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Volumn 21, Issue 9, 2014, Pages 817-824

EF-G catalyzes tRNA translocation by disrupting interactions between decoding center and codon-anticodon duplex

Author keywords

[No Author keywords available]

Indexed keywords

ELONGATION FACTOR G; TRANSFER RNA; ANTICODON; CODON; ESCHERICHIA COLI PROTEIN;

EID: 84921973570     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.2869     Document Type: Article
Times cited : (37)

References (63)
  • 2
    • 77957730420 scopus 로고    scopus 로고
    • The ribosome: Some hard facts about its structure and hot air about its evolution
    • Ramakrishnan, V. The ribosome: some hard facts about its structure and hot air about its evolution. Cold Spring Harb. Symp. Quant. Biol. 74, 25-33 (2009).
    • (2009) Cold Spring Harb. Symp. Quant. Biol. , vol.74 , pp. 25-33
    • Ramakrishnan, V.1
  • 3
    • 84870391656 scopus 로고    scopus 로고
    • Intermediate states during mRNA-tRNA translocation
    • Frank, J. Intermediate states during mRNA-tRNA translocation. Curr. Opin. Struct. Biol. 22, 778-785 (2012).
    • (2012) Curr. Opin. Struct. Biol. , vol.22 , pp. 778-785
    • Frank, J.1
  • 4
    • 0037159243 scopus 로고    scopus 로고
    • Coupling of GTP hydrolysis by elongation factor G to translocation and factor recycling on the ribosome
    • Katunin, V.I., Savelsbergh, A., Rodnina, M.V. & Wintermeyer, W. Coupling of GTP hydrolysis by elongation factor G to translocation and factor recycling on the ribosome. Biochemistry 41, 12806-12812 (2002).
    • (2002) Biochemistry , vol.41 , pp. 12806-12812
    • Katunin, V.I.1    Savelsbergh, A.2    Rodnina, M.V.3    Wintermeyer, W.4
  • 6
    • 70350602056 scopus 로고    scopus 로고
    • The structure of the ribosome with elongation factor G trapped in the posttranslocational state
    • Gao, Y.G. Et al. The structure of the ribosome with elongation factor G trapped in the posttranslocational state. Science 326, 694-699 (2009).
    • (2009) Science , vol.326 , pp. 694-699
    • Gao, Y.G.1
  • 7
    • 78649873931 scopus 로고    scopus 로고
    • Head swivel on the ribosome facilitates translocation by means of intra-subunit tRNA hybrid sites
    • Ratje, A.H. Et al. Head swivel on the ribosome facilitates translocation by means of intra-subunit tRNA hybrid sites. Nature 468, 713-716 (2010).
    • (2010) Nature , vol.468 , pp. 713-716
    • Ratje, A.H.1
  • 8
    • 79954596928 scopus 로고    scopus 로고
    • Molecular dynamics of EF-G during translocation
    • Li, W., Trabuco, L.G., Schulten, K. & Frank, J. Molecular dynamics of EF-G during translocation. Proteins 79, 1478-1486 (2011).
    • (2011) Proteins , vol.79 , pp. 1478-1486
    • Li, W.1    Trabuco, L.G.2    Schulten, K.3    Frank, J.4
  • 9
    • 84879663355 scopus 로고    scopus 로고
    • Elongation factor G bound to the ribosome in an intermediate state of translocation
    • Tourigny, D.S., Fernandez, I.S., Kelley, A.C. & Ramakrishnan, V. Elongation factor G bound to the ribosome in an intermediate state of translocation. Science 340, 1235490 (2013).
    • (2013) Science , vol.340 , pp. 1235490
    • Tourigny, D.S.1    Fernandez, I.S.2    Kelley, A.C.3    Ramakrishnan, V.4
  • 10
    • 84879625362 scopus 로고    scopus 로고
    • Crystal structures of EF-G-ribosome complexes trapped in intermediate states of translocation
    • Zhou, J., Lancaster, L., Donohue, J.P. & Noller, H.F. Crystal structures of EF-G-ribosome complexes trapped in intermediate states of translocation. Science 340, 1236086 (2013).
