATTERING;

EID: 43949083746     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi8000598     Document Type: Article
Times cited : (8)

References (57)
  • 1
    • 0031915895 scopus 로고    scopus 로고
    • Universally conserved translation initiation factors
    • Kyrpides, N. C., and Woese, C. R. (1998) Universally conserved translation initiation factors. Proc. Natl. Acad. Sci. U.S.A. 95, 224-228.
    • (1998) Proc. Natl. Acad. Sci. U.S.A , vol.95 , pp. 224-228
    • Kyrpides, N.C.1    Woese, C.R.2
  • 2
    • 0037956259 scopus 로고    scopus 로고
    • Remarkable conservation of translation initiation factors: IF1/eIF1A and IF2/eIF5B are universally distributed phylogenetic markers
    • Sørensen, H. P., Hedegaard, J., Sperling-Petersen, H. U., and Mortensen, K. K. (2001) Remarkable conservation of translation initiation factors: IF1/eIF1A and IF2/eIF5B are universally distributed phylogenetic markers. IUBMB Life 51, 321-327.
    • (2001) IUBMB Life , vol.51 , pp. 321-327
    • Sørensen, H.P.1    Hedegaard, J.2    Sperling-Petersen, H.U.3    Mortensen, K.K.4
  • 3
    • 13044292050 scopus 로고    scopus 로고
    • Universal conservation in translation initiation revealed by human and archaeal homologs of bacterial translation initiation factor IF2
    • Lee, J. H., Choi, S. K., Roll-Mecak, A., Burley, S. K., and Dever, T. E. (1999) Universal conservation in translation initiation revealed by human and archaeal homologs of bacterial translation initiation factor IF2. Proc. Natl. Acad. Sci. U.S.A. 96, 4342-4347.
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 4342-4347
    • Lee, J.H.1    Choi, S.K.2    Roll-Mecak, A.3    Burley, S.K.4    Dever, T.E.5
  • 5
    • 0026331349 scopus 로고
    • Tandem translation of E. coli initiation factor IF2 β: Purification and characterization in vitro of two active forms
    • Nyengaard, N. R., Mortensen, K. K., Lassen, S. F., Hershey, J. W., and Sperling-Petersen, H. U. (1991) Tandem translation of E. coli initiation factor IF2 β: Purification and characterization in vitro of two active forms. Biochem. Biophys. Res. Commun. 181, 1572-1579.
    • (1991) Biochem. Biophys. Res. Commun , vol.181 , pp. 1572-1579
    • Nyengaard, N.R.1    Mortensen, K.K.2    Lassen, S.F.3    Hershey, J.W.4    Sperling-Petersen, H.U.5
  • 6
    • 0026485435 scopus 로고
    • Tandem translation of Bacillus subtilis initiation factor IF2 in E. coli. Over-expression of infBB.su in E. coli and purification of α- and β-forms of IF2B.su
    • Hubert, M., Nyengaard, N. R., Shazand, K., Mortensen, K. K., Lassen, S. F., Grunberg-Manago, M., and Sperling-Petersen, H. U. (1992) Tandem translation of Bacillus subtilis initiation factor IF2 in E. coli. Over-expression of infBB.su in E. coli and purification of α- and β-forms of IF2B.su. FEBS Lett. 312, 132-138.
    • (1992) FEBS Lett , vol.312 , pp. 132-138
    • Hubert, M.1    Nyengaard, N.R.2    Shazand, K.3    Mortensen, K.K.4    Lassen, S.F.5    Grunberg-Manago, M.6    Sperling-Petersen, H.U.7
  • 7
    • 1642580810 scopus 로고    scopus 로고
    • Preferential translation of cold-shock mRNAs during cold adaptation
    • Giuliodori, A. M., Brandi, A., Gualerzi, C. O., and Pon, C. L. (2004) Preferential translation of cold-shock mRNAs during cold adaptation. RNA 10, 265-276.
