메뉴 건너뛰기




Volumn 337, Issue 1, 2004, Pages 15-30

Interactions of Translation Factor EF-G with the Bacterial Ribosome before and after mRNA Translocation

Author keywords

Elongation factor; Ribosomes; rRNA; Translation; Translocation

Indexed keywords

BACTERIAL PROTEIN; EDETIC ACID; FERRIC ION; GUANOSINE TRIPHOSPHATE; HYDROXYL RADICAL; MESSENGER RNA; NUCLEOTIDE; RIBOSOME RNA; TRANSLATION FACTOR EF G; UNCLASSIFIED DRUG; BACTERIAL RNA; ELONGATION FACTOR G; PROTEIN SUBUNIT; RNA 16S; RNA 23S;

EID: 1442326707     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.01.013     Document Type: Article
Times cited : (30)

References (50)
  • 2
    • 0035787732 scopus 로고    scopus 로고
    • Ratchet-like movements between the two ribosomal subunits: Their implications in elongation factor recognition and tRNA translocation
    • B. Stillman. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Frank J., Agrawal R.K. Ratchet-like movements between the two ribosomal subunits: their implications in elongation factor recognition and tRNA translocation. Stillman B. The Ribosome. 2001;67-75 Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (2001) The Ribosome , pp. 67-75
    • Frank, J.1    Agrawal, R.K.2
  • 3
    • 0032931788 scopus 로고    scopus 로고
    • Dynamics of translation on the ribosome: Molecular mechanics of translocation
    • Rodnina M.V., Savelsbergh A., Wintermeyer W. Dynamics of translation on the ribosome: molecular mechanics of translocation. FEMS Microbiol. Rev. 23:1999;317-333.
    • (1999) FEMS Microbiol. Rev. , vol.23 , pp. 317-333
    • Rodnina, M.V.1    Savelsbergh, A.2    Wintermeyer, W.3
  • 4
    • 0032488946 scopus 로고    scopus 로고
    • Molecular movement inside the translational engine
    • Wilson K.S., Noller H.F. Molecular movement inside the translational engine. Cell. 92:1998;337-349.
    • (1998) Cell , vol.92 , pp. 337-349
    • Wilson, K.S.1    Noller, H.F.2
  • 5
    • 0024458904 scopus 로고
    • Intermediate states in the movement of transfer RNA in the ribosome
    • Moazed D., Noller H.F. Intermediate states in the movement of transfer RNA in the ribosome. Nature. 342:1989;142-148.
    • (1989) Nature , vol.342 , pp. 142-148
    • Moazed, D.1    Noller, H.F.2
  • 7
    • 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. 406:2000;318-322.
    • (2000) Nature , vol.406 , pp. 318-322
    • Frank, J.1    Agrawal, R.K.2
  • 8
    • 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. 385:1997;37-41.
    • (1997) Nature , vol.385 , pp. 37-41
    • Rodnina, M.V.1    Savelsbergh, A.2    Katunin, V.I.3    Wintermeyer, W.4
  • 9
    • 0037108102 scopus 로고    scopus 로고
    • GTPase activation of elongation factors Tu and G on the ribosome
    • Mohr D., Wintermeyer W., Rodnina M.V. GTPase activation of elongation factors Tu and G on the ribosome. Biochemistry. 41:2002;12520-12528.
    • (2002) Biochemistry , vol.41 , pp. 12520-12528
    • Mohr, D.1    Wintermeyer, W.2    Rodnina, M.V.3
  • 10
    • 0021112383 scopus 로고
    • Chemical crosslinking of elongation factor G to the 23 S RNA in 70 S ribosomes from Escherichia coli
    • Skold S.E. Chemical crosslinking of elongation factor G to the 23 S RNA in 70 S ribosomes from Escherichia coli. Nucl. Acids Res. 11:1983;4923-4932.
    • (1983) Nucl. Acids Res. , vol.11 , pp. 4923-4932
    • Skold, S.E.1
  • 11
    • 0023722010 scopus 로고
    • Interaction of elongation factors EF-G and EF-Tu with a conserved loop in 23 S RNA
    • Moazed D., Robertson J.M., Noller H.F. Interaction of elongation factors EF-G and EF-Tu with a conserved loop in 23 S RNA. Nature. 334:1988;362-364.