    • (2013) Science , vol.340 , pp. 1236086
    • Zhou, J.1    Lancaster, L.2    Donohue, J.P.3    Noller, H.F.4
  • 11
    • 84879661481 scopus 로고    scopus 로고
    • Control of ribosomal subunit rotation by elongation factor G
    • Pulk, A. & Cate, J.H. Control of ribosomal subunit rotation by elongation factor G. Science 340, 1235970 (2013).
    • (2013) Science , vol.340 , pp. 1235970
    • Pulk, A.1    Cate, J.H.2
  • 12
    • 84883672314 scopus 로고    scopus 로고
    • Structure of EF-G-ribosome complex in a pretranslocation state
    • Chen, Y., Feng, S., Kumar, V., Ero, R. & Gao, Y.G. Structure of EF-G-ribosome complex in a pretranslocation state. Nat. Struct. Mol. Biol. 20, 1077-1084 (2013).
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 1077-1084
    • Chen, Y.1    Feng, S.2    Kumar, V.3    Ero, R.4    Gao, Y.G.5
  • 13
    • 33750799914 scopus 로고    scopus 로고
    • The highly conserved LepA is a ribosomal elongation factor that back-translocates the ribosome
    • Qin, Y. Et al. The highly conserved LepA is a ribosomal elongation factor that back-translocates the ribosome. Cell 127, 721-733 (2006).
    • (2006) Cell , vol.127 , pp. 721-733
    • Qin, Y.1
  • 14
    • 77649273875 scopus 로고    scopus 로고
    • Interrupted catalysis: The EF4 (LepA) effect on back-translocation
    • Liu, H., Pan, D., Pech, M. & Cooperman, B.S. Interrupted catalysis: the EF4 (LepA) effect on back-translocation. J. Mol. Biol. 396, 1043-1052 (2010).
    • (2010) J. Mol. Biol. , vol.396 , pp. 1043-1052
    • Liu, H.1    Pan, D.2    Pech, M.3    Cooperman, B.S.4
  • 15
    • 80053651205 scopus 로고    scopus 로고
    • The conserved protein EF4 (LepA) modulates the elongation cycle of protein synthesis
    • Liu, H. Et al. The conserved protein EF4 (LepA) modulates the elongation cycle of protein synthesis. Proc. Natl. Acad. Sci. USA 108, 16223-16228 (2011).
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 16223-16228
    • Liu, H.1
  • 16
    • 84877744053 scopus 로고    scopus 로고
    • The paradox of elongation factor 4: Highly conserved, yet of no physiological significance?
    • Zhang, D. & Qin, Y. The paradox of elongation factor 4: highly conserved, yet of no physiological significance? Biochem. J. 452, 173-181 (2013).
    • (2013) Biochem. J. , vol.452 , pp. 173-181
    • Zhang, D.1    Qin, Y.2
  • 17
    • 0033046906 scopus 로고    scopus 로고
    • Domain IV of elongation factor G from Thermus thermophilus is strictly required for translocation
    • Martemyanov, K.A. & Gudkov, A.T. Domain IV of elongation factor G from Thermus thermophilus is strictly required for translocation. FEBS Lett. 452, 155-159 (1999).
    • (1999) FEBS Lett. , vol.452 , pp. 155-159
    • Martemyanov, K.A.1    Gudkov, A.T.2
  • 18
    • 0034697995 scopus 로고    scopus 로고
    • Role of domains 4 and 5 in elongation factor G functions on the ribosome
    • Savelsbergh, A., Matassova, N.B., Rodnina, M.V. & Wintermeyer, W. Role of domains 4 and 5 in elongation factor G functions on the ribosome. J. Mol. Biol. 300, 951-961 (2000).