    • (2004) RNA 10 , pp. 265-276
    • Giuliodori, A.M.1    Brandi, A.2    Gualerzi, C.O.3    Pon, C.L.4
  • 8
    • 0034608861 scopus 로고    scopus 로고
    • Escherichia coli CspA-family RNA chaperones are transcription antiterminators
    • Bae, W., Xia, B., Inouye, M., and Severinov, K. (2000) Escherichia coli CspA-family RNA chaperones are transcription antiterminators. Proc. Natl. Acad. Sci. U.S.A. 97, 7784-7789.
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 7784-7789
    • Bae, W.1    Xia, B.2    Inouye, M.3    Severinov, K.4
  • 9
    • 0142041880 scopus 로고    scopus 로고
    • The roles of initiation factor 2 and guanosine triphosphate in initiation of protein synthesis
    • Antoun, A., Pavlov, M. Y., Andersson, K., Tenson, T., and 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
  • 10
    • 0014938066 scopus 로고
    • Interaction between guanosine derivatives and factors involved in the initiation of protein synthesis
    • Lelong, J. C., Grunberg-Manago, M., Dondon, J., Gros, D., and Gros, F. (1970) Interaction between guanosine derivatives and factors involved in the initiation of protein synthesis. Nature 226, 505-510.
    • (1970) Nature , vol.226 , pp. 505-510
    • Lelong, J.C.1    Grunberg-Manago, M.2    Dondon, J.3    Gros, D.4    Gros, F.5
  • 11
    • 0015445155 scopus 로고
    • Release of polypeptide chain initiation factor IF-2 during initiation complex formation
    • Lockwood, A. H., Sarkar, P., and Maitra, U. (1972) Release of polypeptide chain initiation factor IF-2 during initiation complex formation. Proc. Natl. Acad. Sci. U.S.A. 69, 3602-3605.
    • (1972) Proc. Natl. Acad. Sci. U.S.A , vol.69 , pp. 3602-3605
    • Lockwood, A.H.1    Sarkar, P.2    Maitra, U.3
  • 12
    • 0029913289 scopus 로고    scopus 로고
    • Late events in translation initiation. Adjustment of fMet-tRNA in the ribosomal P-site
    • La Teana, A., Pon, C. L., and Gualerzi, C. O. (1996) Late events in translation initiation. Adjustment of fMet-tRNA in the ribosomal P-site. J. Mol. Biol. 256, 667-675.
    • (1996) J. Mol. Biol , vol.256 , pp. 667-675
    • La Teana, A.1    Pon, C.L.2    Gualerzi, C.O.3
  • 13
    • 0028232085 scopus 로고
    • In vivo study of engineered G-domain mutants of Escherichia coli translation initiation factor IF2
    • Laalami, S., Timofeev, A. V., Putzer, H., Leautey, J., and Grunberg-Manago, M. (1994) In vivo study of engineered G-domain mutants of Escherichia coli translation initiation factor IF2. Mol. Microbiol. 11, 293-302.
    • (1994) Mol. Microbiol , vol.11 , pp. 293-302
    • Laalami, S.1    Timofeev, A.V.2    Putzer, H.3    Leautey, J.4    Grunberg-Manago, M.5
  • 16
    • 0033525871 scopus 로고    scopus 로고
    • In vitro study of two dominant inhibitory GTPase mutants of Escherichia coli translation initiation factor IF2. Direct evidence that GTP hydrolysis is necessary for factor recycling
    • Luchin, S., Putzer, H., Hershey, J. W., Cenatiempo, Y., Grunberg-Manago, M., and Laalami, S. (1999) In vitro study of two dominant inhibitory GTPase mutants of Escherichia coli translation initiation factor IF2. Direct evidence that GTP hydrolysis is necessary for factor recycling. J. Biol. Chem. 274, 6074-6079.
    • (1999) J. Biol. Chem , vol.274 , pp. 6074-6079
    • Luchin, S.1    Putzer, H.2    Hershey, J.W.3    Cenatiempo, Y.4    Grunberg-Manago, M.5    Laalami, S.6
  • 17
    • 0034903857 scopus 로고    scopus 로고
    • Initiation factor IF 2 binds to the α-sarcin loop and helix 89 of Escherichia coli 23S ribosomal RNA
    • La Teana, A.. Gualerzi, C. O., and Dahlberg, A. E. (2001) Initiation factor IF 2 binds to the α-sarcin loop and helix 89 of Escherichia coli 23S ribosomal RNA. RNA 7, 1173-1179.