    • (1988) Nature , vol.334 , pp. 362-364
    • Moazed, D.1    Robertson, J.M.2    Noller, H.F.3
  • 12
    • 0014961169 scopus 로고
    • Studies on translocation. VI. Thiostrepton prevents the formation of a ribosome-G factor-guanine nucleotide complex
    • Bodley J.W., Lin L., Highland J.H. Studies on translocation. VI. Thiostrepton prevents the formation of a ribosome-G factor-guanine nucleotide complex. Biochem. Biophys. Res. Commun. 41:1970;1406-1411.
    • (1970) Biochem. Biophys. Res. Commun. , vol.41 , pp. 1406-1411
    • Bodley, J.W.1    Lin, L.2    Highland, J.H.3
  • 14
    • 0023405923 scopus 로고
    • Evidence that the G2661 region of 23S rRNA is located at the ribosomal binding sites of both elongation factors
    • Hausner T.P., Atmadja J., Nierhaus K.H. Evidence that the G2661 region of 23S rRNA is located at the ribosomal binding sites of both elongation factors. Biochimie. 69:1987;911-923.
    • (1987) Biochimie , vol.69 , pp. 911-923
    • Hausner, T.P.1    Atmadja, J.2    Nierhaus, K.H.3
  • 15
    • 0024589101 scopus 로고
    • Effect of a-sarcin and ribosome-inactivating proteins on the interaction of elongation factors with ribosomes
    • Brigotti M., Rambelli F., Zamboni M., Montanaro L., Sperti S. Effect of a-sarcin and ribosome-inactivating proteins on the interaction of elongation factors with ribosomes. Biochem. J. 257:1989;723-727.
    • (1989) Biochem. J. , vol.257 , pp. 723-727
    • Brigotti, M.1    Rambelli, F.2    Zamboni, M.3    Montanaro, L.4    Sperti, S.5
  • 16
    • 0014940652 scopus 로고
    • Studies on translocation. IV. the hydrolysis of a single round of guanosine triphosphate in the presence of fusidic acid
    • Bodley J.W., Zieve F.J., Lin L. Studies on translocation. IV. The hydrolysis of a single round of guanosine triphosphate in the presence of fusidic acid. J. Biol. Chem. 245:1970;5662-5667.
    • (1970) J. Biol. Chem. , vol.245 , pp. 5662-5667
    • Bodley, J.W.1    Zieve, F.J.2    Lin, L.3
  • 17
    • 0032498266 scopus 로고    scopus 로고
    • Mapping the position of translational elongation factor EF-G in the ribosome by directed hydroxyl radical probing
    • Wilson K.S., Noller H.F. Mapping the position of translational elongation factor EF-G in the ribosome by directed hydroxyl radical probing. Cell. 92:1998;131-139.
    • (1998) Cell , vol.92 , pp. 131-139
    • Wilson, K.S.1    Noller, H.F.2
  • 18
    • 0032568584 scopus 로고    scopus 로고
    • Visualization of elongation factor G on the Escherichia coli 70S ribosome: The mechanism of translocation
    • Agrawal R.K., Penczek P., Grassucci R.A., Frank J. Visualization of elongation factor G on the Escherichia coli 70S ribosome: the mechanism of translocation. Proc. Natl Acad. Sci. USA. 95:1998;6134-6138.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 6134-6138
    • Agrawal, R.K.1    Penczek, P.2    Grassucci, R.A.3    Frank, J.4
  • 19
    • 0032982866 scopus 로고    scopus 로고
    • EF-G-dependent GTP hydrolysis induces translocation accompanied by large conformational changes in the 70S ribosome
    • Agrawal R.K., Heagle A.B., Penczek P., Grassucci R.A., Frank J. EF-G-dependent GTP hydrolysis induces translocation accompanied by large conformational changes in the 70S ribosome. Nature Struct. Biol. 6:1999;643-647.