    • (2000) J. Mol. Biol. , vol.300 , pp. 951-961
    • Savelsbergh, A.1    Matassova, N.B.2    Rodnina, M.V.3    Wintermeyer, W.4
  • 19
    • 0035805229 scopus 로고    scopus 로고
    • Recognition of cognate transfer RNA by the 30S ribosomal subunit
    • Ogle, J.M. Et al. Recognition of cognate transfer RNA by the 30S ribosomal subunit. Science 292, 897-902 (2001).
    • (2001) Science , vol.292 , pp. 897-902
    • Ogle, J.M.1
  • 20
    • 84859593945 scopus 로고    scopus 로고
    • A new understanding of the decoding principle on the ribosome
    • Demeshkina, N., Jenner, L., Westhof, E., Yusupov, M. & Yusupova, G. A new understanding of the decoding principle on the ribosome. Nature 484, 256-259 (2012).
    • (2012) Nature , vol.484 , pp. 256-259
    • Demeshkina, N.1    Jenner, L.2    Westhof, E.3    Yusupov, M.4    Yusupova, G.5
  • 21
    • 0034691576 scopus 로고    scopus 로고
    • A ratchet-like inter-subunit reorganization of the ribosome during translocation
    • Frank, J. & Agrawal, R.K. A ratchet-like inter-subunit reorganization of the ribosome during translocation. Nature 406, 318-322 (2000).
    • (2000) Nature , vol.406 , pp. 318-322
    • Frank, J.1    Agrawal, R.K.2
  • 23
    • 79955494464 scopus 로고    scopus 로고
    • Single-molecule fluorescence measurements of ribosomal translocation dynamics
    • Chen, C. Et al. Single-molecule fluorescence measurements of ribosomal translocation dynamics. Mol. Cell 42, 367-377 (2011).
    • (2011) Mol. Cell , vol.42 , pp. 367-377
    • Chen, C.1
  • 24
    • 84875116452 scopus 로고    scopus 로고
    • Crystal structure of 70S ribosome with both cognate tRNAs in the e and P sites representing an authentic elongation complex
    • Feng, S., Chen, Y. & Gao, Y.G. Crystal structure of 70S ribosome with both cognate tRNAs in the E and P sites representing an authentic elongation complex. PLoS ONE 8, e58829 (2013).
    • (2013) PLoS ONE , vol.8 , pp. e58829
    • Feng, S.1    Chen, Y.2    Gao, Y.G.3
  • 25
    • 84892669376 scopus 로고    scopus 로고
    • EF-G and EF4: Translocation and back-translocation on the bacterial ribosome
    • Yamamoto, H. Et al. EF-G and EF4: translocation and back-translocation on the bacterial ribosome. Nat. Rev. Microbiol. 12, 89-100 (2014).
    • (2014) Nat. Rev. Microbiol. , vol.12 , pp. 89-100
    • Yamamoto, H.1
  • 26
    • 68949204220 scopus 로고    scopus 로고
    • EF-G2mt is an exclusive recycling factor in mammalian mitochondrial protein synthesis
    • Tsuboi, M. Et al. EF-G2mt is an exclusive recycling factor in mammalian mitochondrial protein synthesis. Mol. Cell 35, 502-510 (2009).
    • (2009) Mol. Cell , vol.35 , pp. 502-510
    • Tsuboi, M.1
  • 27
    • 0035947076 scopus 로고    scopus 로고
    • Localization of the ribosomal protection protein Tet(O) on the ribosome and the mechanism of tetracycline resistance
    • Spahn, C.M. Et al. Localization of the ribosomal protection protein Tet(O) on the ribosome and the mechanism of tetracycline resistance. Mol. Cell 7, 1037-1045 (2001).
    • (2001) Mol. Cell , vol.7 , pp. 1037-1045
    • Spahn, C.M.1
  • 28
    • 0037450699 scopus 로고    scopus 로고
    • Mechanism of Tet(O)-mediated tetracycline resistance
    • Connell, S.R. Et al. Mechanism of Tet(O)-mediated tetracycline resistance. EMBO J. 22, 945-953 (2003).