    • (2001) RNA , vol.7 , pp. 1173-1179
    • La Teana, A.1    Gualerzi, C.O.2    Dahlberg, A.E.3
  • 19
    • 0033969301 scopus 로고    scopus 로고
    • Chaperone properties of bacterial elongation factor EF-G and initiation factor IF2
    • Caldas, T., Laalami, S., and Richarme, G. (2000) Chaperone properties of bacterial elongation factor EF-G and initiation factor IF2. J. Biol. Chem. 275, 855-860.
    • (2000) J. Biol. Chem , vol.275 , pp. 855-860
    • Caldas, T.1    Laalami, S.2    Richarme, G.3
  • 20
    • 0023186464 scopus 로고
    • Induction of proteins in response to low temperature in Escherichia coli
    • Jones, P. G., VanBogelen, R. A., and Neidhardt, F. C. (1987) Induction of proteins in response to low temperature in Escherichia coli. J. Bacteriol. 169, 2092-2095.
    • (1987) J. Bacteriol , vol.169 , pp. 2092-2095
    • Jones, P.G.1    VanBogelen, R.A.2    Neidhardt, F.C.3
  • 21
    • 0034254538 scopus 로고    scopus 로고
    • Selective stimulation of translation of leaderless mRNA by initiation factor 2: Evolutionary implications for translation
    • Grill, S., Gualerzi, C. O., Londei, P., and Blasi, U. (2000) Selective stimulation of translation of leaderless mRNA by initiation factor 2: Evolutionary implications for translation. EMBO J. 19, 4101-4110.
    • (2000) EMBO J , vol.19 , pp. 4101-4110
    • Grill, S.1    Gualerzi, C.O.2    Londei, P.3    Blasi, U.4
  • 22
    • 0035957756 scopus 로고    scopus 로고
    • Modulation of ribosomal recruitment to 5′-terminal start codons by translation initiation factors IF2 and IF3
    • Grill, S., Moll, I., Hasenohrl, D., Gualerzi, C. O., and Blasi, U. (2001) Modulation of ribosomal recruitment to 5′-terminal start codons by translation initiation factors IF2 and IF3. FEBS Lett. 495, 167-171.
    • (2001) FEBS Lett , vol.495 , pp. 167-171
    • Grill, S.1    Moll, I.2    Hasenohrl, D.3    Gualerzi, C.O.4    Blasi, U.5
  • 23
    • 0036198887 scopus 로고    scopus 로고
    • Leaderless mRNAs in bacteria: Surprises in ribosomal recruitment and translational control
    • Moll, I., Grill, S., Gualerzi, C. O., and Blasi, U. (2002) Leaderless mRNAs in bacteria: Surprises in ribosomal recruitment and translational control. Mol. Microbiol. 43, 239-246.
    • (2002) Mol. Microbiol , vol.43 , pp. 239-246
    • Moll, I.1    Grill, S.2    Gualerzi, C.O.3    Blasi, U.4
  • 24
    • 0032445375 scopus 로고    scopus 로고
    • A six-domain structural model for Escherichia coli translation initiation factor IF2. Characterisation of twelve surface epitopes
    • Mortensen, K. K., Kildsgaard, J., Moreno, J. M., Steffensen, S. A., Egebjerg, J., and Sperling-Petersen, H. U. (1998) A six-domain structural model for Escherichia coli translation initiation factor IF2. Characterisation of twelve surface epitopes. Biochem. Mol. Biol. Int. 46, 1027-1041.
    • (1998) Biochem. Mol. Biol. Int , vol.46 , pp. 1027-1041
    • Mortensen, K.K.1    Kildsgaard, J.2    Moreno, J.M.3    Steffensen, S.A.4    Egebjerg, J.5    Sperling-Petersen, H.U.6
  • 25
    • 0031449546 scopus 로고    scopus 로고
    • Steffensen, S. A., Poulsen, A. B., Mortensen, K. K., and Sperling-Petersen, H. U. (1997) E. coli translation initiation factor IF2 - An extremely conserved protein. Comparative sequence analysis of the infB gene in clinical isolates of E. coli. FEBS Lett. 419, 281-284.