    • (1999) Nature Struct. Biol. , vol.6 , pp. 643-647
    • Agrawal, R.K.1    Heagle, A.B.2    Penczek, P.3    Grassucci, R.A.4    Frank, J.5
  • 20
    • 0034603196 scopus 로고    scopus 로고
    • Large-scale movement of elongation factor G and extensive conformational change of the ribosome during translocation
    • Stark H., Rodnina M.V., Wieden H.J., van Heel M., Wintermeyer W. Large-scale movement of elongation factor G and extensive conformational change of the ribosome during translocation. Cell. 100:2000;301-309.
    • (2000) Cell , vol.100 , pp. 301-309
    • Stark, H.1    Rodnina, M.V.2    Wieden, H.J.3    Van Heel, M.4    Wintermeyer, W.5
  • 21
    • 0037319733 scopus 로고    scopus 로고
    • Electron microscopy of functional ribosome complexes
    • Frank J. Electron microscopy of functional ribosome complexes. Biopolymers. 68:2003;223-233.
    • (2003) Biopolymers , vol.68 , pp. 223-233
    • Frank, J.1
  • 22
    • 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. 17:1998;3478-3483.
    • (1998) EMBO J. , vol.17 , pp. 3478-3483
    • Joseph, S.1    Noller, H.F.2
  • 23
    • 0036301166 scopus 로고    scopus 로고
    • Initiation factor IF2, thiostrepton and micrococcin prevent the binding of elongation factor G to the Escherichia coli ribosome
    • Cameron D.M., Thompson J., March P.E., Dahlberg A.E. Initiation factor IF2, thiostrepton and micrococcin prevent the binding of elongation factor G to the Escherichia coli ribosome. J. Mol. Biol. 319:2002;27-35.
    • (2002) J. Mol. Biol. , vol.319 , pp. 27-35
    • Cameron, D.M.1    Thompson, J.2    March, P.E.3    Dahlberg, A.E.4
  • 24
    • 0037459218 scopus 로고    scopus 로고
    • Rapid kinetic analysis of EF-G-dependent mRNA translocation in the ribosome
    • Studer S.M., Feinberg J.S., Joseph S. Rapid kinetic analysis of EF-G-dependent mRNA translocation in the ribosome. J. Mol. Biol. 327:2003;369-381.
    • (2003) J. Mol. Biol. , vol.327 , pp. 369-381
    • Studer, S.M.1    Feinberg, J.S.2    Joseph, S.3
  • 26
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution
    • Ban N., Nissen P., Hansen J., Moore P.B., Steitz T.A. The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution. Science. 289:2000;905-920.
    • (2000) Science , vol.289 , pp. 905-920
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Moore, P.B.4    Steitz, T.A.5
  • 27
    • 0033553439 scopus 로고    scopus 로고
    • A detailed view of a ribosomal active site: The structure of the L11-RNA complex
    • Wimberly B.T., Guymon R., McCutcheon J.P., White S.W., Ramakrishnan V. A detailed view of a ribosomal active site: the structure of the L11-RNA complex. Cell. 97:1999;491-502.
    • (1999) Cell , vol.97 , pp. 491-502
    • Wimberly, B.T.1    Guymon, R.2    McCutcheon, J.P.3    White, S.W.4    Ramakrishnan, V.5
  • 28
    • 0027732617 scopus 로고
    • 4 and the antibiotic thiostrepton interact with overlapping regions of the 23 S rRNA backbone in the ribosomal GTPase centre
    • 4 and the antibiotic thiostrepton interact with overlapping regions of the 23 S rRNA backbone in the ribosomal GTPase centre. J. Mol. Biol. 234:1993;1013-1020.
    • (1993) J. Mol. Biol. , vol.234 , pp. 1013-1020
    • Rosendahl, G.1    Douthwaite, S.2
  • 30
    • 0034268836 scopus 로고    scopus 로고
    • Structure of functionally activated small ribosomal subunit at 3.3 Å resolution
    • Schluenzen F., Tocilj A., Zarivach R., Harms J., Gluehmann M., Janell D., et al. Structure of functionally activated small ribosomal subunit at 3.3 Å resolution. Cell. 102:2000;615-623.