    • (2003) EMBO J. , vol.22 , pp. 945-953
    • Connell, S.R.1
  • 29
    • 84867656705 scopus 로고    scopus 로고
    • Structural basis for TetM-mediated tetracycline resistance
    • Dönhöfer, A. Et al. Structural basis for TetM-mediated tetracycline resistance. Proc. Natl. Acad. Sci. USA 109, 16900-16905 (2012).
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 16900-16905
    • Dönhöfer, A.1
  • 30
    • 84874584155 scopus 로고    scopus 로고
    • Mechanism of tetracycline resistance by ribosomal protection protein Tet(O)
    • Li, W. Et al. Mechanism of tetracycline resistance by ribosomal protection protein Tet(O). Nat. Commun. 4, 1477 (2013).
    • (2013) Nat. Commun. , vol.4 , pp. 1477
    • Li, W.1
  • 31
    • 0017668860 scopus 로고
    • Regulation of ribosome production in Escherichia coli: Synthesis and stability of ribosomal RNA and of ribosomal protein messenger RNA at different growth rates
    • Gausing, K. Regulation of ribosome production in Escherichia coli: synthesis and stability of ribosomal RNA and of ribosomal protein messenger RNA at different growth rates. J. Mol. Biol. 115, 335-354 (1977).
    • (1977) J. Mol. Biol. , vol.115 , pp. 335-354
    • Gausing, K.1
  • 32
    • 51349114071 scopus 로고    scopus 로고
    • A new tRNA intermediate revealed on the ribosome during EF4-mediated back-translocation
    • Connell, S.R. Et al. A new tRNA intermediate revealed on the ribosome during EF4-mediated back-translocation. Nat. Struct. Mol. Biol. 15, 910-915 (2008).
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 910-915
    • Connell, S.R.1
  • 33
    • 0027980558 scopus 로고
    • The crystal structure of elongation factor G complexed with GDP, at 2.7 A resolution
    • Czworkowski, J., Wang, J., Seitz, T.A. & Moore, P.B. The crystal structure of elongation factor G complexed with GDP, at 2.7 A resolution. EMBO J. 13, 3661-3668 (1994).
    • (1994) EMBO J. , vol.13 , pp. 3661-3668
    • Czworkowski, J.1    Wang, J.2    Seitz, T.A.3    Moore, P.B.4
  • 34
    • 0025070318 scopus 로고
    • Binding of tRNA to the ribosomal A and P sites protects two distinct sets of nucleotides in the 16S rRNA
    • Moazed, D. & Noller, H.F. Binding of tRNA to the ribosomal A and P sites protects two distinct sets of nucleotides in the 16S rRNA. J. Mol. Biol. 211, 135-145 (1990).
    • (1990) J. Mol. Biol. , vol.211 , pp. 135-145
    • Moazed, D.1    Noller, H.F.2
  • 35
    • 34548339675 scopus 로고    scopus 로고
    • Elongation factor G stabilizes the hybrid-state conformation of the 70S ribosome
    • Spiegel, P.C., Ermolenko, D.N. & Noller, H.F. Elongation factor G stabilizes the hybrid-state conformation of the 70S ribosome. RNA 13, 1473-1482 (2007).
    • (2007) RNA , vol.13 , pp. 1473-1482
    • Spiegel, P.C.1    Ermolenko, D.N.2    Noller, H.F.3
  • 36
    • 84891369006 scopus 로고    scopus 로고
    • Visualization of two transfer RNAs trapped in transit during elongation factor G-mediated translocation
    • Ramrath, D.J. Et al. Visualization of two transfer RNAs trapped in transit during elongation factor G-mediated translocation. Proc. Natl. Acad. Sci. USA 110, 20964-20969 (2013).
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 20964-20969
    • Ramrath, D.J.1
  • 37
    • 84891354515 scopus 로고    scopus 로고
    • Structure of the ribosome with elongation factor G trapped in the pretranslocation state
    • Brilot, A.F., Korostelev, A.A., Ermolenko, D.N. & Grigorieff, N. Structure of the ribosome with elongation factor G trapped in the pretranslocation state. Proc. Natl. Acad. Sci. USA 110, 20994-20999 (2013).