    • Steffensen, S. A., Poulsen, A. B., Mortensen, K. K., and Sperling-Petersen, H. U. (1997) E. coli translation initiation factor IF2 - An extremely conserved protein. Comparative sequence analysis of the infB gene in clinical isolates of E. coli. FEBS Lett. 419, 281-284.
  • 26
    • 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, T. E., and Burley, S. K. (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
  • 27
    • 0346733331 scopus 로고    scopus 로고
    • The N-terminal domain (IF2N) of bacterial translation initiation factor IF2 is connected to the conserved C-terminal domains by a flexible linker
    • Laursen, B. S., Kjaergaard, A. C., Mortensen, K. K., Hoffman, D. W., and Sperling-Petersen, H. U. (2004) The N-terminal domain (IF2N) of bacterial translation initiation factor IF2 is connected to the conserved C-terminal domains by a flexible linker. Protein Sci. 13, 230-239.
    • (2004) Protein Sci , vol.13 , pp. 230-239
    • Laursen, B.S.1    Kjaergaard, A.C.2    Mortensen, K.K.3    Hoffman, D.W.4    Sperling-Petersen, H.U.5
  • 28
    • 0038182530 scopus 로고    scopus 로고
    • A conserved structural motif at the N-terminus of bacterial translation initiation factor IF2
    • Laursen, B. S., Mortensen, K. K., Sperling-Petersen, H. U., and Hoffman, D. W. (2003) A conserved structural motif at the N-terminus of bacterial translation initiation factor IF2. J. Biol. Chem. 278, 16320-16328.
    • (2003) J. Biol. Chem , vol.278 , pp. 16320-16328
    • Laursen, B.S.1    Mortensen, K.K.2    Sperling-Petersen, H.U.3    Hoffman, D.W.4
  • 29
    • 20444365142 scopus 로고    scopus 로고
    • The cryo-EM structure of a translation initiation complex from Escherichia coli
    • Allen, G. S., Zavialov, A., Gursky, R., Ehrenberg, M., and 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
  • 31
    • 0347911980 scopus 로고    scopus 로고
    • A favorable solubility partner for the recombinant expression of streptavidin
    • Sorensen, H. P., Sperling-Petersen, H. U., and Mortensen, K. K. (2003) A favorable solubility partner for the recombinant expression of streptavidin. Protein Expression Purif. 32, 252-259.
    • (2003) Protein Expression Purif , vol.32 , pp. 252-259
    • Sorensen, H.P.1    Sperling-Petersen, H.U.2    Mortensen, K.K.3
  • 33
    • 0029958571 scopus 로고    scopus 로고
    • The GTP binding motif: Variations on a theme
    • Kjeldgaard, M., Nyborg, J., and Clark, B. F. (1996) The GTP binding motif: Variations on a theme. FASEB J. 10, 1347-1368.
    • (1996) FASEB J , vol.10 , pp. 1347-1368
    • Kjeldgaard, M.1    Nyborg, J.2    Clark, B.F.3
  • 35
    • 0035834388 scopus 로고    scopus 로고
    • The guanine nucleotide-binding switch in three dimensions
    • Vetter, I. R., and 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
  • 36
    • 24344440731 scopus 로고    scopus 로고
    • Solution structure of the C1 -subdomain of Bacillus stearothermophilus translation initiation factor IF2
    • Wienk, H., Tomaselli, S., Bernard, C., Spurio, R., Picone, D., Gualerzi, C. O., and Boelens, R. (2005) Solution structure of the C1 -subdomain of Bacillus stearothermophilus translation initiation factor IF2. Protein Sci. 14, 2461-2468.
    • (2005) Protein Sci , vol.14 , pp. 2461-2468
    • Wienk, H.1    Tomaselli, S.2    Bernard, C.3    Spurio, R.4    Picone, D.5    Gualerzi, C.O.6    Boelens, R.7
  • 37
    • 0034678924 scopus 로고    scopus 로고
    • Structure of the fMet-tRNA(fMet)-binding domain of B. stearothermophilus initiation factor IF2
    • Meunier, S., Spurio, R., Czisch, M., Wechselberger, R., Guenneugues, M., Gualerzi, C. O., and Boelens, R. (2000) Structure of the fMet-tRNA(fMet)-binding domain of B. stearothermophilus initiation factor IF2. EMBO J. 19, 1918-1926.