    • (2000) Cell , vol.102 , pp. 615-623
    • Schluenzen, F.1    Tocilj, A.2    Zarivach, R.3    Harms, J.4    Gluehmann, M.5    Janell, D.6
  • 32
    • 0035943352 scopus 로고    scopus 로고
    • Localization of L11 protein on the ribosome and elucidation of its involvement in EF-G-dependent translocation
    • Agrawal R.K., Linde J., Sengupta J., Nierhaus K.H., Frank J. Localization of L11 protein on the ribosome and elucidation of its involvement in EF-G-dependent translocation. J. Mol. Biol. 311:2001;777-787.
    • (2001) J. Mol. Biol. , vol.311 , pp. 777-787
    • Agrawal, R.K.1    Linde, J.2    Sengupta, J.3    Nierhaus, K.H.4    Frank, J.5
  • 33
    • 0038275890 scopus 로고    scopus 로고
    • Study of the structural dynamics of the E. coli 70S ribosome using real-space refinement
    • Gao H., Sengupta J., Valle M., Korostelev A., Eswar N., Stagg S.M., et al. Study of the structural dynamics of the E. coli 70S ribosome using real-space refinement. Cell. 113:2003;789-801.
    • (2003) Cell , vol.113 , pp. 789-801
    • Gao, H.1    Sengupta, J.2    Valle, M.3    Korostelev, A.4    Eswar, N.5    Stagg, S.M.6
  • 34
    • 0027980558 scopus 로고
    • The crystal structure of elongation factor G complexed with GDP, at 2.7 Å resolution
    • Czworkowski J., Wang J., Steitz T.A., Moore P.B. The crystal structure of elongation factor G complexed with GDP, at 2.7 Å resolution. EMBO J. 13:1994;3661-3668.
    • (1994) EMBO J. , vol.13 , pp. 3661-3668
    • Czworkowski, J.1    Wang, J.2    Steitz, T.A.3    Moore, P.B.4
  • 36
  • 37
    • 0028355760 scopus 로고
    • The antibiotics micrococcin and thiostrepton interact directly with 23S rRNA nucleotides 1067A and 1095A
    • Rosendahl G., Douthwaite S. The antibiotics micrococcin and thiostrepton interact directly with 23S rRNA nucleotides 1067A and 1095A. Nucl. Acids Res. 22:1994;357-363.
    • (1994) Nucl. Acids Res. , vol.22 , pp. 357-363
    • Rosendahl, G.1    Douthwaite, S.2
  • 38
    • 0030774277 scopus 로고    scopus 로고
    • The ribosome-in-pieces: Binding of elongation factor EF-G to oligoribonucleotides that mimic the sarcin/ricin and thiostrepton domains of 23S ribosomal RNA
    • Munishkin A., Wool I.G. The ribosome-in-pieces: binding of elongation factor EF-G to oligoribonucleotides that mimic the sarcin/ricin and thiostrepton domains of 23S ribosomal RNA. Proc. Natl Acad. Sci. USA. 94:1997;12280-12284.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 12280-12284
    • Munishkin, A.1    Wool, I.G.2
  • 39
    • 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. 93:1996;4202-4206.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 4202-4206
    • Borowski, C.1    Rodnina, M.V.2    Wintermeyer, W.3
  • 40
    • 0033638447 scopus 로고    scopus 로고
    • Conformationally restricted elongation factor G retains GTPase activity but is inactive in translocation on the ribosome
    • Peske F., Matassova N.B., Savelsbergh A., Rodnina M.V., Wintermeyer W. Conformationally restricted elongation factor G retains GTPase activity but is inactive in translocation on the ribosome. Mol. Cell. 6:2000;501-505.
    • (2000) Mol. Cell , vol.6 , pp. 501-505
    • Peske, F.1    Matassova, N.B.2    Savelsbergh, A.3    Rodnina, M.V.4    Wintermeyer, W.5
  • 41
    • 0036303417 scopus 로고    scopus 로고
    • Crystal structure of the 30 S ribosomal subunit from Thermus thermophilus: Structure of the proteins and their interactions with 16S RNA
    • Brodersen D.E., Clemons W.M. Jr, Carter A.P., Wimberly B.T., Ramakrishnan V. Crystal structure of the 30 S ribosomal subunit from Thermus thermophilus: structure of the proteins and their interactions with 16S RNA. J. Mol. Biol. 316:2002;725-768.