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 20994-20999
    • Brilot, A.F.1    Korostelev, A.A.2    Ermolenko, D.N.3    Grigorieff, N.4
  • 38
    • 0035670662 scopus 로고    scopus 로고
    • Elongation factor G-induced structural change in helix 34 of 16S rRNA related to translocation on the ribosome
    • Matassova, A.B., Rodnina, M.V. & Wintermeyer, W. Elongation factor G-induced structural change in helix 34 of 16S rRNA related to translocation on the ribosome. RNA 7, 1879-1885 (2001).
    • (2001) RNA , vol.7 , pp. 1879-1885
    • Matassova, A.B.1    Rodnina, M.V.2    Wintermeyer, W.3
  • 39
    • 69249112231 scopus 로고    scopus 로고
    • Structures of the ribosome in intermediate states of ratcheting
    • Zhang, W., Dunkle, J.A. & Cate, J.H. Structures of the ribosome in intermediate states of ratcheting. Science 325, 1014-1017 (2009).
    • (2009) Science , vol.325 , pp. 1014-1017
    • Zhang, W.1    Dunkle, J.A.2    Cate, J.H.3
  • 40
    • 84870928681 scopus 로고    scopus 로고
    • Rotation of the head of the 30S ribosomal subunit during mRNA translocation
    • Guo, Z. & Noller, H.F. Rotation of the head of the 30S ribosomal subunit during mRNA translocation. Proc. Natl. Acad. Sci. USA 109, 20391-20394 (2012).
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 20391-20394
    • Guo, Z.1    Noller, H.F.2
  • 41
    • 84885183798 scopus 로고    scopus 로고
    • Steric complementarity in the decoding center is important for tRNA selection by the ribosome
    • Khade, P.K., Shi, X. & Joseph, S. Steric complementarity in the decoding center is important for tRNA selection by the ribosome. J. Mol. Biol. 425, 3778-3789 (2013).
    • (2013) J. Mol. Biol. , vol.425 , pp. 3778-3789
    • Khade, P.K.1    Shi, X.2    Joseph, S.3
  • 42
    • 0037184536 scopus 로고    scopus 로고
    • Selection of tRNA by the ribosome requires a transition from an open to a closed form
    • Ogle, J.M., Murphy, F.V., Tarry, M.J. & Ramakrishnan, V. Selection of tRNA by the ribosome requires a transition from an open to a closed form. Cell 111, 721-732 (2002).
    • (2002) Cell , vol.111 , pp. 721-732
    • Ogle, J.M.1    Murphy, F.V.2    Tarry, M.J.3    Ramakrishnan, V.4
  • 43
    • 79955020725 scopus 로고    scopus 로고
    • Structural insights into cognate versus near-cognate discrimination during decoding
    • Agirrezabala, X. Et al. Structural insights into cognate versus near-cognate discrimination during decoding. EMBO J. 30, 1497-1507 (2011).
    • (2011) EMBO J. , vol.30 , pp. 1497-1507
    • Agirrezabala, X.1
  • 44
    • 0032526979 scopus 로고    scopus 로고
    • EF-G-catalyzed translocation of anticodon stem-loop analogs of transfer RNA in the ribosome
    • Joseph, S. & Noller, H.F. EF-G-catalyzed translocation of anticodon stem-loop analogs of transfer RNA in the ribosome. EMBO J. 17, 3478-3483 (1998).
    • (1998) EMBO J. , vol.17 , pp. 3478-3483
    • Joseph, S.1    Noller, H.F.2
  • 45
    • 0036809730 scopus 로고    scopus 로고
    • Universally conserved interactions between the ribosome and the anticodon stem-loop of a site tRNA important for translocation
    • Phelps, S.S., Jerinic, O. & Joseph, S. Universally conserved interactions between the ribosome and the anticodon stem-loop of a site tRNA important for translocation. Mol. Cell 10, 799-807 (2002).