    • (2000) EMBO J , vol.19 , pp. 1918-1926
    • Meunier, S.1    Spurio, R.2    Czisch, M.3    Wechselberger, R.4    Guenneugues, M.5    Gualerzi, C.O.6    Boelens, R.7
  • 38
    • 33846625924 scopus 로고    scopus 로고
    • Structural insights on the translation initiation complex: Ghosts of a universal initiation complex
    • Allen, G. S., and Frank, J. (2007) Structural insights on the translation initiation complex: Ghosts of a universal initiation complex. Mol. Microbiol. 63, 941-950.
    • (2007) Mol. Microbiol , vol.63 , pp. 941-950
    • Allen, G.S.1    Frank, J.2
  • 39
    • 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, I. B., Didenko, T., Wagner, G., Hellen, C. U., and Pestova, T. V. (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
  • 40
    • 3442880149 scopus 로고    scopus 로고
    • A flux- and background-optimized version of the NanoSTAR small-angle X-ray scattering camera for solution scattering
    • Pedersen, J. S. (2004) A flux- and background-optimized version of the NanoSTAR small-angle X-ray scattering camera for solution scattering. J. Appl. Crystallogr. 37, 369-380.
    • (2004) J. Appl. Crystallogr , vol.37 , pp. 369-380
    • Pedersen, J.S.1
  • 41
    • 0000897622 scopus 로고
    • A new method for the evaluation of small-angle scattering data
    • Glatter, O. (1977) A new method for the evaluation of small-angle scattering data. J. Appl. Crystallogr. 10, 415-421.
    • (1977) J. Appl. Crystallogr , vol.10 , pp. 415-421
    • Glatter, O.1
  • 42
    • 0028295752 scopus 로고
    • The aggregation behavior of zinc-free insulin studied by small-angle neutron scattering
    • Pedersen, J. S., Hansen, S., and Bauer, R. (1994) The aggregation behavior of zinc-free insulin studied by small-angle neutron scattering. Eur. Biophys. J. 22, 379-389.
    • (1994) Eur. Biophys. J , vol.22 , pp. 379-389
    • Pedersen, J.S.1    Hansen, S.2    Bauer, R.3
  • 44
    • 0242571958 scopus 로고    scopus 로고
    • Small-angle scattering studies of biological macromolecules in solution
    • Svergun, D. I., and Koch, M. H. J. (2003) Small-angle scattering studies of biological macromolecules in solution. Rep. Prog. Phys. 66, 1735-1782.
    • (2003) Rep. Prog. Phys , vol.66 , pp. 1735-1782
    • Svergun, D.I.1    Koch, M.H.J.2
  • 45
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • Volkov, V. V., and Svergun, D. I. (2003) Uniqueness of ab initio shape determination in small-angle scattering. J. Appl. Crystallogr. 36, 860-864.
    • (2003) J. Appl. Crystallogr , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 46
    • 23244455562 scopus 로고    scopus 로고
    • Global rigid body modeling of macromolecular complexes against small-angle scattering data
    • Petoukhov, M. V., and Svergun, D. I. (2005) Global rigid body modeling of macromolecular complexes against small-angle scattering data. Biophys. J. 89, 1237-1250.
    • (2005) Biophys. J , vol.89 , pp. 1237-1250
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 47
    • 0035124442 scopus 로고    scopus 로고
    • Automated matching of high- and low-resolution structural models
    • Kozin, M. B., and Svergun, D. I. (2001) Automated matching of high- and low-resolution structural models. J. Appl. Crystallogr. 34, 33-41.
    • (2001) J. Appl. Crystallogr , vol.34 , pp. 33-41
    • Kozin, M.B.1    Svergun, D.I.2
  • 48
    • 0029185933 scopus 로고
    • CRYSOL - A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun, D., Barberato, C., and Koch, M. H. J. (1995) CRYSOL - A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Crystallogr. 128, 768-773.