    • (2002) J. Mol. Biol. , vol.316 , pp. 725-768
    • Brodersen, D.E.1    Clemons Jr., W.M.2    Carter, A.P.3    Wimberly, B.T.4    Ramakrishnan, V.5
  • 42
    • 0034909325 scopus 로고    scopus 로고
    • Evolution of a molecular switch: Universal bacterial GTPases regulate ribosome function
    • Caldon C.E., Yoong P., March P.E. Evolution of a molecular switch: universal bacterial GTPases regulate ribosome function. Mol. Microbiol. 41:2001;289-297.
    • (2001) Mol. Microbiol. , vol.41 , pp. 289-297
    • Caldon, C.E.1    Yoong, P.2    March, P.E.3
  • 43
    • 0034903857 scopus 로고    scopus 로고
    • Initiation factor IF-2 binds to the a-sarcin loop and helix 89 of Escherichia coli 23S ribosomal RNA
    • La Teana A., Gualerzi C.O., Dahlberg A.E. Initiation factor IF-2 binds to the a-sarcin loop and helix 89 of Escherichia coli 23S ribosomal RNA. RNA. 7:2001;1173-1179.
    • (2001) RNA , vol.7 , pp. 1173-1179
    • La Teana, A.1    Gualerzi, C.O.2    Dahlberg, A.E.3
  • 44
  • 46
    • 0002477677 scopus 로고
    • Isolation and analysis of ribosomes from prokaryotes, eukaryotes, and organelles
    • G. Spedding. Oxford: Oxford University Press
    • Spedding G. Isolation and analysis of ribosomes from prokaryotes, eukaryotes, and organelles. Spedding G. Ribosomes and Protein Synthesis: A Practical Approach. 1990;1-27 Oxford University Press, Oxford.
    • (1990) Ribosomes and Protein Synthesis: A Practical Approach , pp. 1-27
    • Spedding, G.1
  • 47
    • 0031455374 scopus 로고    scopus 로고
    • Substrate recognition by the leucyl/phenylalanyl-tRNA-protein transferase. Conservation within the enzyme family and localization to the trypsin-resistant domain
    • Ichetovkin I.E., Abramochkin G., Shrader T.E. Substrate recognition by the leucyl/phenylalanyl-tRNA-protein transferase. Conservation within the enzyme family and localization to the trypsin-resistant domain. J. Biol. Chem. 272:1997;33009-33014.
    • (1997) J. Biol. Chem. , vol.272 , pp. 33009-33014
    • Ichetovkin, I.E.1    Abramochkin, G.2    Shrader, T.E.3
  • 48
    • 0024252185 scopus 로고
    • Extension inhibition analysis of translation initiation complexes
    • Hartz D., McPheeters D.S., Traut R., Gold L. Extension inhibition analysis of translation initiation complexes. Methods Enzymol. 164:1988;419-425.
    • (1988) Methods Enzymol. , vol.164 , pp. 419-425
    • Hartz, D.1    McPheeters, D.S.2    Traut, R.3    Gold, L.4
  • 49
    • 0024241761 scopus 로고
    • Structural analysis of RNA using chemical and enzymatic probing monitored by primer extension
    • Stern S., Moazed D., Noller H.F. Structural analysis of RNA using chemical and enzymatic probing monitored by primer extension. Methods Enzymol. 164:1988;481-489.
    • (1988) Methods Enzymol. , vol.164 , pp. 481-489
    • Stern, S.1    Moazed, D.2    Noller, H.F.3
  • 50
    • 0032544035 scopus 로고    scopus 로고
    • DNA strand breaking by the hydroxyl radical is governed by the accessible surface areas of the hydrogen atoms of the DNA backbone
    • Balasubramanian B., Pogozelski W.K., Tullius T.D. DNA strand breaking by the hydroxyl radical is governed by the accessible surface areas of the hydrogen atoms of the DNA backbone. Proc. Natl Acad. Sci. USA. 95:1998;9738-9743.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 9738-9743
    • Balasubramanian, B.1    Pogozelski, W.K.2    Tullius, T.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.