    • (2002) Mol. Cell , vol.10 , pp. 799-807
    • Phelps, S.S.1    Jerinic, O.2    Joseph, S.3
  • 46
    • 80555130939 scopus 로고    scopus 로고
    • Messenger RNA interactions in the decoding center control the rate of translocation
    • Khade, P.K. & Joseph, S. Messenger RNA interactions in the decoding center control the rate of translocation. Nat. Struct. Mol. Biol. 18, 1300-1302 (2011).
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 1300-1302
    • Khade, P.K.1    Joseph, S.2
  • 47
    • 53949119816 scopus 로고    scopus 로고
    • Precise alignment of peptidyl tRNA by the decoding center is essential for EF-G-dependent translocation
    • Garcia-Ortega, L., Stephen, J. & Joseph, S. Precise alignment of peptidyl tRNA by the decoding center is essential for EF-G-dependent translocation. Mol. Cell 32, 292-299 (2008).
    • (2008) Mol. Cell , vol.32 , pp. 292-299
    • Garcia-Ortega, L.1    Stephen, J.2    Joseph, S.3
  • 48
    • 27144439460 scopus 로고    scopus 로고
    • Contribution of 16S rRNA nucleotides forming the 30S subunit A and P sites to translation in Escherichia coli
    • Abdi, N.M. & Fredrick, K. Contribution of 16S rRNA nucleotides forming the 30S subunit A and P sites to translation in Escherichia coli. RNA 11, 1624-1632 (2005).
    • (2005) RNA , vol.11 , pp. 1624-1632
    • Abdi, N.M.1    Fredrick, K.2
  • 49
    • 0031028688 scopus 로고    scopus 로고
    • Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome
    • Rodnina, M.V., Savelsbergh, A., Katunin, V.I. & Wintermeyer, W. Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome. Nature 385, 37-41 (1997).
    • (1997) Nature , vol.385 , pp. 37-41
    • Rodnina, M.V.1    Savelsbergh, A.2    Katunin, V.I.3    Wintermeyer, W.4
  • 50
    • 67651178174 scopus 로고    scopus 로고
    • The ribosome as a conceying themal ratchet machine
    • Spirin, A.S. The ribosome as a conceying themal ratchet machine. J. Biol. Chem. 284, 21103-21119 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 21103-21119
    • Spirin, A.S.1
  • 51
    • 84870605357 scopus 로고    scopus 로고
    • Common chaperone activity in the G-domain of trGTPase protects L11-L12 interaction on the ribosome
    • Zhang, D. Et al. Common chaperone activity in the G-domain of trGTPase protects L11-L12 interaction on the ribosome. Nucleic Acids Res. 40, 10851-10865 (2012).
    • (2012) Nucleic Acids Res. , vol.40 , pp. 10851-10865
    • Zhang, D.1
  • 53
    • 84861314628 scopus 로고    scopus 로고
    • A conserved proline switch on the ribosome facilitates the recruitment and binding of trGTPases
    • Wang, L. Et al. A conserved proline switch on the ribosome facilitates the recruitment and binding of trGTPases. Nat. Struct. Mol. Biol. 19, 403-410 (2012).
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 403-410
    • Wang, L.1
  • 54
    • 17444373920 scopus 로고    scopus 로고
    • Structural insights into fusidic acid resistance and sensitivity in EF-G
    • Hansson, S., Singh, R., Gudkov, A.T., Liljas, A. & Logan, D.T. Structural insights into fusidic acid resistance and sensitivity in EF-G. J. Mol. Biol. 348, 939-949 (2005).
    • (2005) J. Mol. Biol. , vol.348 , pp. 939-949
    • Hansson, S.1    Singh, R.2    Gudkov, A.T.3    Liljas, A.4    Logan, D.T.5
  • 55
    • 0034006565 scopus 로고    scopus 로고
    • Extremely thermostable elongation factor G from Aquifex aeolicus: Cloning, expression, purification, and characterization in a heterologous translation system
    • Martemyanov, K.A., Liljas, A. & Gudkov, A.T. Extremely thermostable elongation factor G from Aquifex aeolicus: cloning, expression, purification, and characterization in a heterologous translation system. Protein Expr. Purif. 18, 257-261 (2000).