    • (1995) J. Appl. Crystallogr , vol.128 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.J.3
  • 49
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M., and Wuthrich, K. (1996) MOLMOL: A program for display and analysis of macromolecular structures. J. Mol. Graphics 14, 51-55, 29-32.
    • (1996) J. Mol. Graphics , vol.14 , Issue.51-55 , pp. 29-32
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 50
    • 0001229341 scopus 로고    scopus 로고
    • Calculation of hydrodynamic properties of globular proteins from their atomic-level structure
    • Garcia de la Torre, J., Huertas, M. L., and Carrasco, B. (2000) Calculation of hydrodynamic properties of globular proteins from their atomic-level structure. Biophys. J. 78, 719-730.
    • (2000) Biophys. J , vol.78 , pp. 719-730
    • Garcia de la Torre, J.1    Huertas, M.L.2    Carrasco, B.3
  • 51
    • 0032544922 scopus 로고    scopus 로고
    • Binding of Escherichia coli initiation factor IF2 to 30S ribosomal subunits: A functional role for the N-terminus of the factor
    • Moreno, J. M., Kildsgaard, J., Siwanowicz, I., Mortensen, K. K., and Sperling-Petersen, H. U. (1998) Binding of Escherichia coli initiation factor IF2 to 30S ribosomal subunits: A functional role for the N-terminus of the factor. Biochem. Biophys. Res. Commun. 252, 465-471.
    • (1998) Biochem. Biophys. Res. Commun , vol.252 , pp. 465-471
    • Moreno, J.M.1    Kildsgaard, J.2    Siwanowicz, I.3    Mortensen, K.K.4    Sperling-Petersen, H.U.5
  • 53
    • 0021109418 scopus 로고
    • Direct cross-links between initiation factors 1, 2, and 3 and ribosomal proteins promoted by 2-iminothiolane
    • Boileau, G., Butler, P., Hershey, J. W., and Traut, R. R. (1983) Direct cross-links between initiation factors 1, 2, and 3 and ribosomal proteins promoted by 2-iminothiolane. Biochemistry 22, 3162-3170.
    • (1983) Biochemistry , vol.22 , pp. 3162-3170
    • Boileau, G.1    Butler, P.2    Hershey, J.W.3    Traut, R.R.4
  • 54
    • 0037452587 scopus 로고    scopus 로고
    • Mapping the binding interface between human eukaryotic initiation factors IA and 5B: A new interaction between old partners
    • Marintchev, A., Kolupaeva, V. G., Pestova, T. V., and Wagner, G. (2003) Mapping the binding interface between human eukaryotic initiation factors IA and 5B: A new interaction between old partners. Proc. Natl. Acad. Sci. U.S.A. 100, 1535-1540.
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 1535-1540
    • Marintchev, A.1    Kolupaeva, V.G.2    Pestova, T.V.3    Wagner, G.4
  • 56
    • 0031026590 scopus 로고    scopus 로고
    • Effect of the amino acid attached to Escherichia coli initiator tRNA on its affinity for the initiation factor IF2 and on the IF2 dependence of its binding to the ribosome
    • Wu, X. Q., and RajBhandary, U. L. (1997) Effect of the amino acid attached to Escherichia coli initiator tRNA on its affinity for the initiation factor IF2 and on the IF2 dependence of its binding to the ribosome. J. Biol. Chem. 272, 1891-1895.
    • (1997) J. Biol. Chem , vol.272 , pp. 1891-1895
    • Wu, X.Q.1    RajBhandary, U.L.2
  • 57
    • 33748314478 scopus 로고    scopus 로고
    • Translation initiation factor IF2 interacts with the 30 S ribosomal subunit via two separate binding sites
    • Caserta, E., Tomsk, J., Spurio, R., La Teana, A., Pon, C. L., and Gualerzi, C. O. (2006) Translation initiation factor IF2 interacts with the 30 S ribosomal subunit via two separate binding sites. J. Mol. Biol. 362, 787-799.
    • (2006) J. Mol. Biol , vol.362 , pp. 787-799
    • Caserta, E.1    Tomsk, J.2    Spurio, R.3    La Teana, A.4    Pon, C.L.5    Gualerzi, C.O.6


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