    • (2000) Protein Expr. Purif. , vol.18 , pp. 257-261
    • Martemyanov, K.A.1    Liljas, A.2    Gudkov, A.T.3
  • 56
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 57
    • 0027538548 scopus 로고
    • Structural changes accompanying memory storage
    • Bailey, C.H. & Kandel, E.R. Structural changes accompanying memory storage. Annu. Rev. Physiol. 55, 397-426 (1993).
    • (1993) Annu. Rev. Physiol. , vol.55 , pp. 397-426
    • Bailey, C.H.1    Kandel, E.R.2
  • 58
    • 0034602449 scopus 로고    scopus 로고
    • Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site
    • Laurberg, M. Et al. Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site. J. Mol. Biol. 303, 593-603 (2000).
    • (2000) J. Mol. Biol. , vol.303 , pp. 593-603
    • Laurberg, M.1
  • 59
    • 2542470615 scopus 로고    scopus 로고
    • The active site of the ribosome is composed of two layers of conserved nucleotides with distinct roles in peptide bond formation and peptide release
    • Youngman, E.M., Brunelle, J.L., Kochaniak, A.B. & Green, R. The active site of the ribosome is composed of two layers of conserved nucleotides with distinct roles in peptide bond formation and peptide release. Cell 117, 589-599 (2004).
    • (2004) Cell , vol.117 , pp. 589-599
    • Youngman, E.M.1    Brunelle, J.L.2    Kochaniak, A.B.3    Green, R.4
  • 60
    • 0029994962 scopus 로고    scopus 로고
    • Truncated elongation factor G lacking the G domain promotes translocation of the 3′ end but not of the anticodon domain of peptidyl-tRNA
    • Borowski, C., Rodnina, M.V. & Wintermeyer, W. Truncated elongation factor G lacking the G domain promotes translocation of the 3′ end but not of the anticodon domain of peptidyl-tRNA. Proc. Natl. Acad. Sci. USA 93, 4202-4206 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4202-4206
    • Borowski, C.1    Rodnina, M.V.2    Wintermeyer, W.3
  • 61
    • 23644434688 scopus 로고    scopus 로고
    • Measurement of internal movements within the 30 S ribosomal subunit using Forster resonance energy transfer
    • Hickerson, R., Majumdar, Z.K., Baucom, A., Clegg, R.M. & Noller, H.F. Measurement of internal movements within the 30 S ribosomal subunit using Forster resonance energy transfer. J. Mol. Biol. 354, 459-472 (2005).
    • (2005) J. Mol. Biol. , vol.354 , pp. 459-472
    • Hickerson, R.1    Majumdar, Z.K.2    Baucom, A.3    Clegg, R.M.4    Noller, H.F.5
  • 62
    • 0033642214 scopus 로고    scopus 로고
    • In vitro reconstitution of 30S ribosomal subunits using complete set of recombinant proteins
    • Culver, G.M. & Noller, H.F. In vitro reconstitution of 30S ribosomal subunits using complete set of recombinant proteins. Methods Enzymol. 318, 446-460 (2000).
    • (2000) Methods Enzymol. , vol.318 , pp. 446-460
    • Culver, G.M.1    Noller, H.F.2
  • 63
    • 84866872784 scopus 로고    scopus 로고
    • Direct observation of the uptake of outer membrane proteins by the periplasmic chaperone Skp
    • Lyu, Z.X., Shao, Q., Gao, Y.Q. & Zhao, X.S. Direct observation of the uptake of outer membrane proteins by the periplasmic chaperone Skp. PLoS ONE 7, e46068 (2012).
    • (2012) PLoS ONE , vol.7 , pp. e46068
    • Lyu, Z.X.1    Shao, Q.2    Gao, Y.Q.3    Zhao, X.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.